ID AFP4_GADMO Reviewed; 125 AA. AC Q56TU0; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 22-SEP-2009, entry version 20. DE RecName: Full=Type-4 ice-structuring protein; DE AltName: Full=Antifreeze protein type IV; DE Flags: Precursor; OS Gadus morhua (Atlantic cod). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Gadus. OX NCBI_TaxID=8049; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Ovary; RA Goetz F.W., Norberg B., Duman J.; RT "A cod antifreeze protein."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point (By CC similarity). CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY584595; AAT95404.1; -; mRNA. DR HOVERGEN; Q56TU0; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 2: Evidence at transcript level; KW Antifreeze protein; Secreted; Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 125 Type-4 ice-structuring protein. FT /FTId=PRO_0000042948. SQ SEQUENCE 125 AA; 13991 MW; 4ED7D330E8D66FF8 CRC64; MKYTLIAAIV VLALAQGTLA VEQSPELEKM AQFFEGMKTE LMATVQKVSE SLQSQTIIED GRTQLEPIMT QIQEHLAPLA TSVQEKVTPL AEDMQQKLKP YVDEFQSELE SVLRKLLDQA KAITQ // ID AFP4_MYOOC Reviewed; 128 AA. AC P80961; O73699; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 18-OCT-2001, sequence version 2. DT 22-SEP-2009, entry version 44. DE RecName: Full=Type-4 ice-structuring protein LS-12; DE Short=ISP LS-12; DE AltName: Full=Antifreeze protein LS-12; DE Flags: Precursor; OS Myoxocephalus octodecimspinosis (Longhorn sculpin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes; OC Cottoidei; Cottidae; Myoxocephalus. OX NCBI_TaxID=68557; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=98201665; PubMed=9540788; DOI=10.1016/S0167-4838(97)00197-0; RA Zhao Z., Deng G., Lui Q., Laursen R.A.; RT "Cloning and sequencing of cDNA encoding the LS-12 antifreeze protein RT in the longhorn sculpin, Myoxocephalus octodecimspinosis."; RL Biochim. Biophys. Acta 1382:177-180(1998). RN [2] RP PROTEIN SEQUENCE OF 21-128. RC TISSUE=Blood; RX MEDLINE=97165956; PubMed=9013849; DOI=10.1016/S0014-5793(96)01466-4; RA Deng G., Andrews D.W., Laursen R.A.; RT "Amino acid sequence of a new type of antifreeze protein, from the RT longhorn sculpin Myoxocephalus octodecimspinosis."; RL FEBS Lett. 402:17-20(1997). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF026525; AAC27986.1; -; mRNA. DR PIR; A59010; A59010. DR HOVERGEN; P80961; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008289; F:lipid binding; IEA:InterPro. DR GO; GO:0006869; P:lipid transport; IEA:InterPro. DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR000074; ApoA1_A4_E. DR Pfam; PF01442; Apolipoprotein; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; KW Pyrrolidone carboxylic acid; Secreted; Signal. FT SIGNAL 1 20 FT CHAIN 21 128 Type-4 ice-structuring protein LS-12. FT /FTId=PRO_0000001698. FT MOD_RES 21 21 Pyrrolidone carboxylic acid. SQ SEQUENCE 128 AA; 14378 MW; FC9688BD6E32F55D CRC64; MKFSLVATIV LLALAQGSFA QGAADLESLG QYFEEMKTKL IQDMTEIIRS QDLANQAQAF VEDKKTQLQP LVAQIQEQMK TVATNVEEQI RPLTANVQAH LQPQIDNFQK QMEAIIKKLT DQTMAIEN // ID AFP4_PAROL Reviewed; 124 AA. AC Q8JI37; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 22-SEP-2009, entry version 22. DE RecName: Full=Type-4 ice-structuring protein; DE AltName: Full=Antifreeze protein type IV; DE Flags: Precursor; OS Paralichthys olivaceus (Japanese flounder). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Paralichthyidae; Paralichthys. OX NCBI_TaxID=8255; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Lee J., Song Y.; RT "Antifreeze protein gene of Japanese flounder similar to antifreeze RT protein type IV of Longhorn sculpin."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point (By CC similarity). CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF384676; AAM46175.1; -; Genomic_DNA. DR HOVERGEN; Q8JI37; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Antifreeze protein; Pyrrolidone carboxylic acid; Secreted; Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 124 Type-4 ice-structuring protein. FT /FTId=PRO_0000042949. FT MOD_RES 21 21 Pyrrolidone carboxylic acid (By FT similarity). SQ SEQUENCE 124 AA; 13946 MW; EA84868080E761F5 CRC64; MKFSLIAAVA LLALAQGSFA QDAADLEKIT QYFENLKNKM TEDVTAFLTN QDVANQAQTF MQERKTQLEP LATQIQEQLR AAATKFEEHI TPLAANVQPV VENFQQQMEA LVQKLMEKTR SISN // ID ANP11_MACAM Reviewed; 62 AA. AC P19613; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 52. DE RecName: Full=Ice-structuring protein SP2(HPLC 11); DE Short=ISP SP2(HPLC 11); DE AltName: Full=Antifreeze protein SP2(HPLC 11); OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; I31075; I31075. DR HSSP; P19608; 1OPS. DR SMR; P19613; 1-62. DR HOVERGEN; P19613; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 62 Ice-structuring protein SP2(HPLC 11). FT /FTId=PRO_0000155156. FT DOMAIN 1 60 AFP-like. FT SITE 6 6 Important for ice-binding (By FT similarity). FT SITE 11 11 Important for ice-binding (By FT similarity). FT SITE 15 15 Important for ice-binding (By FT similarity). FT SITE 41 41 Important for ice-binding (By FT similarity). SQ SEQUENCE 62 AA; 6585 MW; 3F8B94CDE6977E89 CRC64; SVVATQLIPI NTALTPAMME GKVTNPIGIP FAEMSQIVGK QVNRIVAKGQ TLMPNMVKTY AA // ID ANP12_MACAM Reviewed; 66 AA. AC P19614; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 64. DE RecName: Full=Type-3 ice-structuring protein HPLC 12; DE AltName: Full=ISP type III HPLC 12; DE AltName: Full=Antifreeze protein QAE(HPLC 12); OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). RN [2] RP NOMENCLATURE. RX PubMed=12050776; RA Clarke C.J., Buckley S.L., Lindner N.; RT "Ice structuring proteins - a new name for antifreeze proteins."; RL Cryo Lett. 23:89-92(2002). RN [3] RP STRUCTURE BY NMR. RX MEDLINE=97094988; PubMed=8939756; DOI=10.1016/S0969-2126(96)00140-2; RA Soennichsen F.D., Deluca C.I., Davies P.L., Sykes B.D.; RT "Refined solution structure of type III antifreeze protein: RT hydrophobic groups may be involved in the energetics of the protein- RT ice interaction."; RL Structure 4:1325-1337(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS). RX MEDLINE=97078758; PubMed=8918883; DOI=10.1038/384285a0; RA Jia Z., Deluca C.I., Chao H., Davies P.L.; RT "Structural basis for the binding of a globular antifreeze protein to RT ice."; RL Nature 384:285-288(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF MUTANTS. RX MEDLINE=98139965; PubMed=9466928; DOI=10.1006/jmbi.1997.1482; RA Deluca C.I., Davies P.L., Ye Q., Jia Z.; RT "The effects of steric mutations on the structure of type III RT antifreeze protein and its interaction with ice."; RL J. Mol. Biol. 275:515-525(1998). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RA Antson A.A., Lewis S., Roper D.I., Smith D.J., Hubbard R.E.; RL Submitted (OCT-1996) to the PDB data bank. RN [7] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS). RX MEDLINE=99223507; PubMed=10207002; DOI=10.1074/jbc.274.17.11842; RA Graether S.P., Deluca C.I., Baardsnes J., Hill G.A., Davies P.L., RA Jia Z.; RT "Quantitative and qualitative analysis of type III antifreeze protein RT structure and function."; RL J. Biol. Chem. 274:11842-11847(1999). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A30839; A30839. DR PDB; 1AME; X-ray; 1.65 A; A=1-63. DR PDB; 1B7I; X-ray; 1.65 A; A=1-63. DR PDB; 1B7J; X-ray; 1.65 A; A=1-63. DR PDB; 1B7K; X-ray; 2.50 A; A=1-63. DR PDB; 1EKL; X-ray; 1.65 A; A=1-63. DR PDB; 1GZI; X-ray; 1.80 A; A=1-63. DR PDB; 1HG7; X-ray; 1.15 A; A=1-63. DR PDB; 1JAB; X-ray; 1.65 A; A=1-63. DR PDB; 1KDE; NMR; -; A=1-63. DR PDB; 1KDF; NMR; -; A=1-63. DR PDB; 1MSI; X-ray; 1.25 A; A=2-63. DR PDB; 1MSJ; X-ray; 2.30 A; A=1-63. DR PDB; 2AME; X-ray; 2.00 A; A=1-63. DR PDB; 2JIA; X-ray; 1.60 A; A=1-63. DR PDB; 2MSI; X-ray; 1.90 A; A=2-63. DR PDB; 2MSJ; X-ray; 1.90 A; A=1-63. DR PDB; 2SPG; X-ray; 1.75 A; A=1-63. DR PDB; 3AME; X-ray; 2.30 A; A=1-63. DR PDB; 3MSI; X-ray; 1.43 A; A=2-63. DR PDB; 4AME; X-ray; 2.05 A; A=1-63. DR PDB; 4MSI; X-ray; 1.60 A; A=2-63. DR PDB; 5MSI; X-ray; 1.60 A; A=2-63. DR PDB; 6AME; X-ray; 2.10 A; A=1-63. DR PDB; 6MSI; X-ray; 1.65 A; A=2-63. DR PDB; 7AME; X-ray; 1.70 A; A=1-63. DR PDB; 7MSI; X-ray; 1.70 A; A=2-63. DR PDB; 8AME; X-ray; 1.90 A; A=1-63. DR PDB; 8MSI; X-ray; 2.60 A; A=1-63. DR PDB; 9AME; X-ray; 1.80 A; A=1-63. DR PDB; 9MSI; X-ray; 2.60 A; A=1-63. DR PDBsum; 1AME; -. DR PDBsum; 1B7I; -. DR PDBsum; 1B7J; -. DR PDBsum; 1B7K; -. DR PDBsum; 1EKL; -. DR PDBsum; 1GZI; -. DR PDBsum; 1HG7; -. DR PDBsum; 1JAB; -. DR PDBsum; 1KDE; -. DR PDBsum; 1KDF; -. DR PDBsum; 1MSI; -. DR PDBsum; 1MSJ; -. DR PDBsum; 2AME; -. DR PDBsum; 2JIA; -. DR PDBsum; 2MSI; -. DR PDBsum; 2MSJ; -. DR PDBsum; 2SPG; -. DR PDBsum; 3AME; -. DR PDBsum; 3MSI; -. DR PDBsum; 4AME; -. DR PDBsum; 4MSI; -. DR PDBsum; 5MSI; -. DR PDBsum; 6AME; -. DR PDBsum; 6MSI; -. DR PDBsum; 7AME; -. DR PDBsum; 7MSI; -. DR PDBsum; 8AME; -. DR PDBsum; 8MSI; -. DR PDBsum; 9AME; -. DR PDBsum; 9MSI; -. DR HOVERGEN; P19614; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 66 Type-3 ice-structuring protein HPLC 12. FT /FTId=PRO_0000155160. FT DOMAIN 4 63 AFP-like. FT SITE 9 9 Important for ice-binding. FT SITE 14 14 Important for ice-binding. FT SITE 18 18 Important for ice-binding. FT SITE 44 44 Important for ice-binding. FT STRAND 4 9 FT HELIX 19 21 FT STRAND 22 25 FT HELIX 34 36 FT HELIX 37 40 FT STRAND 44 47 FT HELIX 57 59 SQ SEQUENCE 66 AA; 7027 MW; B6121A9902ED89F9 CRC64; NQASVVANQL IPINTALTLV MMRSEVVTPV GIPAEDIPRL VSMQVNRAVP LGTTLMPDMV KGYPPA // ID ANP1_ANALU Reviewed; 88 AA. AC P12416; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 22-SEP-2009, entry version 55. DE RecName: Full=Type-3 ice-structuring protein 1.9; DE AltName: Full=ISP 3; DE AltName: Full=Antifreeze protein type III; DE Flags: Precursor; OS Anarhichas lupus (Atlantic wolffish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Anarhichadidae; Anarhichas. OX NCBI_TaxID=8204; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89127205; PubMed=2851724; RA Scott G.K., Hayes P.H., Fletcher G.L., Davies P.L.; RT "Wolffish antifreeze protein genes are primarily organized as tandem RT repeats that each contain two genes in inverted orientation."; RL Mol. Cell. Biol. 8:3670-3675(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22125; AAA74890.1; -; Genomic_DNA. DR PIR; A30238; A30238. DR HSSP; P19608; 1OPS. DR SMR; P12416; 23-86. DR HOVERGEN; P12416; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 3: Inferred from homology; KW Antifreeze protein; Secreted; Signal. FT SIGNAL 1 23 FT CHAIN 24 88 Type-3 ice-structuring protein 1.9. FT /FTId=PRO_0000001696. FT DOMAIN 25 84 AFP-like. FT SITE 30 30 Important for ice-binding (By FT similarity). FT SITE 35 35 Important for ice-binding (By FT similarity). FT SITE 39 39 Important for ice-binding (By FT similarity). FT SITE 65 65 Important for ice-binding (By FT similarity). SQ SEQUENCE 88 AA; 9438 MW; 738EB9E62B3F347C CRC64; MKSAILTGLL FVLLCVDHLS SASQSVVATQ LIPINTALTP IMMKGQVVNP AGIPFAEMSQ IVGKQVNRPV AKDETLMPNM VKTYRAAK // ID ANP1_LYCPO Reviewed; 66 AA. AC P24028; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 22-SEP-2009, entry version 49. DE RecName: Full=Ice-structuring protein LP; DE Short=ISP LP; DE AltName: Full=Antifreeze protein LP; OS Lycodes polaris (Canadian eelpout). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Lycodinae; Lycodes. OX NCBI_TaxID=8197; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=88000728; PubMed=3477289; DOI=10.1016/0167-4838(87)90021-5; RA Schrag J.D., Cheng C.-H.C., Panico M., Morris H.R., Devries A.L.; RT "Primary and secondary structure of antifreeze peptides from arctic RT and antarctic zoarcid fishes."; RL Biochim. Biophys. Acta 915:357-370(1987). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S07150; FDFILC. DR HSSP; P19614; 9AME. DR SMR; P24028; 1-64. DR HOVERGEN; P24028; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 66 Ice-structuring protein LP. FT /FTId=PRO_0000155154. FT DOMAIN 4 63 AFP-like. FT SITE 9 9 Important for ice-binding (By FT similarity). FT SITE 14 14 Important for ice-binding (By FT similarity). FT SITE 18 18 Important for ice-binding (By FT similarity). FT SITE 44 44 Important for ice-binding (By FT similarity). SQ SEQUENCE 66 AA; 6982 MW; 6F06E38A329767EC CRC64; NKASVVANQL IPINTALTLV MMRAEVVTPA GIPAEDIPRL VGLQVNRAVL IGTTLMPDMV KGYAPQ // ID ANP1_MACAM Reviewed; 64 AA. AC P19608; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 58. DE RecName: Full=Ice-structuring protein SP2(HPLC 1); DE Short=ISP SP2(HPLC 1); DE AltName: Full=Antifreeze protein SP2(HPLC 1); OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; D31075; D31075. DR PDB; 1OPS; X-ray; 2.00 A; A=1-64. DR PDBsum; 1OPS; -. DR HOVERGEN; P19608; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 64 Ice-structuring protein SP2(HPLC 1). FT /FTId=PRO_0000155155. FT DOMAIN 3 62 AFP-like. FT SITE 8 8 Important for ice-binding (By FT similarity). FT SITE 13 13 Important for ice-binding (By FT similarity). FT SITE 17 17 Important for ice-binding (By FT similarity). FT SITE 43 43 Important for ice-binding (By FT similarity). FT STRAND 3 8 FT HELIX 18 20 FT STRAND 21 24 FT HELIX 33 38 FT TURN 39 41 FT STRAND 43 46 FT HELIX 56 58 FT TURN 60 63 SQ SEQUENCE 64 AA; 6775 MW; DC6F90A2119FE0B0 CRC64; SQSVVATQLI PMNTALTPVM MEGKVTNPIG IPFAEMSQIV GKQVNTPVAK GQTIMPNMVK TYAA // ID ANP1_PACBR Reviewed; 63 AA. AC P12100; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 22-SEP-2009, entry version 55. DE RecName: Full=Ice-structuring protein AB1; DE Short=ISP AB1; DE AltName: Full=Antifreeze peptide AB1; OS Pachycara brachycephalum (Antarctic eelpout) (Austrolycichthys OS brachycephalus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Lycodinae; Pachycara. OX NCBI_TaxID=36221; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=89323219; PubMed=2752054; DOI=10.1016/0167-4838(89)90135-0; RA Cheng C.-H.C., Devries A.L.; RT "Structures of antifreeze peptides from the antarctic eel pout, RT Austrolycicthys brachycephalus."; RL Biochim. Biophys. Acta 997:55-64(1989). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S04973; S04973. DR HSSP; P35753; 1C8A. DR SMR; P12100; 2-63. DR HOVERGEN; P12100; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 63 Ice-structuring protein AB1. FT /FTId=PRO_0000155149. FT DOMAIN 3 62 AFP-like. FT SITE 8 8 Important for ice-binding (By FT similarity). FT SITE 13 13 Important for ice-binding (By FT similarity). FT SITE 17 17 Important for ice-binding (By FT similarity). FT SITE 43 43 Important for ice-binding (By FT similarity). SQ SEQUENCE 63 AA; 6846 MW; AC84FD14247193B4 CRC64; TKSVVASQLI PINTALTPAM MKAKEVSPKG IPAEEMSKIV GMQVNRAVNL DETLMPDMVK TYQ // ID ANP1_RHIDE Reviewed; 64 AA. AC P35751; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 22-SEP-2009, entry version 56. DE RecName: Full=Ice-structuring protein RD1; DE Short=ISP RD1; DE AltName: Full=Antifreeze peptide RD1; OS Rhigophila dearborni (Antarctic eelpout) (Lycodichthys dearborni). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Lycodinae; Lycodichthys. OX NCBI_TaxID=8201; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=95210308; PubMed=7696304; DOI=10.1016/0167-4838(94)00205-U; RA Wang X., Devries A.L., Cheng C.-H.C.; RT "Antifreeze peptide heterogeneity in an antarctic eel pout includes an RT unusually large major variant comprised of two 7 kDa type III AFPs RT linked in tandem."; RL Biochim. Biophys. Acta 1247:163-172(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (0.62 ANGSTROMS). RX PubMed=12547803; RA Ko T.-P., Robinson H., Gao Y.-G., Cheng C.H.-C., DeVries A.L., RA Wang A.H.-J.; RT "The refined crystal structure of an eel pout type III antifreeze RT protein RD1 at 0.62-A resolution reveals structuRAl microheterogeneity RT of protein and solvation."; RL Biophys. J. 84:1228-1237(2003). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S53512; S53512. DR PDB; 1UCS; X-ray; 0.62 A; A=1-64. DR PDBsum; 1UCS; -. DR HOVERGEN; P35751; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 64 Ice-structuring protein RD1. FT /FTId=PRO_0000155151. FT DOMAIN 4 63 AFP-like. FT SITE 9 9 Important for ice-binding (By FT similarity). FT SITE 14 14 Important for ice-binding (By FT similarity). FT SITE 18 18 Important for ice-binding (By FT similarity). FT SITE 44 44 Important for ice-binding (By FT similarity). FT STRAND 4 9 FT HELIX 19 21 FT STRAND 22 25 FT HELIX 34 36 FT HELIX 37 40 FT STRAND 44 47 FT HELIX 57 59 SQ SEQUENCE 64 AA; 6906 MW; 154C6BE62D913192 CRC64; NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPKL VGMQVNRAVP LGTTLMPDMV KNYE // ID ANP1C_MACAM Reviewed; 87 AA. AC P07457; P19610; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 22-SEP-2009, entry version 64. DE RecName: Full=Ice-structuring protein SP1-C; DE Short=ISP SP1-C; DE AltName: Full=Antifreeze protein SP1-C; DE Flags: Precursor; OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=86033715; PubMed=3840475; RA Li X.-M., Trinh K.-Y., Hew C.-L., Buettner B., Baenziger J., RA Davies P.L.; RT "Structure of an antifreeze polypeptide and its precursor from the RT ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 260:12904-12909(1985). RN [2] RP PROTEIN SEQUENCE OF 23-86. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M11790; AAA49347.1; -; mRNA. DR PIR; A24081; FDFICP. DR HSSP; P19608; 1OPS. DR SMR; P07457; 22-85. DR HOVERGEN; P07457; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; KW Pyrrolidone carboxylic acid; Secreted; Signal. FT SIGNAL 1 22 FT CHAIN 23 87 Ice-structuring protein SP1-C. FT /FTId=PRO_0000001691. FT DOMAIN 24 83 AFP-like. FT SITE 29 29 Important for ice-binding (By FT similarity). FT SITE 34 34 Important for ice-binding (By FT similarity). FT SITE 38 38 Important for ice-binding (By FT similarity). FT SITE 64 64 Important for ice-binding (By FT similarity). FT MOD_RES 23 23 Pyrrolidone carboxylic acid. SQ SEQUENCE 87 AA; 9229 MW; 58D79961968D87B8 CRC64; MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPINTALTPA MMEGKVTNPI GIPFAEMSQI VGKQVNTPVA KGQTLMPNMV KTYVAGK // ID ANP2_ANALU Reviewed; 88 AA. AC P12417; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 22-SEP-2009, entry version 54. DE RecName: Full=Type-3 ice-structuring protein 1.5; DE AltName: Full=ISP 3; DE AltName: Full=Antifreeze protein type III; DE Flags: Precursor; OS Anarhichas lupus (Atlantic wolffish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Anarhichadidae; Anarhichas. OX NCBI_TaxID=8204; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89127205; PubMed=2851724; RA Scott G.K., Hayes P.H., Fletcher G.L., Davies P.L.; RT "Wolffish antifreeze protein genes are primarily organized as tandem RT repeats that each contain two genes in inverted orientation."; RL Mol. Cell. Biol. 8:3670-3675(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M22125; AAA74891.1; -; Genomic_DNA. DR HSSP; P19608; 1OPS. DR SMR; P12417; 23-86. DR HOVERGEN; P12417; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 3: Inferred from homology; KW Antifreeze protein; Secreted; Signal. FT SIGNAL 1 23 FT CHAIN 24 88 Type-3 ice-structuring protein 1.5. FT /FTId=PRO_0000001697. FT DOMAIN 25 84 AFP-like. FT SITE 30 30 Important for ice-binding (By FT similarity). FT SITE 35 35 Important for ice-binding (By FT similarity). FT SITE 39 39 Important for ice-binding (By FT similarity). FT SITE 65 65 Important for ice-binding (By FT similarity). FT CONFLICT 24 24 Q -> QQ (in Ref. 1; AAA74891). SQ SEQUENCE 88 AA; 9430 MW; 72CAFCFA474E85CC CRC64; MKSAILTGLL FVLLCVDHMS SASQSVVATQ LIPINTALTP IMMKGQVVNP AGIPFAEMSQ IVGKQVNRAV AKDETLMPNM VKTYRAAK // ID ANP2_PACBR Reviewed; 63 AA. AC P12101; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 22-SEP-2009, entry version 55. DE RecName: Full=Ice-structuring protein AB2; DE Short=ISP AB2; DE AltName: Full=Antifreeze peptide AB2; OS Pachycara brachycephalum (Antarctic eelpout) (Austrolycichthys OS brachycephalus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Lycodinae; Pachycara. OX NCBI_TaxID=36221; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=89323219; PubMed=2752054; DOI=10.1016/0167-4838(89)90135-0; RA Cheng C.-H.C., Devries A.L.; RT "Structures of antifreeze peptides from the antarctic eel pout, RT Austrolycicthys brachycephalus."; RL Biochim. Biophys. Acta 997:55-64(1989). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S04974; S04974. DR HSSP; P35753; 1C8A. DR SMR; P12101; 2-63. DR HOVERGEN; P12101; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 63 Ice-structuring protein AB2. FT /FTId=PRO_0000155150. FT DOMAIN 3 62 AFP-like. FT SITE 8 8 Important for ice-binding (By FT similarity). FT SITE 13 13 Important for ice-binding (By FT similarity). FT SITE 17 17 Important for ice-binding (By FT similarity). FT SITE 43 43 Important for ice-binding (By FT similarity). SQ SEQUENCE 63 AA; 7001 MW; A1E7F954598DD061 CRC64; TKSVVANQLI PINTALTLVM MKAEEVSPKG IPAEEIPRLV GMQVNRAVYL DETLMPDMVK NYE // ID ANP2_RHIDE Reviewed; 64 AA. AC P12102; P35752; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 22-SEP-2009, entry version 56. DE RecName: Full=Ice-structuring protein RD2; DE Short=ISP RD2; DE AltName: Full=Antifreeze peptide RD2; OS Rhigophila dearborni (Antarctic eelpout) (Lycodichthys dearborni). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Lycodinae; Lycodichthys. OX NCBI_TaxID=8201; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=95210308; PubMed=7696304; DOI=10.1016/0167-4838(94)00205-U; RA Wang X., Devries A.L., Cheng C.-H.C.; RT "Antifreeze peptide heterogeneity in an antarctic eel pout includes an RT unusually large major variant comprised of two 7 kDa type III AFPs RT linked in tandem."; RL Biochim. Biophys. Acta 1247:163-172(1995). RN [2] RP PROTEIN SEQUENCE. RX MEDLINE=88000728; PubMed=3477289; DOI=10.1016/0167-4838(87)90021-5; RA Schrag J.D., Cheng C.-H.C., Panico M., Morris H.R., Devries A.L.; RT "Primary and secondary structure of antifreeze peptides from arctic RT and antarctic zoarcid fishes."; RL Biochim. Biophys. Acta 915:357-370(1987). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S08561; FDFIRE. DR HSSP; P35751; 1UCS. DR SMR; P12102; 1-64. DR HOVERGEN; P12102; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 64 Ice-structuring protein RD2. FT /FTId=PRO_0000155152. FT DOMAIN 4 63 AFP-like. FT SITE 9 9 Important for ice-binding (By FT similarity). FT SITE 14 14 Important for ice-binding (By FT similarity). FT SITE 18 18 Important for ice-binding (By FT similarity). FT SITE 44 44 Important for ice-binding (By FT similarity). SQ SEQUENCE 64 AA; 6934 MW; 41EBAF6F2C812084 CRC64; NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEDIPRI IGMQVNRAVP LGTTLMPDMV KNYE // ID ANP3_MACAM Reviewed; 91 AA. AC P19606; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 58. DE RecName: Full=Ice-structuring protein lambda OP-3; DE Short=ISP lambda OP-3; DE AltName: Full=Antifreeze protein lambda OP-3; DE Flags: Precursor; OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J03923; AAA49348.1; -; Genomic_DNA. DR PIR; B30839; B30839. DR HSSP; P19614; 1HG7. DR SMR; P19606; 21-84. DR HOVERGEN; P19606; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 3: Inferred from homology; KW Antifreeze protein; Secreted; Signal. FT SIGNAL 1 22 By similarity. FT CHAIN 23 91 Ice-structuring protein lambda OP-3. FT /FTId=PRO_0000001694. FT DOMAIN 25 84 AFP-like. FT SITE 30 30 Important for ice-binding (By FT similarity). FT SITE 35 35 Important for ice-binding (By FT similarity). FT SITE 39 39 Important for ice-binding (By FT similarity). FT SITE 65 65 Important for ice-binding (By FT similarity). SQ SEQUENCE 91 AA; 9912 MW; B85C9037F969F7CE CRC64; MKSVILTGLL FVLLCVDHMS SANQSVVATQ LIPINTALTL VMMTTRVIYP TGIPAEDIPR LVSMQVNQAV PMGTTLMPDM VKFYCLCAPK N // ID ANP3_MYOSC Reviewed; 33 AA. AC P04367; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 22-SEP-2009, entry version 52. DE RecName: Full=Ice-structuring protein SS-3; DE Short=ISP SS-3; DE AltName: Full=Antifreeze peptide SS-3; OS Myoxocephalus scorpius (Shorthorn sculpin) (Daddy sculpin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes; OC Cottoidei; Cottidae; Myoxocephalus. OX NCBI_TaxID=8097; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=85285003; PubMed=4029130; RX DOI=10.1111/j.1432-1033.1985.tb09081.x; RA Hew C.-L., Joshi S., Wang N.-C., Kao M.H., Ananthanarayanan V.S.; RT "Structures of shorthorn sculpin antifreeze polypeptides."; RL Eur. J. Biochem. 151:167-172(1985). RN [2] RP PROTEIN SEQUENCE. RX MEDLINE=96223980; PubMed=8626748; DOI=10.1074/jbc.271.8.4106; RA Gong Z., Ewart K.V., Hu Z., Fletcher G.L., Hew C.-L.; RT "Skin antifreeze protein genes of the winter flounder, Pleuronectes RT americanus, encode distinct and active polypeptides without the RT secretory signal and prosequences."; RL J. Biol. Chem. 271:4106-4112(1996). RN [3] RP STRUCTURE BY NMR. RX PubMed=15697223; DOI=10.1021/bi047782j; RA Kwan A.H., Fairley K., Anderberg P.I., Liew C.W., Harding M.M., RA Mackay J.P.; RT "Solution structure of a recombinant type I sculpin antifreeze RT protein."; RL Biochemistry 44:1980-1988(2005). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A05162; A05162. DR PDB; 1Y03; NMR; -; A=1-33. DR PDB; 1Y04; NMR; -; A=1-33. DR PDBsum; 1Y03; -. DR PDBsum; 1Y04; -. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW 3D-structure; Antifreeze protein; Direct protein sequencing; Repeat. FT CHAIN 1 33 Ice-structuring protein SS-3. FT /FTId=PRO_0000155144. FT HELIX 3 8 FT HELIX 10 31 SQ SEQUENCE 33 AA; 2939 MW; 8B74CC4C06A1208A CRC64; MNAPARAAAK TAADALAAAK KTAADAAAAA AAA // ID ANP3_PAGBO Reviewed; 31 AA. AC P02732; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 22-SEP-2009, entry version 41. DE RecName: Full=Ice-structuring glycoprotein 3; DE Short=ISGP 3; DE AltName: Full=Antifreeze glycoprotein 3; DE Flags: Fragments; OS Pagothenia borchgrevinki (Bald rockcod) (Trematomus borchgrevinki). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; OC Notothenioidei; Nototheniidae; Pagothenia. OX NCBI_TaxID=8213; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=71104882; PubMed=5542001; RA Devries A.L., Vandenheede J., Feeney R.E.; RT "Primary structure of freezing point-depressing glycoproteins."; RL J. Biol. Chem. 246:305-308(1971). RN [2] RP PROTEIN SEQUENCE. RX MEDLINE=72056127; PubMed=5006918; DOI=10.1016/0006-291X(72)90633-X; RA Lin Y., Duman J.G., Devries A.L.; RT "Studies on the structure and activity of low molecular weight RT glycoproteins from an antarctic fish."; RL Biochem. Biophys. Res. Commun. 46:87-92(1972). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. This CC fish lives in antarctic waters where it experiences water CC temperatures near -1.9 degrees Celsius. Its blood has a freezing CC point of about -2.0 degrees Celsius, and 30% of the freezing-point CC depression is due mainly to the 3 major high molecular weight CC glycoproteins in the plasma. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: O-linked glycans consist of Gal-GalNAc disaccharides. The CC three proteins may differ only in the number of repeating units of CC -Ala-Ala-Thr-. CC -!- MISCELLANEOUS: The two small glycopeptides are present in a much CC higher concentration (5 times by weight) than the HMW CC glycoproteins but produce only a small depression effect. The CC exact physiological role of the small glycopeptides is not known. CC -!- MISCELLANEOUS: The three major glycoproteins (3, 4, and 5) have CC the same N-terminal sequence, A-A-T-A-A-T, and C-terminal Ala. CC Each protein is composed only of Ala and Thr residues in a ratio CC of 2:1 and arranged in the repeating sequence -A-A-T-. CC -!- MISCELLANEOUS: The small glycopeptides 7 and 8 appear to contain CC 20 and 14 residues, respectively, and to have the same N-terminal CC sequence and C-terminal residue as the 3 major proteins. However, CC each has 2 Pro residues (instead of 1 of the Ala in each of 2 CC repeating units). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A03191; A03191. DR HOVERGEN; P02732; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Glycoprotein; Repeat; KW Secreted. FT CHAIN 1 31 Ice-structuring glycoprotein 3. FT /FTId=PRO_0000155143. FT CARBOHYD 3 3 O-linked (GalNAc...). FT CARBOHYD 6 6 O-linked (GalNAc...). FT CARBOHYD 9 9 O-linked (GalNAc...). FT CARBOHYD 12 12 O-linked (GalNAc...). FT CARBOHYD 15 15 O-linked (GalNAc...). FT CARBOHYD 18 18 O-linked (GalNAc...). FT CARBOHYD 21 21 O-linked (GalNAc...). FT CARBOHYD 24 24 O-linked (GalNAc...). FT CARBOHYD 27 27 O-linked (GalNAc...). FT CARBOHYD 30 30 O-linked (GalNAc...). FT NON_CONS 30 31 SQ SEQUENCE 31 AA; 2522 MW; 613109D78109D7D0 CRC64; AATAATAATA ATAATAATAA TAATAATAAT A // ID ANP3_PSEAM Reviewed; 37 AA. AC P02733; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 22-SEP-2009, entry version 41. DE RecName: Full=Ice-structuring protein 3; DE Short=ISP 3; DE AltName: Full=Antifreeze peptide 3; OS Pseudopleuronectes americanus (Winter flounder) (Pleuronectes OS americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes. OX NCBI_TaxID=8265; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=78060969; PubMed=588591; DOI=10.1016/0005-2795(77)90395-6; RA Devries A.L., Lin Y.; RT "Structure of a peptide antifreeze and mechanism of adsorption to RT ice."; RL Biochim. Biophys. Acta 495:388-392(1977). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A03192; FDFL3W. DR GO; GO:0050825; F:ice binding; IEA:InterPro. DR GO; GO:0042309; P:homoiothermy; IEA:InterPro. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR000104; Antifreeze_1. DR PRINTS; PR00308; ANTIFREEZEI. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Repeat. FT CHAIN 1 37 Ice-structuring protein 3. FT /FTId=PRO_0000155148. SQ SEQUENCE 37 AA; 3144 MW; 46AA951A962DECA9 CRC64; DTASDAAAAA ALTAABAAAA AKLTABBAAA AAAATAA // ID ANP3_RHIDE Reviewed; 134 AA. AC P35753; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 22-SEP-2009, entry version 59. DE RecName: Full=Ice-structuring protein RD3; DE Short=ISP RD3; DE AltName: Full=Antifreeze peptide RD3; OS Rhigophila dearborni (Antarctic eelpout) (Lycodichthys dearborni). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Lycodinae; Lycodichthys. OX NCBI_TaxID=8201; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=95210308; PubMed=7696304; DOI=10.1016/0167-4838(94)00205-U; RA Wang X., Devries A.L., Cheng C.-H.C.; RT "Antifreeze peptide heterogeneity in an antarctic eel pout includes an RT unusually large major variant comprised of two 7 kDa type III AFPs RT linked in tandem."; RL Biochim. Biophys. Acta 1247:163-172(1995). RN [2] RP STRUCTURE BY NMR OF 1-73. RX MEDLINE=99353969; PubMed=10423534; RA Miura K., Ohgiya S., Hoshino T., Nemoto N., Odaira M., Nitta K., RA Tsuda S.; RT "Determination of the solution structure of the N-domain plus linker RT of antarctic eel pout antifreeze protein RD3."; RL J. Biochem. 126:387-394(1999). RN [3] RP STRUCTURE BY NMR. RX PubMed=11010977; DOI=10.1074/jbc.M007902200; RA Miura K., Ohgiya S., Hoshino T., Nemoto N., Suetake T., Miura A., RA Spyracopoulos L., Kondo H., Tsuda S.; RT "NMR analysis of type III antifreeze protein intramolecular dimer. RT Structural basis for enhanced activity."; RL J. Biol. Chem. 276:1304-1310(2001). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 2 AFP-like domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S53514; S53514. DR PDB; 1C89; NMR; -; A=1-134. DR PDB; 1C8A; NMR; -; A=1-134. DR PDB; 3NLA; NMR; -; A=1-73. DR PDB; 3RDN; NMR; -; A=1-73. DR PDBsum; 1C89; -. DR PDBsum; 1C8A; -. DR PDBsum; 3NLA; -. DR PDBsum; 3RDN; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 2. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 2. DR PROSITE; PS50844; AFP_LIKE; 2. PE 1: Evidence at protein level; KW 3D-structure; Antifreeze protein; Direct protein sequencing; Repeat; KW Secreted. FT CHAIN 1 134 Ice-structuring protein RD3. FT /FTId=PRO_0000155153. FT DOMAIN 4 63 AFP-like 1. FT DOMAIN 74 133 AFP-like 2. FT REGION 65 70 Linker. FT SITE 9 9 Important for ice-binding (By FT similarity). FT SITE 14 14 Important for ice-binding (By FT similarity). FT SITE 18 18 Important for ice-binding (By FT similarity). FT SITE 44 44 Important for ice-binding (By FT similarity). FT SITE 79 79 Important for ice-binding (By FT similarity). FT SITE 84 84 Important for ice-binding (By FT similarity). FT SITE 88 88 Important for ice-binding (By FT similarity). FT SITE 114 114 Important for ice-binding (By FT similarity). FT STRAND 4 9 FT TURN 19 21 FT STRAND 22 25 FT STRAND 32 34 FT HELIX 37 40 FT TURN 57 59 FT STRAND 71 79 FT TURN 89 91 FT STRAND 93 96 FT STRAND 103 106 FT HELIX 107 110 FT STRAND 121 124 FT TURN 127 129 SQ SEQUENCE 134 AA; 14480 MW; F7F208BF3E2CAA54 CRC64; NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPNL VGMQVNRAVP LGTTLMPDMV KNYEDGTTSP GLKSVVANQL IPINTALTLV MMKAEEVSPK GIPSEEISKL VGMQVNRAVY LDQTLMPDMV KNYE // ID ANP4_MACAM Reviewed; 63 AA. AC P19609; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 52. DE RecName: Full=Ice-structuring protein SP1(HPLC 4); DE Short=ISP SP1(HPLC 4); DE AltName: Full=Antifreeze protein SP1(HPLC 4); OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; E31075; E31075. DR HSSP; P19608; 1OPS. DR SMR; P19609; 1-63. DR HOVERGEN; P19609; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 63 Ice-structuring protein SP1(HPLC 4). FT /FTId=PRO_0000155157. FT DOMAIN 2 61 AFP-like. FT SITE 7 7 Important for ice-binding (By FT similarity). FT SITE 12 12 Important for ice-binding (By FT similarity). FT SITE 16 16 Important for ice-binding (By FT similarity). FT SITE 42 42 Important for ice-binding (By FT similarity). SQ SEQUENCE 63 AA; 6642 MW; 3FEFE507C6972FD8 CRC64; QSVVATQLIP INTALTPAMM EGKVTNPIGI PFAEMSQIVG KQVNTPVAKG QTIMPNMVKT YAA // ID ANP4_PSEAM Reviewed; 85 AA. AC P02734; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 22-SEP-2009, entry version 47. DE RecName: Full=Ice-structuring protein 4; DE Short=ISP 4; DE AltName: Full=Antifreeze peptide 4; DE Flags: Precursor; OS Pseudopleuronectes americanus (Winter flounder) (Pleuronectes OS americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes. OX NCBI_TaxID=8265; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=81247379; PubMed=6265915; DOI=10.1073/pnas.78.5.2825; RA Lin Y., Gross J.K.; RT "Molecular cloning and characterization of winter flounder antifreeze RT cDNA."; RL Proc. Natl. Acad. Sci. U.S.A. 78:2825-2829(1981). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J00930; AAA49467.1; -; mRNA. DR PIR; A03193; FDFL4W. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050825; F:ice binding; IEA:InterPro. DR GO; GO:0042309; P:homoiothermy; IEA:InterPro. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR000104; Antifreeze_1. DR PRINTS; PR00308; ANTIFREEZEI. PE 3: Inferred from homology; KW Antifreeze protein; Repeat; Secreted; Signal. FT SIGNAL 1 21 FT CHAIN 22 85 Ice-structuring protein 4. FT /FTId=PRO_0000001684. SQ SEQUENCE 85 AA; 7215 MW; 8E62E1D2B44117BC CRC64; MRITEANPDP DAKAVPAAAA PSTASDAAAA AAATAATAAA AAAATAATAA AAAAATAATA AKAAALTAAN AAAAAAATAA AAARG // ID ANP5_MACAM Reviewed; 87 AA. AC P19607; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 56. DE RecName: Full=Ice-structuring protein lambda OP-5; DE Short=ISP lambda OP-5; DE AltName: Full=Antifreeze protein lambda OP-5; DE Flags: Precursor; OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J03924; AAA49346.1; -; Genomic_DNA. DR PIR; C31075; C31075. DR HSSP; P19608; 1OPS. DR SMR; P19607; 22-85. DR HOVERGEN; P19607; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 3: Inferred from homology; KW Antifreeze protein; Secreted; Signal. FT SIGNAL 1 21 By similarity. FT CHAIN 22 87 Ice-structuring protein lambda OP-5. FT /FTId=PRO_0000001695. FT DOMAIN 24 83 AFP-like. FT SITE 29 29 Important for ice-binding (By FT similarity). FT SITE 34 34 Important for ice-binding (By FT similarity). FT SITE 38 38 Important for ice-binding (By FT similarity). FT SITE 64 64 Important for ice-binding (By FT similarity). SQ SEQUENCE 87 AA; 9229 MW; B5615B2E868D87AB CRC64; MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPINTALTPV MMEGKVTNPI GIPFAEMSQI VGKQVNTPVA KGQTLMPNMV KTYAAGK // ID ANP5_MYOAE Reviewed; 33 AA. AC P20421; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 35. DE RecName: Full=Ice-structuring protein GS-5; DE Short=ISP GS-5; DE AltName: Full=Antifreeze peptide GS-5; OS Myoxocephalus aenaeus (Grubby sculpin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes; OC Cottoidei; Cottidae; Myoxocephalus. OX NCBI_TaxID=8096; RN [1] RP PROTEIN SEQUENCE. RA Chakrabartty A., Hew C.-L., Shears M., Fletcher G.; RT "Primary structures of the alanine-rich antifreeze polypeptides from RT grubby sculpin, Myoxocephalus aenaeus."; RL Can. J. Zool. 66:403-408(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S06417; FDFI5G. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Repeat. FT CHAIN 1 33 Ice-structuring protein GS-5. FT /FTId=PRO_0000155146. FT MOD_RES 1 1 Blocked amino end (Met). SQ SEQUENCE 33 AA; 2980 MW; 7F2ACC56B70A2080 CRC64; MDAPAIAAAK TAADALAAAK KTAADAAAAA AKP // ID ANP7_ELEGR Reviewed; 19 AA. AC P11920; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 22-SEP-2009, entry version 33. DE RecName: Full=Ice-structuring glycoprotein 7R; DE Short=ISGP 7R; DE AltName: Full=Antifreeze glycoprotein 7R; OS Eleginus gracilis (Saffron cod). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Eleginus. OX NCBI_TaxID=8047; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=86196057; PubMed=3700395; RA Burcham T.S., Osuga D.T., Rao B.N.N., Bush C.A., Feeney R.E.; RT "Purification and primary sequences of the major arginine-containing RT antifreeze glycopeptides from the fish Eleginus gracilis."; RL J. Biol. Chem. 261:6384-6389(1986). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: O-glycosylated; contains disaccharide galactose-N- CC acetylgalactosamine attached to threonines (By similarity). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; B25213; B25213. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Glycoprotein; Secreted. FT PEPTIDE 1 19 Ice-structuring glycoprotein 7R. FT /FTId=PRO_0000155141. SQ SEQUENCE 19 AA; 1656 MW; E290F8FEF1FD9324 CRC64; AATAATPATA ATPATAARA // ID ANP7_MACAM Reviewed; 64 AA. AC P19611; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 52. DE RecName: Full=Ice-structuring protein SP4(HPLC 7); DE Short=ISP SP4(HPLC 7); DE AltName: Full=Antifreeze protein SP4(HPLC 7); OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; G31075; G31075. DR HSSP; P19608; 1OPS. DR SMR; P19611; 1-64. DR HOVERGEN; P19611; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 64 Ice-structuring protein SP4(HPLC 7). FT /FTId=PRO_0000155158. FT DOMAIN 3 62 AFP-like. FT SITE 8 8 Important for ice-binding (By FT similarity). FT SITE 13 13 Important for ice-binding (By FT similarity). FT SITE 17 17 Important for ice-binding (By FT similarity). FT SITE 43 43 Important for ice-binding (By FT similarity). SQ SEQUENCE 64 AA; 6846 MW; FD2E27DB328C423A CRC64; SQSVVATRLI PMNTALTPAM MEGKVTNPIG IPFAEMSQIV GKQVNRIVAK GQTLMPNMVK TYAA // ID ANP8_ELEGR Reviewed; 16 AA. AC P11921; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 22-SEP-2009, entry version 33. DE RecName: Full=Ice-structuring glycoprotein 8R; DE Short=ISGP 8R; DE AltName: Full=Antifreeze glycoprotein 8R; OS Eleginus gracilis (Saffron cod). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Eleginus. OX NCBI_TaxID=8047; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=86196057; PubMed=3700395; RA Burcham T.S., Osuga D.T., Rao B.N.N., Bush C.A., Feeney R.E.; RT "Purification and primary sequences of the major arginine-containing RT antifreeze glycopeptides from the fish Eleginus gracilis."; RL J. Biol. Chem. 261:6384-6389(1986). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: O-glycosylated; contains disaccharide galactose-N- CC acetylgalactosamine attached to threonines (By similarity). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A25213; A25213. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Glycoprotein; Secreted. FT PEPTIDE 1 16 Ice-structuring glycoprotein 8R. FT /FTId=PRO_0000155142. SQ SEQUENCE 16 AA; 1413 MW; 8EF45D9324E88994 CRC64; AATAATPATA ATPARA // ID ANP8_MYOAE Reviewed; 40 AA. AC P20617; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 35. DE RecName: Full=Ice-structuring protein GS-8; DE Short=ISP GS-8; DE AltName: Full=Antifreeze peptide GS-8; OS Myoxocephalus aenaeus (Grubby sculpin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes; OC Cottoidei; Cottidae; Myoxocephalus. OX NCBI_TaxID=8096; RN [1] RP PROTEIN SEQUENCE. RA Chakrabartty A., Hew C.-L., Shears M., Fletcher G.; RT "Primary structures of the alanine-rich antifreeze polypeptides from RT grubby sculpin, Myoxocephalus aenaeus."; RL Can. J. Zool. 66:403-408(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S07046; FDFI8G. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Repeat. FT CHAIN 1 40 Ice-structuring protein GS-8. FT /FTId=PRO_0000155147. FT MOD_RES 1 1 Blocked amino end (Met). SQ SEQUENCE 40 AA; 3579 MW; 32F50EE243C2AD11 CRC64; MDGETPAQKA ARLAAAAAAL AAKTAADAAA KAAAIAAAAA // ID ANP8_MYOSC Reviewed; 45 AA. AC P04368; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 22-SEP-2009, entry version 42. DE RecName: Full=Ice-structuring protein SS-8; DE Short=ISP SS-8; DE AltName: Full=Antifreeze peptide SS-8; OS Myoxocephalus scorpius (Shorthorn sculpin) (Daddy sculpin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes; OC Cottoidei; Cottidae; Myoxocephalus. OX NCBI_TaxID=8097; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=85285003; PubMed=4029130; RX DOI=10.1111/j.1432-1033.1985.tb09081.x; RA Hew C.-L., Joshi S., Wang N.-C., Kao M.H., Ananthanarayanan V.S.; RT "Structures of shorthorn sculpin antifreeze polypeptides."; RL Eur. J. Biochem. 151:167-172(1985). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A05163; A05163. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Repeat. FT CHAIN 1 45 Ice-structuring protein SS-8. FT /FTId=PRO_0000155145. FT REPEAT 9 21 FT REPEAT 22 33 FT REPEAT 34 45 FT MOD_RES 1 1 Blocked amino end (Met). SQ SEQUENCE 45 AA; 4007 MW; 260C0BCC663B6878 CRC64; MNGETPAQKA ARLAAAAALA AKTAADAAAK AAAKAAAIAA AAASA // ID ANP9_MACAM Reviewed; 64 AA. AC P19612; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 52. DE RecName: Full=Ice-structuring protein SP3(HPLC 9); DE Short=ISP SP3(HPLC 9); DE AltName: Full=Antifreeze protein SP3(HPLC 9); OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; H31075; H31075. DR HSSP; P19608; 1OPS. DR SMR; P19612; 1-64. DR HOVERGEN; P19612; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Secreted. FT CHAIN 1 64 Ice-structuring protein SP3(HPLC 9). FT /FTId=PRO_0000155159. FT DOMAIN 3 62 AFP-like. FT SITE 8 8 Important for ice-binding (By FT similarity). FT SITE 13 13 Important for ice-binding (By FT similarity). FT SITE 17 17 Important for ice-binding (By FT similarity). FT SITE 43 43 Important for ice-binding (By FT similarity). SQ SEQUENCE 64 AA; 6818 MW; FE2D27D8318C423A CRC64; SQSVVATQLI PMNTALTPAM MEGKVTNPIG IPFAEMSQIV GKQVNRIVAK GQTLMPNMVK TYAA // ID ANP_LIMFE Reviewed; 97 AA. AC P09031; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 22-SEP-2009, entry version 44. DE RecName: Full=Ice-structuring protein; DE Short=ISP; DE AltName: Full=Antifreeze protein; DE Short=AFP; DE Flags: Precursor; OS Limanda ferruginea (Yellowtail flounder). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Pleuronectidae; Pleuronectinae; Limanda. OX NCBI_TaxID=8258; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=88029483; PubMed=3665937; RX DOI=10.1111/j.1432-1033.1987.tb13462.x; RA Scott G.K., Davies P.L., Shears M.A., Fletcher G.L.; RT "Structural variations in the alanine-rich antifreeze proteins of the RT pleuronectinae."; RL Eur. J. Biochem. 168:629-633(1987). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X06356; CAA29655.1; -; mRNA. DR PIR; S02376; S02376. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050825; F:ice binding; IEA:InterPro. DR GO; GO:0042309; P:homoiothermy; IEA:InterPro. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR000104; Antifreeze_1. DR PRINTS; PR00308; ANTIFREEZEI. PE 3: Inferred from homology; KW Antifreeze protein; Repeat; Secreted; Signal. FT SIGNAL 1 23 FT PROPEP 24 48 Removed by a dipeptidylpeptidase FT (Probable). FT /FTId=PRO_0000001682. FT CHAIN 49 97 Ice-structuring protein. FT /FTId=PRO_0000001683. SQ SEQUENCE 97 AA; 8865 MW; 62AD582DF8E459B6 CRC64; MALSLFTVGQ LIFLFWTLRI TEANPDPAAK AAPAAVADPA AAAAAAVADT ASDAAAAAAA TAAAAAKAAA DTAAAAAKAA ADTAAAAAEA AAATARG // ID ANP_NOTCO Reviewed; 790 AA. AC P24856; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 22-SEP-2009, entry version 58. DE RecName: Full=Ice-structuring glycoprotein; DE Short=ISGP; DE AltName: Full=Antifreeze glycopeptide polyprotein; DE Short=AFGP polyprotein; DE Contains: DE RecName: Full=AFGP7; DE AltName: Full=AFGP 7; DE Contains: DE RecName: Full=AFGP8; DE AltName: Full=AFGP 8; DE Contains: DE RecName: Full=AFGP8-like; DE Flags: Precursor; Fragment; GN Name=afgp8; OS Notothenia coriiceps neglecta (Black rockcod) (Yellowbelly rockcod). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; OC Notothenioidei; Nototheniidae; Notothenia. OX NCBI_TaxID=8209; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Testis; RX MEDLINE=91067687; PubMed=2251271; DOI=10.1073/pnas.87.23.9265; RA Hsiao K.-C., Cheng C.-H.C., Fernandes I.E., Detrich H.W. III, RA Devries A.L.; RT "An antifreeze glycopeptide gene from the antarctic cod Notothenia RT coriiceps neglecta encodes a polyprotein of high peptide copy RT number."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9265-9269(1990). RN [2] RP SEQUENCE REVISION TO N-TERMINUS AND 457. RA Cheng C.-H.C.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Synthesized by the liver and secreted into the CC blood from which they become distributed to almost the entire CC extracellular space. CC -!- DOMAIN: Contains 44 copies of AFGP8 and two copies of AFGP7. CC -!- PTM: O-glycosylated; contains disaccharide galactose-N- CC acetylgalactosamine attached to threonines in AFGP8 and AFGP7. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Cool news - Issue 5 of CC December 2000; CC URL="http://www.expasy.org/spotlight/back_issues/sptlt005.shtml"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M55000; AAA49392.2; -; Genomic_DNA. DR PIR; A38420; A38420. DR HOVERGEN; P24856; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Glycoprotein; Repeat; KW Secreted. FT PROPEP <1 5 FT /FTId=PRO_0000001634. FT CHAIN 6 790 Ice-structuring glycoprotein. FT /FTId=PRO_0000001635. FT PEPTIDE 6 19 AFGP8. FT /FTId=PRO_0000001636. FT PEPTIDE 23 36 AFGP8. FT /FTId=PRO_0000001637. FT PEPTIDE 40 53 AFGP8. FT /FTId=PRO_0000001638. FT PEPTIDE 57 70 AFGP8. FT /FTId=PRO_0000001639. FT PEPTIDE 74 87 AFGP8. FT /FTId=PRO_0000001640. FT PEPTIDE 91 104 AFGP8. FT /FTId=PRO_0000001641. FT PEPTIDE 108 121 AFGP8. FT /FTId=PRO_0000001642. FT PEPTIDE 125 138 AFGP8. FT /FTId=PRO_0000001643. FT PEPTIDE 142 155 AFGP8. FT /FTId=PRO_0000001644. FT PEPTIDE 159 172 AFGP8. FT /FTId=PRO_0000001645. FT PEPTIDE 176 189 AFGP8. FT /FTId=PRO_0000001646. FT PEPTIDE 193 206 AFGP8. FT /FTId=PRO_0000001647. FT PEPTIDE 210 223 AFGP8. FT /FTId=PRO_0000001648. FT PEPTIDE 227 240 AFGP8. FT /FTId=PRO_0000001649. FT PEPTIDE 244 257 AFGP8. FT /FTId=PRO_0000001650. FT PEPTIDE 261 274 AFGP8. FT /FTId=PRO_0000001651. FT PEPTIDE 278 291 AFGP8. FT /FTId=PRO_0000001652. FT PEPTIDE 295 308 AFGP8. FT /FTId=PRO_0000001653. FT PEPTIDE 312 325 AFGP8. FT /FTId=PRO_0000001654. FT PEPTIDE 329 342 AFGP8. FT /FTId=PRO_0000001655. FT PEPTIDE 346 359 AFGP8. FT /FTId=PRO_0000001656. FT PEPTIDE 363 376 AFGP8. FT /FTId=PRO_0000001657. FT PEPTIDE 380 393 AFGP8. FT /FTId=PRO_0000001658. FT PEPTIDE 397 410 AFGP8. FT /FTId=PRO_0000001659. FT PEPTIDE 414 427 AFGP8. FT /FTId=PRO_0000001660. FT PEPTIDE 431 444 AFGP8. FT /FTId=PRO_0000001661. FT PEPTIDE 448 461 AFGP8. FT /FTId=PRO_0000001662. FT PEPTIDE 465 478 AFGP8. FT /FTId=PRO_0000001663. FT PEPTIDE 482 495 AFGP8. FT /FTId=PRO_0000001664. FT PEPTIDE 499 512 AFGP8. FT /FTId=PRO_0000001665. FT PEPTIDE 516 529 AFGP8. FT /FTId=PRO_0000001666. FT PEPTIDE 533 546 AFGP8. FT /FTId=PRO_0000001667. FT PEPTIDE 550 563 AFGP8. FT /FTId=PRO_0000001668. FT PEPTIDE 567 580 AFGP8. FT /FTId=PRO_0000001669. FT PEPTIDE 584 597 AFGP8. FT /FTId=PRO_0000001670. FT PEPTIDE 601 614 AFGP8. FT /FTId=PRO_0000001671. FT PEPTIDE 618 631 AFGP8. FT /FTId=PRO_0000001672. FT PEPTIDE 635 648 AFGP8. FT /FTId=PRO_0000001673. FT PEPTIDE 652 665 AFGP8. FT /FTId=PRO_0000001674. FT PEPTIDE 669 682 AFGP8. FT /FTId=PRO_0000001675. FT PEPTIDE 686 699 AFGP8. FT /FTId=PRO_0000001676. FT PEPTIDE 703 716 AFGP8. FT /FTId=PRO_0000001677. FT PEPTIDE 720 736 AFGP7. FT /FTId=PRO_0000001678. FT PEPTIDE 740 756 AFGP7. FT /FTId=PRO_0000001679. FT PEPTIDE 760 773 AFGP8. FT /FTId=PRO_0000001680. FT PEPTIDE 777 790 AFGP8-like. FT /FTId=PRO_0000001681. FT NON_TER 1 1 SQ SEQUENCE 790 AA; 71267 MW; 4C7CCCADC48FE902 CRC64; VTAAPAATAA TAATPATAAL NFAATAATPA TPATPALIFA ATAATAATPA TAALNFAATA ATPATAATPA LIFAAAAATA ATPATAALNF AATAATPATA ATPALIFAAT AATAATPATP AFHFAATAAT PATAATPALI FAATAATAAT PATPAFHFAA TAATPATAAT PALIFAATAA TAATPATAAL NFAATAATPA TAATPALIFA ATAATAATPA TAALNFAATA ATAATPATAA CNFAATAATP ATAATPALIF AATAATAATP ATAACNFAAT AATPATAATP ALIFAATAAT AATPATAALN FAATAATPAT AATPALIFAA TAATAATPAT AALNFAATAA TPATAATPAL IFAATAATAA TPATAALNFA ATAATAATPA TPAFNFAATA ATPATAATPA LIFAATAATA ATPATAALNF AATAATPATA ATPALIFAAT AATAATPATA ALHFAATAAT AATPATAALN FAATAATPAT AATPALIFAA TAATAATPAT AAFNFAATAA TAATPATAAL NFAATAATPA TAATPALIFA ATAATAATPA TAALNFAATA ATPATAATPA LIFAATAATA ATPATPAFHF AATAATPATA ATPALIFAAT AATAATPATA ALNFAATAAT AATPATAALN FAATAATPAT AATPALIFAA TAATAATPAT AALNFAATAA TPATAATPAL IFAATAATAA TPATAAFNFA ATAATAATPA TAATPALIFA ATAATAATPA TPATPALIFA ATAATAATPA TPALNFAATA ATAATTAARG // ID ANPA_PSEAM Reviewed; 82 AA. AC P04002; Q7SIC4; DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-1986, sequence version 1. DT 28-JUL-2009, entry version 67. DE RecName: Full=Ice-structuring protein A; DE Short=ISP A; DE AltName: Full=Antifreeze protein A; DE AltName: Full=HPLC6; DE Flags: Precursor; OS Pseudopleuronectes americanus (Winter flounder) (Pleuronectes OS americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes. OX NCBI_TaxID=8265; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-70. RX MEDLINE=82197490; PubMed=6952188; DOI=10.1073/pnas.79.2.335; RA Davies P.L., Roach A.H., Hew C.-L.; RT "DNA sequence coding for an antifreeze protein precursor from winter RT flounder."; RL Proc. Natl. Acad. Sci. U.S.A. 79:335-339(1982). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84264559; PubMed=6086629; RA Davies P.L., Hough C., Scott G.K., Ng N.F.L., White B.N., Hew C.-L.; RT "Antifreeze protein genes of the winter flounder."; RL J. Biol. Chem. 259:9241-9247(1984). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88259236; PubMed=3133486; DOI=10.1007/BF02099727; RA Scott G.K., Davies P.L., Kao M.H., Fletcher G.L.; RT "Differential amplification of antifreeze protein genes in the RT pleuronectinae."; RL J. Mol. Evol. 27:29-35(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-36. RC TISSUE=Testis; RX MEDLINE=92209995; PubMed=1555765; DOI=10.1016/0378-1119(92)90372-V; RA Davies P.L.; RT "Conservation of antifreeze protein-encoding genes in tandem RT repeats."; RL Gene 112:163-170(1992). RN [5] RP PROTEIN SEQUENCE OF 24-28, AND AMIDATION. RC TISSUE=Liver; RX PubMed=3769927; DOI=10.1111/j.1432-1033.1986.tb09966.x; RA Hew C.-L., Wang N.-C., Yan S., Cai H., Sclater A., Fletcher G.L.; RT "Biosynthesis of antifreeze polypeptides in the winter flounder. RT Characterization and seasonal occurrence of precursor polypeptides."; RL Eur. J. Biochem. 160:267-272(1986). RN [6] RP 3D-STRUCTURE MODELING OF 45-81. RX MEDLINE=92148833; PubMed=1738160; DOI=10.1016/0022-2836(92)90666-8; RA Chou K.-C.; RT "Energy-optimized structure of antifreeze protein and its binding RT mechanism."; RL J. Mol. Biol. 223:509-517(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 45-81, AND AMIDATION AT RP ARG-81. RX MEDLINE=95281060; PubMed=7760940; DOI=10.1038/375427a0; RA Sicheri F., Yang D.S.C.; RT "Ice-binding structure and mechanism of an antifreeze protein from RT winter flounder."; RL Nature 375:427-431(1995). RN [8] RP STRUCTURE BY NMR OF 45-81, AMIDATION AT ARG-81, AND MUTAGENESIS OF RP THR-46; ALA-51; ALA-55; THR-57; THR-68; ALA-73; ALA-77 AND THR-79. RX MEDLINE=21845977; PubMed=11856360; RX DOI=10.1046/j.1432-1033.2002.02766.x; RA Liepinsh E., Otting G., Harding M.M., Ward L.G., Mackay J.P., RA Haymet A.D.; RT "Solution structure of a hydrophobic analogue of the winter flounder RT antifreeze protein."; RL Eur. J. Biochem. 269:1259-1266(2002). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- INDUCTION: By winter conditions, at least in part by water CC temperatures of below 8 degrees Celsius. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L00138; AAB59964.1; -; Genomic_DNA. DR EMBL; L29178; AAB59964.1; JOINED; Genomic_DNA. DR EMBL; X07506; CAA30389.1; -; Genomic_DNA. DR EMBL; M62414; AAA49469.1; -; Genomic_DNA. DR EMBL; M62416; AAA49471.1; -; Genomic_DNA. DR EMBL; M62417; AAA49472.1; -; Genomic_DNA. DR PIR; A05161; A05161. DR PIR; JS0704; FDFLAW. DR PIR; JS0706; JS0706. DR PIR; S02326; S02326. DR PDB; 1ATF; Model; -; A=45-81. DR PDB; 1J5B; NMR; -; A=47-81. DR PDB; 1WFA; X-ray; 1.70 A; A/B=45-81. DR PDB; 1WFB; X-ray; 1.50 A; A/B=45-81. DR PDBsum; 1ATF; -. DR PDBsum; 1J5B; -. DR PDBsum; 1WFA; -. DR PDBsum; 1WFB; -. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0050825; F:ice binding; TAS:UniProtKB. DR GO; GO:0042309; P:homoiothermy; IEP:UniProtKB. DR GO; GO:0050826; P:response to freezing; IEP:UniProtKB. DR InterPro; IPR000104; Antifreeze_1. DR PRINTS; PR00308; ANTIFREEZEI. PE 1: Evidence at protein level; KW 3D-structure; Amidation; Antifreeze protein; KW Direct protein sequencing; Polymorphism; Repeat; Secreted; Signal. FT SIGNAL 1 23 FT PROPEP 24 44 Removed by a dipeptidylpeptidase FT (Probable). FT /FTId=PRO_0000001685. FT CHAIN 45 81 Ice-structuring protein A. FT /FTId=PRO_0000001686. FT COMPBIAS 28 80 Ala-rich. FT MOD_RES 81 81 Arginine amide. FT VARIANT 36 36 A -> V. FT VARIANT 70 70 A -> D. FT MUTAGEN 46 46 T->V: No significant effect on 3D FT structure; when associated with K-51; E- FT 55; V-57; V-68; K-73; E-77 and V-79. FT MUTAGEN 51 51 A->K: No significant effect on 3D FT structure; when associated with V-46; E- FT 55; V-57; V-68; K-73; E-77 and V-79. FT MUTAGEN 55 55 A->E: No significant effect on 3D FT structure; when associated with V-46; K- FT 51; V-57; V-68; K-73; E-77 and V-79. FT MUTAGEN 57 57 T->V: No significant effect on 3D FT structure; when associated with V-46; K- FT 51; E-55; V-68; K-73; E-77 and V-79. FT MUTAGEN 68 68 T->V: No significant effect on 3D FT structure; when associated with V-46; K- FT 51; E-55; V-57; K-73; E-77 and V-79. FT MUTAGEN 73 73 A->K: No significant effect on 3D FT structure; when associated with V-46; K- FT 51; E-55; V-57; V-68; E-77 and V-79. FT MUTAGEN 77 77 A->E: No significant effect on 3D FT structure; when associated with V-46; K- FT 51; E-55; V-57; V-68; K-73 and V-79. FT MUTAGEN 79 79 T->V: No significant effect on 3D FT structure; when associated with V-46; K- FT 51; E-55; V-57; V-68; K-73 and E-77. FT CONFLICT 24 24 S -> R (in Ref. 3; CAA30389 and 4; FT AAA49469). FT HELIX 46 79 SQ SEQUENCE 82 AA; 7711 MW; C2AE7B74C0D46CC1 CRC64; MALSLFTVGQ LIFLFWTMRI TEASPDPAAK AAPAAAAAPA AAAPDTASDA AAAAALTAAN AKAAAELTAA NAAAAAAATA RG // ID ANPB_PSEAM Reviewed; 82 AA. AC Q99013; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-JUL-2009, entry version 36. DE RecName: Full=Ice-structuring protein B; DE Short=ISP B; DE AltName: Full=Antifreeze protein B; DE AltName: Full=HPLC8; DE Flags: Precursor; OS Pseudopleuronectes americanus (Winter flounder) (Pleuronectes OS americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes. OX NCBI_TaxID=8265; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=92209995; PubMed=1555765; DOI=10.1016/0378-1119(92)90372-V; RA Davies P.L.; RT "Conservation of antifreeze protein-encoding genes in tandem RT repeats."; RL Gene 112:163-170(1992). RN [2] RP PROTEIN SEQUENCE OF 24-28, AND AMIDATION. RC TISSUE=Liver; RX PubMed=3769927; DOI=10.1111/j.1432-1033.1986.tb09966.x; RA Hew C.-L., Wang N.-C., Yan S., Cai H., Sclater A., Fletcher G.L.; RT "Biosynthesis of antifreeze polypeptides in the winter flounder. RT Characterization and seasonal occurrence of precursor polypeptides."; RL Eur. J. Biochem. 160:267-272(1986). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- INDUCTION: By winter conditions, at least in part by water CC temperatures of below 8 degrees Celsius. CC -!- PTM: Amidated. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M62413; AAA49468.1; -; Genomic_DNA. DR PIR; JS0705; JS0705. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0050825; F:ice binding; TAS:UniProtKB. DR GO; GO:0042309; P:homoiothermy; IEP:UniProtKB. DR GO; GO:0050826; P:response to freezing; IEP:UniProtKB. DR InterPro; IPR000104; Antifreeze_1. DR PRINTS; PR00308; ANTIFREEZEI. PE 1: Evidence at protein level; KW Amidation; Antifreeze protein; Direct protein sequencing; Repeat; KW Secreted; Signal. FT SIGNAL 1 23 FT PROPEP 24 44 Removed by a dipeptidylpeptidase FT (Probable). FT /FTId=PRO_0000225596. FT CHAIN 45 81 Ice-structuring protein B. FT /FTId=PRO_0000225597. FT COMPBIAS 28 80 Ala-rich. FT MOD_RES 81 81 Arginine amide (By similarity). SQ SEQUENCE 82 AA; 7794 MW; C8AEDA75DA4B87FA CRC64; MALSLFTVGQ LIFLFWTMRI TEARPDPAAK AAPAAAAVPA AAAPDTASDA AAAAALTAAN AAAAAKLTAD NAAAAAAATA RG // ID ANPD_MACAM Reviewed; 87 AA. AC P19604; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 54. DE RecName: Full=Ice-structuring protein C7; DE Short=ISP C7; DE AltName: Full=Antifreeze protein C7; DE Flags: Precursor; OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; B31075; B31075. DR HSSP; P19608; 1OPS. DR SMR; P19604; 22-85. DR HOVERGEN; P19604; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 3: Inferred from homology; KW Antifreeze protein; Secreted; Signal. FT SIGNAL 1 21 By similarity. FT CHAIN 22 87 Ice-structuring protein C7. FT /FTId=PRO_0000001692. FT DOMAIN 24 83 AFP-like. FT SITE 29 29 Important for ice-binding (By FT similarity). FT SITE 34 34 Important for ice-binding (By FT similarity). FT SITE 38 38 Important for ice-binding (By FT similarity). FT SITE 64 64 Important for ice-binding (By FT similarity). SQ SEQUENCE 87 AA; 9229 MW; B5615B2E82DC87AB CRC64; MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPINTALTPV MMEGKVTNPI GIPFAEMSQI VGKQVNTPVA KGQTIMPNMV KTYAAGK // ID ANPE_MACAM Reviewed; 87 AA. AC P19605; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 22-SEP-2009, entry version 54. DE RecName: Full=Ice-structuring protein C10; DE Short=ISP C10; DE AltName: Full=Antifreeze protein C10; DE Flags: Precursor; OS Macrozoarces americanus (Ocean pout) (Zoarces americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei; OC Zoarcidae; Zoarcinae; Macrozoarces. OX NCBI_TaxID=8199; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=88298890; PubMed=3403560; RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., RA Hayes P.H., Buettner B., Davies P.L.; RT "Multiple genes provide the basis for antifreeze protein diversity and RT dosage in the ocean pout, Macrozoarces americanus."; RL J. Biol. Chem. 263:12049-12055(1988). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point by CC absorbing ice and inhibiting its growth. CC -!- SUBCELLULAR LOCATION: Secreted (By similarity). CC -!- SIMILARITY: Belongs to the type-III AFP family. CC -!- SIMILARITY: Contains 1 AFP-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A31075; A31075. DR HSSP; P19608; 1OPS. DR SMR; P19605; 22-85. DR HOVERGEN; P19605; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013974; SAF. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR ProDom; PD003258; AntifreezeIII; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 3: Inferred from homology; KW Antifreeze protein; Secreted; Signal. FT SIGNAL 1 21 By similarity. FT CHAIN 22 87 Ice-structuring protein C10. FT /FTId=PRO_0000001693. FT DOMAIN 24 83 AFP-like. FT SITE 29 29 Important for ice-binding (By FT similarity). FT SITE 34 34 Important for ice-binding (By FT similarity). FT SITE 38 38 Important for ice-binding (By FT similarity). FT SITE 64 64 Important for ice-binding (By FT similarity). SQ SEQUENCE 87 AA; 9306 MW; 92655F2AC313A0B5 CRC64; MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPMNSALTPV MMEGKVTNPI GIPFAEMSQM VGKQVNRPVA KGQTIMPNMV KTYAAGK // ID ANPX_PSEAM Reviewed; 91 AA. AC P07835; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 22-SEP-2009, entry version 46. DE RecName: Full=Ice-structuring protein 2A7; DE Short=ISP 2A7; DE AltName: Full=Antifreeze protein IIA7; DE Short=AFP; DE Flags: Precursor; OS Pseudopleuronectes americanus (Winter flounder) (Pleuronectes OS americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes. OX NCBI_TaxID=8265; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=85054993; PubMed=6548752; RA Gourlie B., Lin Y., Price J., Devries A.L., Powers D., Huang R.C.C.; RT "Winter flounder antifreeze proteins: a multigene family."; RL J. Biol. Chem. 259:14960-14965(1984). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M10148; AAA49465.1; -; mRNA. DR PIR; A22592; A22592. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050825; F:ice binding; IEA:InterPro. DR GO; GO:0042309; P:homoiothermy; IEA:InterPro. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR000104; Antifreeze_1. DR PRINTS; PR00308; ANTIFREEZEI. PE 3: Inferred from homology; KW Antifreeze protein; Repeat; Secreted; Signal. FT SIGNAL 1 21 Potential. FT PROPEP 22 39 Removed by a dipeptidylpeptidase FT (Probable). FT /FTId=PRO_0000001687. FT CHAIN 40 91 Ice-structuring protein 2A7. FT /FTId=PRO_0000001688. SQ SEQUENCE 91 AA; 8326 MW; D1FC542FD865012C CRC64; MALSLFTVGQ LIFLFWTMRI TEANPDPAAK AVPAAAAPDT ASDAAAAAAA TAATAAAAAA ATAATAAKAA ALTAANAAAA AAATAAAAAR G // ID ANPY_PSEAM Reviewed; 91 AA. AC P23699; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 22-SEP-2009, entry version 46. DE RecName: Full=Ice-structuring protein; DE Short=ISP; DE AltName: Full=Antifreeze protein; DE Short=AFP; DE Flags: Precursor; OS Pseudopleuronectes americanus (Winter flounder) (Pleuronectes OS americanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes; OC Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes. OX NCBI_TaxID=8265; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=90384854; PubMed=2402466; DOI=10.1093/nar/18.17.5303; RA Gauthier S., Wu Y., Davies P.L.; RT "Nucleotide sequence of a variant antifreeze protein gene."; RL Nucleic Acids Res. 18:5303-5303(1990). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the type-I AFP family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X53718; CAA37754.1; -; Genomic_DNA. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0050825; F:ice binding; IEA:InterPro. DR GO; GO:0042309; P:homoiothermy; IEA:InterPro. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR000104; Antifreeze_1. DR PRINTS; PR00308; ANTIFREEZEI. PE 3: Inferred from homology; KW Antifreeze protein; Repeat; Secreted; Signal. FT SIGNAL 1 21 Potential. FT PROPEP 22 39 Removed by a dipeptidylpeptidase FT (Probable). FT /FTId=PRO_0000001689. FT CHAIN 40 91 Ice-structuring protein. FT /FTId=PRO_0000001690. SQ SEQUENCE 91 AA; 8355 MW; D1FC5439A902012C CRC64; MALSLFTVGQ LIFLFWTMRI TEANPDPAAK AVPAAAAPDT ASDAAAAAAA TAATAAAAAA ATAVTAAKAA ALTAANAAAA AAATAAAAAR G // ID ANTF_ANTPS Reviewed; 20 AA. AC P86268; DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 22-SEP-2009, entry version 3. DE RecName: Full=Antifreeze protein; DE Flags: Fragment; OS Antarctomyces psychrotrophicus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes; OC Thelebolales; Thelebolaceae; Antarctomyces. OX NCBI_TaxID=89416; RN [1] RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, INDUCTION, RP GLYCOSYLATION, AND MASS SPECTROMETRY. RC STRAIN=KG-1; RA Xiao N., Takamichi M., Suzuki K., Nishimiya Y., Kondo H., Tsuda S., RA Hoshino T.; RT "A new antifreeze protein from Antarctic ascomycota."; RL Submitted (MAR-2009) to UniProtKB. CC -!- FUNCTION: Modification of ice crystals, thermal hysteresis and CC recrystallization inhibiton. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- INDUCTION: By low temperature. CC -!- PTM: N-glycosylated and O-glycosylated. CC -!- MASS SPECTROMETRY: Mass=21742; Method=MALDI; Range=1-?; CC Source=Ref.1; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Glycoprotein; Secreted; KW Stress response. FT CHAIN 1 >20 Antifreeze protein. FT /FTId=PRO_0000373064. FT NON_TER 20 20 SQ SEQUENCE 20 AA; 1848 MW; F48180EEC1E885E8 CRC64; AGLDLGAASX FGALAFEGVA // ID ISP2_HEMAM Reviewed; 163 AA. AC P05140; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 2. DT 22-SEP-2009, entry version 67. DE RecName: Full=Type-2 ice-structuring protein; DE AltName: Full=Type II antifreeze protein; DE Short=AFP; DE Flags: Precursor; OS Hemitripterus americanus (Sea raven). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes; OC Cottoidei; Hemitripteridae; Hemitripterus. OX NCBI_TaxID=8094; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87057207; PubMed=3782083; RA Ng N.F.L., Trinh K.-Y., Hew C.-L.; RT "Structure of an antifreeze polypeptide precursor from the sea raven, RT Hemitripterus americanus."; RL J. Biol. Chem. 261:15690-15695(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN RP SEQUENCE. RX MEDLINE=90036986; PubMed=2572595; RA Hayes P., Scott G.K., Ng N.F.L., Hew C.-L., Davies P.L.; RT "Cystine-rich type II antifreeze protein precursor is initiated from RT the third AUG codon of its mRNA."; RL J. Biol. Chem. 264:18761-18767(1989). RN [3] RP PRELIMINARY DISULFIDE BONDS, AND SIMILARITY TO C-TYPE LECTINS. RX MEDLINE=92355557; PubMed=1644794; RA Ng N.F.L., Hew C.-L.; RT "Structure of an antifreeze polypeptide from the sea raven. Disulfide RT bonds and similarity to lectin-binding proteins."; RL J. Biol. Chem. 267:16069-16075(1992). RN [4] RP STRUCTURE BY NMR, AND DISULFIDE BONDS. RX MEDLINE=98206886; PubMed=9537986; DOI=10.1021/bi972788c; RA Gronwald W., Loewen M.C., Lix B., Daugulis A.J., Soennichsen F.D., RA Davies P.L., Sykes B.D.; RT "The solution structure of type II antifreeze protein reveals a new RT member of the lectin family."; RL Biochemistry 37:4712-4721(1998). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Contains 1 C-type lectin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02593; AAA49617.1; ALT_INIT; mRNA. DR EMBL; J05100; AAA49618.1; -; Genomic_DNA. DR PIR; A34313; A34313. DR PDB; 2AFP; NMR; -; A=35-163. DR PDBsum; 2AFP; -. DR HOVERGEN; P05140; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR002353; AntifreezeII. DR InterPro; IPR001304; C-type_lectin. DR InterPro; IPR016186; C-type_lectin-like. DR InterPro; IPR018378; C-type_lectin_CS. DR Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1. DR Pfam; PF00059; Lectin_C; 1. DR PRINTS; PR00356; ANTIFREEZEII. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antifreeze protein; Direct protein sequencing; KW Disulfide bond; Lectin; Secreted; Signal. FT SIGNAL 1 17 Potential. FT PROPEP 18 34 FT /FTId=PRO_0000017544. FT CHAIN 35 163 Type-2 ice-structuring protein. FT /FTId=PRO_0000017545. FT DOMAIN 39 163 C-type lectin. FT DISULFID 41 52 FT DISULFID 69 159 FT DISULFID 103 134 FT DISULFID 123 145 FT DISULFID 135 151 FT CONFLICT 38 38 P -> G (in Ref. 2; AAA49618). FT STRAND 43 45 FT STRAND 49 53 FT HELIX 62 72 FT STRAND 80 82 FT HELIX 83 91 FT STRAND 103 107 FT STRAND 110 114 FT STRAND 122 124 FT STRAND 141 144 FT STRAND 159 161 SQ SEQUENCE 163 AA; 17509 MW; 52C2D284F65E8A47 CRC64; MLTVSLLVCA MMALTQANDD KILKGTATEA GPVSQRAPPN CPAGWQPLGD RCIYYETTAM TWALAETNCM KLGGHLASIH SQEEHSFIQT LNAGVVWIGG SACLQAGAWT WSDGTPMNFR SWCSTKPDDV LAACCMQMTA AADQCWDDLP CPASHKSVCA MTF // ID ISP2_OSMMO Reviewed; 175 AA. AC Q01758; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 22-SEP-2009, entry version 51. DE RecName: Full=Type-2 ice-structuring protein; DE AltName: Full=Type II antifreeze protein; DE Short=AFP; DE Flags: Precursor; OS Osmerus mordax (Rainbow smelt). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; OC Protacanthopterygii; Salmoniformes; Osmeridae; Osmerus. OX NCBI_TaxID=8014; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-65; 69-78; RP 145-154 AND 161-173. RC TISSUE=Liver; RX MEDLINE=92287116; PubMed=1599470; RA Ewart K.V., Rubinsky B., Fletcher G.L.; RT "Structural and functional similarity between fish antifreeze proteins RT and calcium-dependent lectins."; RL Biochem. Biophys. Res. Commun. 185:335-340(1992). CC -!- FUNCTION: Antifreeze proteins lower the blood freezing point. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Contains 1 C-type lectin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M96154; AAA49442.1; -; mRNA. DR PIR; JH0626; JH0626. DR HSSP; P05140; 2AFP. DR HOVERGEN; Q01758; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW. DR GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW. DR InterPro; IPR002353; AntifreezeII. DR InterPro; IPR001304; C-type_lectin. DR InterPro; IPR016186; C-type_lectin-like. DR InterPro; IPR018378; C-type_lectin_CS. DR Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1. DR Pfam; PF00059; Lectin_C; 1. DR PRINTS; PR00356; ANTIFREEZEII. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. PE 1: Evidence at protein level; KW Antifreeze protein; Direct protein sequencing; Disulfide bond; Lectin; KW Secreted; Signal. FT SIGNAL 1 16 Potential. FT PROPEP 17 33 Potential. FT /FTId=PRO_0000017546. FT CHAIN 34 175 Type-2 ice-structuring protein. FT /FTId=PRO_0000017547. FT DOMAIN 36 163 C-type lectin. FT DISULFID 38 49 By similarity. FT DISULFID 66 159 By similarity. FT DISULFID 103 134 By similarity. FT DISULFID 123 145 By similarity. FT DISULFID 135 151 By similarity. SQ SEQUENCE 175 AA; 19054 MW; E2A72D8C030AFAA3 CRC64; MLAALLVCAM VALTRAANGD TGKEAVMTGS SGKNLTECPT DWKMFNGRCF LFNPLQLHWA HAQISCMKDG ANLASIHSLE EYAFVKELTT AGLIPAWIGG SDCHVSTYWF WMDSTSMDFT DWCAAQPDFT LTECCIQINV GVGKCWNDTP CTHLHASVCA KPATVIPEVT PPSIM //