ANP3_LYCDA
ID ANP3_LYCDA Reviewed; 134 AA.
AC P35753;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Ice-structuring protein RD3;
DE Short=ISP RD3;
DE AltName: Full=Antifreeze peptide RD3;
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 STRUCTURE BY NMR OF 1-73.
RX PubMed=10423534; DOI=10.1093/oxfordjournals.jbchem.a022462;
RA Miura K., Ohgiya S., Hoshino T., Nemoto N., Odaira M., Nitta K., Tsuda S.;
RT "Determination of the solution structure of the N-domain plus linker of
RT antarctic eel pout antifreeze protein RD3.";
RL J. Biochem. 126:387-394(1999).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=11010977; DOI=10.1074/jbc.m007902200;
RA Miura K., Ohgiya S., Hoshino T., Nemoto N., Suetake T., Miura A.,
RA Spyracopoulos L., Kondo H., Tsuda S.;
RT "NMR analysis of type III antifreeze protein intramolecular dimer.
RT Structural basis for enhanced activity.";
RL J. Biol. Chem. 276:1304-1310(2001).
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; S53514; S53514.
DR PDB; 1C89; NMR; -; A=1-134.
DR PDB; 1C8A; NMR; -; A=1-134.
DR PDB; 3NLA; NMR; -; A=1-73.
DR PDB; 3RDN; NMR; -; A=1-73.
DR PDBsum; 1C89; -.
DR PDBsum; 1C8A; -.
DR PDBsum; 3NLA; -.
DR PDBsum; 3RDN; -.
DR AlphaFoldDB; P35753; -.
DR BMRB; P35753; -.
DR SMR; P35753; -.
DR EvolutionaryTrace; P35753; -.
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 PRINTS; PR00357; ANTIFREEZIII.
DR SMART; SM00858; SAF; 2.
DR SUPFAM; SSF51269; SSF51269; 2.
DR PROSITE; PS50844; AFP_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antifreeze protein; Direct protein sequencing; Repeat;
KW Secreted.
FT CHAIN 1..134
FT /note="Ice-structuring protein RD3"
FT /id="PRO_0000155153"
FT DOMAIN 4..63
FT /note="AFP-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
FT DOMAIN 74..133
FT /note="AFP-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
FT REGION 65..70
FT /note="Linker"
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 SITE 79
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
FT SITE 88
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
FT SITE 114
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1C89"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1C89"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1C89"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1C89"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1C89"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3RDN"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1C89"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3RDN"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:1C89"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1C89"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1C89"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1C89"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1C89"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1C89"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1C89"
SQ SEQUENCE 134 AA; 14480 MW; F7F208BF3E2CAA54 CRC64;
NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPNL VGMQVNRAVP LGTTLMPDMV
KNYEDGTTSP GLKSVVANQL IPINTALTLV MMKAEEVSPK GIPSEEISKL VGMQVNRAVY
LDQTLMPDMV KNYE
