ID Q53UJ4_9TELE Unreviewed; 88 AA.
AC Q53UJ4;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 22-FEB-2023, entry version 48.
DE RecName: Full=Ice-structuring protein {ECO:0000256|RuleBase:RU362061};
DE AltName: Full=Antifreeze protein {ECO:0000256|RuleBase:RU362061};
OS Zoarces elongatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Zoarcales; Zoarcidae; Zoarcinae;
OC Zoarces.
OX NCBI_TaxID=291231 {ECO:0000313|EMBL:BAD95781.1};
RN [1] {ECO:0000313|EMBL:BAD95781.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15654886; DOI=10.1111/j.1742-4658.2004.04490.x;
RA Nishimiya Y., Sato R., Takamichi M., Miura A., Tsuda S.;
RT "Co-operative effect of the isoforms of type III antifreeze protein
RT expressed in Notched-fin eelpout, Zoarces elongatus Kner.";
RL FEBS J. 272:482-492(2005).
RN [2] {ECO:0007829|PDB:5XQN, ECO:0007829|PDB:5XQP}
RP X-RAY CRYSTALLOGRAPHY (0.97 ANGSTROMS) OF 23-88.
RX PubMed=29735675; DOI=10.1073/pnas.1800635115;
RA Mahatabuddin S., Fukami D., Arai T., Nishimiya Y., Shimizu R.,
RA Shibazaki C., Kondo H., Adachi M., Tsuda S.;
RT "Polypentagonal ice-like water networks emerge solely in an activity-
RT improved variant of ice-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:5456-5461(2018).
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:0000256|ARBA:ARBA00024935}.
CC -!- FUNCTION: Lowers the blood freezing point. Contributes to protect fish
CC blood from freezing at subzero sea water temperatures. Binds to nascent
CC ice crystals and prevents further growth.
CC {ECO:0000256|RuleBase:RU362061}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU362061}.
CC -!- SIMILARITY: Belongs to the type-III AFP family.
CC {ECO:0000256|ARBA:ARBA00007445, ECO:0000256|RuleBase:RU362061}.
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DR EMBL; AB188394; BAD95781.1; -; mRNA.
DR PDB; 5XQN; X-ray; 1.19 A; A/B=23-88.
DR PDB; 5XQP; X-ray; 1.00 A; A/B/C/D=23-88.
DR PDB; 5XQR; X-ray; 1.30 A; A/B=23-88.
DR PDB; 5XQU; X-ray; 1.00 A; A=23-88.
DR PDB; 5XQV; X-ray; 0.97 A; A=23-88.
DR PDB; 5XR0; X-ray; 0.98 A; A=23-88.
DR PDBsum; 5XQN; -.
DR PDBsum; 5XQP; -.
DR PDBsum; 5XQR; -.
DR PDBsum; 5XQU; -.
DR PDBsum; 5XQV; -.
DR PDBsum; 5XR0; -.
DR AlphaFoldDB; Q53UJ4; -.
DR SMR; Q53UJ4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR CDD; cd11617; Antifreeze_III; 1.
DR Gene3D; 3.90.1210.10; Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain; 1.
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 SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; AFP III-like domain; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5XQN, ECO:0007829|PDB:5XQP};
KW Antifreeze protein {ECO:0000256|ARBA:ARBA00023076,
KW ECO:0000256|RuleBase:RU362061};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU362061};
KW Signal {ECO:0000256|RuleBase:RU362061}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU362061"
FT CHAIN 23..88
FT /note="Ice-structuring protein"
FT /evidence="ECO:0000256|RuleBase:RU362061"
FT /id="PRO_5005143468"
FT DOMAIN 25..84
FT /note="AFP-like"
FT /evidence="ECO:0000259|PROSITE:PS50844"
SQ SEQUENCE 88 AA; 9230 MW; BBFE051BC9F1C281 CRC64;
MKSVILTGLL FVLLCVDHMS SAGESVVATQ LIPINTALTP AMMEGKVTNP SGIPFAEMSQ
IVGKQVNTPV AKGQTLMPGM VKTYVPAK
//
