ID   ANP2_LYCDA              Reviewed;          64 AA.
AC   P12102; P35752;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Ice-structuring protein RD2;
DE            Short=ISP RD2;
DE   AltName: Full=Antifreeze peptide RD2;
OS   Lycodichthys dearborni (Antarctic eelpout) (Rhigophila dearborni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Zoarcales; Zoarcidae; Lycodinae;
OC   Lycodichthys.
OX   NCBI_TaxID=8201;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   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 linked
RT   in tandem.";
RL   Biochim. Biophys. Acta 1247:163-172(1995).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   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 and
RT   antarctic zoarcid fishes.";
RL   Biochim. Biophys. Acta 915:357-370(1987).
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:7696304}.
CC   -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC       {ECO:0000269|PubMed:7696304}.
CC   -!- SIMILARITY: Belongs to the type-III AFP family. {ECO:0000305}.
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DR   PIR; S08561; FDFIRE.
DR   AlphaFoldDB; P12102; -.
DR   SMR; P12102; -.
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   SUPFAM; SSF51269; SSF51269; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN           1..64
FT                   /note="Ice-structuring protein RD2"
FT                   /id="PRO_0000155152"
FT   DOMAIN          4..63
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
FT   SITE            9
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            14
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            18
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            44
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   64 AA;  6934 MW;  41EBAF6F2C812084 CRC64;
     NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEDIPRI IGMQVNRAVP LGTTLMPDMV
     KNYE