ANP12_ZOAAM
ID ANP12_ZOAAM Reviewed; 66 AA.
AC P19614;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Type-3 ice-structuring protein HPLC 12;
DE AltName: Full=Antifreeze protein QAE(HPLC 12);
DE AltName: Full=ISP type III HPLC 12;
OS Zoarces americanus (Ocean pout) (Macrozoarces americanus).
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=8199;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=3403560; DOI=10.1016/s0021-9258(18)37891-8;
RA Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K., Hayes P.H.,
RA Buettner B., Davies P.L.;
RT "Multiple genes provide the basis for antifreeze protein diversity and
RT dosage in the ocean pout, Macrozoarces americanus.";
RL J. Biol. Chem. 263:12049-12055(1988).
RN [2]
RP NOMENCLATURE.
RX PubMed=12050776;
RA Clarke C.J., Buckley S.L., Lindner N.;
RT "Ice structuring proteins - a new name for antifreeze proteins.";
RL Cryo Lett. 23:89-92(2002).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=8939756; DOI=10.1016/s0969-2126(96)00140-2;
RA Soennichsen F.D., Deluca C.I., Davies P.L., Sykes B.D.;
RT "Refined solution structure of type III antifreeze protein: hydrophobic
RT groups may be involved in the energetics of the protein-ice interaction.";
RL Structure 4:1325-1337(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
RX PubMed=8918883; DOI=10.1038/384285a0;
RA Jia Z., Deluca C.I., Chao H., Davies P.L.;
RT "Structural basis for the binding of a globular antifreeze protein to
RT ice.";
RL Nature 384:285-288(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF MUTANTS.
RX PubMed=9466928; DOI=10.1006/jmbi.1997.1482;
RA Deluca C.I., Davies P.L., Ye Q., Jia Z.;
RT "The effects of steric mutations on the structure of type III antifreeze
RT protein and its interaction with ice.";
RL J. Mol. Biol. 275:515-525(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA Antson A.A., Lewis S., Roper D.I., Smith D.J., Hubbard R.E.;
RL Submitted (OCT-1996) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX PubMed=10207002; DOI=10.1074/jbc.274.17.11842;
RA Graether S.P., Deluca C.I., Baardsnes J., Hill G.A., Davies P.L., Jia Z.;
RT "Quantitative and qualitative analysis of type III antifreeze protein
RT structure and function.";
RL J. Biol. Chem. 274:11842-11847(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 1-63.
RX PubMed=11162099; DOI=10.1006/jmbi.2000.4336;
RA Antson A.A., Smith D.J., Roper D.I., Lewis S., Caves L.S., Verma C.S.,
RA Buckley S.L., Lillford P.J., Hubbard R.E.;
RT "Understanding the mechanism of ice binding by type III antifreeze
RT proteins.";
RL J. Mol. Biol. 305:875-889(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.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3403560}.
CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC {ECO:0000269|PubMed:3403560}.
CC -!- SIMILARITY: Belongs to the type-III AFP family. {ECO:0000305}.
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DR PIR; A30839; A30839.
DR PDB; 1AME; X-ray; 1.65 A; A=1-63.
DR PDB; 1B7I; X-ray; 1.65 A; A=1-65.
DR PDB; 1B7J; X-ray; 1.65 A; A=1-63.
DR PDB; 1B7K; X-ray; 2.50 A; A=1-63.
DR PDB; 1EKL; X-ray; 1.65 A; A=1-63.
DR PDB; 1GZI; X-ray; 1.80 A; A=1-63.
DR PDB; 1HG7; X-ray; 1.15 A; A=1-63.
DR PDB; 1JAB; X-ray; 1.65 A; A=1-63.
DR PDB; 1KDE; NMR; -; A=1-63.
DR PDB; 1KDF; NMR; -; A=1-63.
DR PDB; 1MSI; X-ray; 1.25 A; A=2-63.
DR PDB; 1MSJ; X-ray; 2.30 A; A=1-63.
DR PDB; 2AME; X-ray; 2.00 A; A=1-63.
DR PDB; 2JIA; X-ray; 1.60 A; A=1-65.
DR PDB; 2MSI; X-ray; 1.90 A; A=2-63.
DR PDB; 2MSJ; X-ray; 1.90 A; A=1-63.
DR PDB; 2SPG; X-ray; 1.75 A; A=1-63.
DR PDB; 3AME; X-ray; 2.30 A; A=1-63.
DR PDB; 3MSI; X-ray; 1.43 A; A=2-63.
DR PDB; 3QF6; Neutron; 1.85 A; A=1-66.
DR PDB; 4AME; X-ray; 2.05 A; A=1-63.
DR PDB; 4MSI; X-ray; 1.60 A; A=2-63.
DR PDB; 4NY6; Other; 1.85 A; A=1-63.
DR PDB; 5C7R; X-ray; 1.94 A; A/B=1-63.
DR PDB; 5MSI; X-ray; 1.60 A; A=2-63.
DR PDB; 6AME; X-ray; 2.10 A; A=1-63.
DR PDB; 6MSI; X-ray; 1.65 A; A=2-63.
DR PDB; 7AME; X-ray; 1.70 A; A=1-63.
DR PDB; 7MSI; X-ray; 1.70 A; A=2-63.
DR PDB; 8AME; X-ray; 1.90 A; A=1-63.
DR PDB; 8MSI; X-ray; 2.60 A; A=1-63.
DR PDB; 9AME; X-ray; 1.80 A; A=1-63.
DR PDB; 9MSI; X-ray; 2.60 A; A=1-63.
DR PDBsum; 1AME; -.
DR PDBsum; 1B7I; -.
DR PDBsum; 1B7J; -.
DR PDBsum; 1B7K; -.
DR PDBsum; 1EKL; -.
DR PDBsum; 1GZI; -.
DR PDBsum; 1HG7; -.
DR PDBsum; 1JAB; -.
DR PDBsum; 1KDE; -.
DR PDBsum; 1KDF; -.
DR PDBsum; 1MSI; -.
DR PDBsum; 1MSJ; -.
DR PDBsum; 2AME; -.
DR PDBsum; 2JIA; -.
DR PDBsum; 2MSI; -.
DR PDBsum; 2MSJ; -.
DR PDBsum; 2SPG; -.
DR PDBsum; 3AME; -.
DR PDBsum; 3MSI; -.
DR PDBsum; 3QF6; -.
DR PDBsum; 4AME; -.
DR PDBsum; 4MSI; -.
DR PDBsum; 4NY6; -.
DR PDBsum; 5C7R; -.
DR PDBsum; 5MSI; -.
DR PDBsum; 6AME; -.
DR PDBsum; 6MSI; -.
DR PDBsum; 7AME; -.
DR PDBsum; 7MSI; -.
DR PDBsum; 8AME; -.
DR PDBsum; 8MSI; -.
DR PDBsum; 9AME; -.
DR PDBsum; 9MSI; -.
DR AlphaFoldDB; P19614; -.
DR BMRB; P19614; -.
DR SMR; P19614; -.
DR EvolutionaryTrace; P19614; -.
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..66
FT /note="Type-3 ice-structuring protein HPLC 12"
FT /id="PRO_0000155160"
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 SITE 14
FT /note="Important for ice-binding"
FT SITE 18
FT /note="Important for ice-binding"
FT SITE 44
FT /note="Important for ice-binding"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1HG7"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1HG7"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1HG7"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:1HG7"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1HG7"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1HG7"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1HG7"
SQ SEQUENCE 66 AA; 7027 MW; B6121A9902ED89F9 CRC64;
NQASVVANQL IPINTALTLV MMRSEVVTPV GIPAEDIPRL VSMQVNRAVP LGTTLMPDMV
KGYPPA
