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   25-MAY-2022, entry version 46.
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 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] {ECO:0000312|EMBL:AAA49468.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis {ECO:0000269|PubMed:1555765};
RX   PubMed=1555765; DOI=10.1016/0378-1119(92)90372-v;
RA   Davies P.L.;
RT   "Conservation of antifreeze protein-encoding genes in tandem repeats.";
RL   Gene 112:163-170(1992).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 24-28, FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP   AMIDATION.
RC   TISSUE=Liver {ECO:0000269|PubMed:3769927};
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: 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.
CC       {ECO:0000269|PubMed:3769927}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC       {ECO:0000269|PubMed:3769927}.
CC   -!- INDUCTION: By winter conditions, at least in part by water temperatures
CC       of below 8 degrees Celsius. {ECO:0000269|PubMed:3769927}.
CC   -!- PTM: Amidated. {ECO:0000269|PubMed:3769927}.
CC   -!- SIMILARITY: Belongs to the type-I AFP family. {ECO:0000255}.
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DR   EMBL; M62413; AAA49468.1; -; Genomic_DNA.
DR   PIR; JS0705; JS0705.
DR   AlphaFoldDB; Q99013; -.
DR   SMR; Q99013; -.
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; Secreted;
KW   Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:3769927"
FT   PROPEP          24..44
FT                   /note="Removed by a dipeptidylpeptidase"
FT                   /evidence="ECO:0000269|PubMed:3769927"
FT                   /id="PRO_0000225596"
FT   CHAIN           45..81
FT                   /note="Ice-structuring protein B"
FT                   /evidence="ECO:0000269|PubMed:3769927"
FT                   /id="PRO_0000225597"
FT   MOD_RES         81
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   82 AA;  7794 MW;  C8AEDA75DA4B87FA CRC64;
     MALSLFTVGQ LIFLFWTMRI TEARPDPAAK AAPAAAAVPA AAAPDTASDA AAAAALTAAN
     AAAAAKLTAD NAAAAAAATA RG