ID   ANPY_PSEAM              Reviewed;          91 AA.
AC   P23699; Q547T1;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Ice-structuring protein;
DE            Short=ISP;
DE   AltName: Full=Type I antifreeze protein IIA8;
DE            Short=AFP;
DE   Flags: Precursor;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC   Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gong H.Y., Hu M.C., Weng C.F., Huang W.T., Huang R.C., Hui C.F., Wu J.L.;
RT   "Expression of soluble winter flounder antifreeze protein with four ice-
RT   binding repeats in E. Coli.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the type-I AFP family. {ECO:0000305}.
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DR   EMBL; X53718; CAA37754.1; -; Genomic_DNA.
DR   EMBL; AF448487; AAM75809.1; -; mRNA.
DR   AlphaFoldDB; P23699; -.
DR   SMR; P23699; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050825; F:ice binding; IEA:InterPro.
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                   /evidence="ECO:0000255"
FT   PROPEP          22..39
FT                   /note="Removed by a dipeptidylpeptidase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000001689"
FT   CHAIN           40..91
FT                   /note="Ice-structuring protein"
FT                   /id="PRO_0000001690"
SQ   SEQUENCE   91 AA;  8355 MW;  D1FC5439A902012C CRC64;
     MALSLFTVGQ LIFLFWTMRI TEANPDPAAK AVPAAAAPDT ASDAAAAAAA TAATAAAAAA
     ATAVTAAKAA ALTAANAAAA AAATAAAAAR G