ANPM_PSEAM
ID ANPM_PSEAM Reviewed; 218 AA.
AC B1P0S1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Antifreeze protein Maxi;
DE AltName: Full=5a-like AFP;
DE AltName: Full=Type 1 hyperactive antifreeze protein;
DE Short=AFP Hyp-1;
DE Flags: Precursor;
OS Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Pseudopleuronectes.
OX NCBI_TaxID=8265;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-30, SIGNAL PEPTIDE,
RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=18225917; DOI=10.1021/bi7020316;
RA Graham L.A., Marshall C.B., Lin F.H., Campbell R.L., Davies P.L.;
RT "Hyperactive antifreeze protein from fish contains multiple ice-binding
RT sites.";
RL Biochemistry 47:2051-2063(2008).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15141201; DOI=10.1038/429153a;
RA Marshall C.B., Fletcher G.L., Davies P.L.;
RT "Hyperactive antifreeze protein in a fish.";
RL Nature 429:153-153(2004).
RN [3]
RP PROTEIN SEQUENCE OF 24-35, SIGNAL PEPTIDE, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15716269; DOI=10.1074/jbc.m500622200;
RA Marshall C.B., Chakrabartty A., Davies P.L.;
RT "Hyperactive antifreeze protein from winter flounder is a very long rod-
RT like dimer of alpha-helices.";
RL J. Biol. Chem. 280:17920-17929(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-218, FUNCTION, SUBUNIT, AND
RP DOMAIN.
RX PubMed=24531972; DOI=10.1126/science.1247407;
RA Sun T., Lin F.H., Campbell R.L., Allingham J.S., Davies P.L.;
RT "An antifreeze protein folds with an interior network of more than 400
RT semi-clathrate waters.";
RL Science 343:795-798(2014).
CC -!- FUNCTION: Contributes to protect fish blood from freezing at subzero
CC sea water temperatures. Lowers the blood freezing point by about 1.1
CC degrees at a concentration of 0.1 mg/ml, and by about 1.5 degrees at a
CC concentration of 0.2 mg/ml. Binds to nascent ice crystals and prevents
CC further growth. {ECO:0000269|PubMed:15141201,
CC ECO:0000269|PubMed:15716269, ECO:0000269|PubMed:18225917,
CC ECO:0000269|PubMed:24531972}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermolabile, displays irreversible loss of activity and aggregation
CC at room temperature. {ECO:0000269|PubMed:15141201,
CC ECO:0000269|PubMed:15716269};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15716269,
CC ECO:0000269|PubMed:18225917, ECO:0000269|PubMed:24531972}.
CC -!- INTERACTION:
CC B1P0S1; B1P0S1: -; NbExp=3; IntAct=EBI-16093390, EBI-16093390;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15141201,
CC ECO:0000269|PubMed:15716269}.
CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC Detected in liver. {ECO:0000269|PubMed:15141201,
CC ECO:0000269|PubMed:15716269, ECO:0000269|PubMed:18225917}.
CC -!- DOMAIN: The polypeptide has an alpha-hairpin structure. Two subunits
CC dimerize to form a four-helix, rod-like structure. Each subunit is
CC composed of a cap structure and of tandem 11 residue repeats with the
CC sequence [TI]-X-X-X-A-X-X-X-A-X-X. Each repeat forms three helical
CC turns with an average of 3.7 residues per turn, as opposed to 3.6
CC residues per turn for a classical alpha helix. Contrary to other
CC proteins, where the protein core is stabilized by hydrophobic
CC interactions and contains little water, this protein contains in its
CC interior over 400 ordered water molecules with a semi-clathrate
CC structure. Most likely, the interaction with the surface of ice
CC crystals is mediated by bound water molecules that protrude between the
CC helices. {ECO:0000269|PubMed:24531972}.
CC -!- MISCELLANEOUS: The concentration in blood serum is about 0.2 mg/ml.
CC -!- SIMILARITY: Belongs to the type-I AFP family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=It did it its way - Issue
CC 162 of July 2014;
CC URL="https://web.expasy.org/spotlight/back_issues/162/";
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DR EMBL; EU188795; ABX38716.1; -; mRNA.
DR PDB; 4KE2; X-ray; 1.80 A; A/B/C=24-218.
DR PDBsum; 4KE2; -.
DR AlphaFoldDB; B1P0S1; -.
DR SMR; B1P0S1; -.
DR DIP; DIP-61370N; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050825; F:ice binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR InterPro; IPR000104; Antifreeze_1.
DR PRINTS; PR00308; ANTIFREEZEI.
PE 1: Evidence at protein level;
KW 3D-structure; Antifreeze protein; Direct protein sequencing; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15716269,
FT ECO:0000269|PubMed:18225917"
FT CHAIN 24..218
FT /note="Antifreeze protein Maxi"
FT /id="PRO_5000320911"
FT HELIX 27..117
FT /evidence="ECO:0007829|PDB:4KE2"
FT HELIX 123..216
FT /evidence="ECO:0007829|PDB:4KE2"
SQ SEQUENCE 218 AA; 19304 MW; 5EDA80C716CC9406 CRC64;
MALSLFTVGQ FIFLFWTISI TEANIDPAAR AAAAAAASKA AVTAADAAAA AATIAASAAS
VAAATAADDA AASIATINAA SAAAKSIAAA AAMAAKDTAA AAASAAAAAV ASAAKALETI
NVKAAYAAAT TANTAAAAAA ATATTAAAAA AAKATIDNAA AAKAAAVATA VSDAAATAAT
AAAVAAATLE AAAAKAAATA VSAAAAAAAA AIAFAAAP
