ID   ANP1_LYCDA              Reviewed;          64 AA.
AC   P35751;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Ice-structuring protein RD1;
DE            Short=ISP RD1;
DE   AltName: Full=Antifreeze peptide RD1;
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   X-RAY CRYSTALLOGRAPHY (0.62 ANGSTROMS).
RX   PubMed=12547803; DOI=10.1016/s0006-3495(03)74938-8;
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 protein
RT   RD1 at 0.62-A resolution reveals structuRAl microheterogeneity of protein
RT   and solvation.";
RL   Biophys. J. 84:1228-1237(2003).
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; S53512; S53512.
DR   PDB; 1UCS; X-ray; 0.62 A; A=1-64.
DR   PDBsum; 1UCS; -.
DR   AlphaFoldDB; P35751; -.
DR   BMRB; P35751; -.
DR   SMR; P35751; -.
DR   EvolutionaryTrace; P35751; -.
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   PRINTS; PR00357; ANTIFREEZIII.
DR   SUPFAM; SSF51269; SSF51269; 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
FT                   /note="Ice-structuring protein RD1"
FT                   /id="PRO_0000155151"
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"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:1UCS"
FT   HELIX           19..21
FT                   /evidence="ECO:0007829|PDB:1UCS"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:1UCS"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:1UCS"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:1UCS"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:1UCS"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:1UCS"
SQ   SEQUENCE   64 AA;  6906 MW;  154C6BE62D913192 CRC64;
     NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPKL VGMQVNRAVP LGTTLMPDMV
     KNYE