ID   ANP1C_ZOAAM             Reviewed;          87 AA.
AC   P07457; P19610;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Ice-structuring protein SP1-C;
DE            Short=ISP SP1-C;
DE   AltName: Full=Antifreeze protein SP1-C;
DE   Flags: Precursor;
OS   Zoarces americanus (Ocean pout) (Macrozoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Zoarcales; Zoarcidae; Zoarcinae;
OC   Zoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE
RP   FORMATION AT GLN-23, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=3840475; DOI=10.1016/s0021-9258(17)38811-7;
RA   Li X.-M., Trinh K.-Y., Hew C.-L., Buettner B., Baenziger J., Davies P.L.;
RT   "Structure of an antifreeze polypeptide and its precursor from the ocean
RT   pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 260:12904-12909(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-86, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=3403560; DOI=10.1016/s0021-9258(18)37891-8;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., Hayes P.H.,
RA   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: Contributes to protect fish blood from freezing at subzero
CC       sea water temperatures. Lowers the blood freezing point. Binds to
CC       nascent ice crystals and prevents further growth (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3403560,
CC       ECO:0000269|PubMed:3840475}.
CC   -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC       {ECO:0000269|PubMed:3403560, ECO:0000269|PubMed:3840475}.
CC   -!- SIMILARITY: Belongs to the type-III AFP family. {ECO:0000305}.
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DR   EMBL; M11790; AAA49347.1; -; mRNA.
DR   PIR; A24081; FDFICP.
DR   AlphaFoldDB; P07457; -.
DR   SMR; P07457; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR036732; AFP_Neu5c_C_sf.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   SMART; SM00858; SAF; 1.
DR   SUPFAM; SSF51269; SSF51269; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Pyrrolidone carboxylic acid;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:3403560"
FT   CHAIN           23..87
FT                   /note="Ice-structuring protein SP1-C"
FT                   /id="PRO_0000001691"
FT   DOMAIN          24..83
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
FT   SITE            29
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            34
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            38
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            64
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         23
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:3840475"
SQ   SEQUENCE   87 AA;  9229 MW;  58D79961968D87B8 CRC64;
     MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPINTALTPA MMEGKVTNPI GIPFAEMSQI
     VGKQVNTPVA KGQTLMPNMV KTYVAGK