OSTCN_SPAAU
ID OSTCN_SPAAU Reviewed; 97 AA.
AC P40148; Q90VW2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Osteocalcin;
DE AltName: Full=Bone Gla protein;
DE Short=BGP;
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein;
DE Flags: Precursor;
GN Name=bglap;
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=11404005; DOI=10.1016/s0378-1119(01)00426-7;
RA Pinto J.P., Ohresser M.C.P., Cancela M.L.;
RT "Cloning of the bone Gla protein gene from the teleost fish Sparus aurata.
RT Evidence for overall conservation in gene organization and bone-specific
RT expression from fish to man.";
RL Gene 270:77-91(2001).
RN [2]
RP PROTEIN SEQUENCE OF 53-97, AND GAMMA-CARBOXYGLUTAMATION AT GLU-63; GLU-67
RP AND GLU-70.
RX PubMed=8567186; DOI=10.1111/j.1399-3011.1995.tb01076.x;
RA Cancela M.L., Williamson M.K., Price P.A.;
RT "Amino-acid sequence of bone Gla protein from the African clawed toad
RT Xenopus laevis and the fish Sparus aurata.";
RL Int. J. Pept. Protein Res. 46:419-423(1995).
CC -!- FUNCTION: Binds strongly to apatite and calcium.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:8567186}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF048703; AAK66568.1; -; mRNA.
DR EMBL; AF289506; AAK62679.1; -; Genomic_DNA.
DR AlphaFoldDB; P40148; -.
DR SMR; P40148; -.
DR Ensembl; ENSSAUT00010015051; ENSSAUP00010014176; ENSSAUG00010006659.
DR GeneTree; ENSGT00710000107036; -.
DR OMA; CEANMAC; -.
DR Proteomes; UP000472265; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IEA:InterPro.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IEA:InterPro.
DR GO; GO:0032571; P:response to vitamin K; IEA:InterPro.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR039176; Osteocalcin.
DR PANTHER; PTHR14235; PTHR14235; 1.
DR SMART; SM00069; GLA; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..52
FT /evidence="ECO:0000269|PubMed:8567186"
FT /id="PRO_0000011098"
FT CHAIN 53..97
FT /note="Osteocalcin"
FT /id="PRO_0000011099"
FT DOMAIN 53..93
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:8567186"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:8567186"
FT MOD_RES 70
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:8567186"
FT DISULFID 69..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 97 AA; 10434 MW; B95608824FDFEECB CRC64;
MKTLAFLVLC SLAAICLTSD ASTGSQPASD NPADEGMFVE RDQASAVVRQ KRAAGQLSLT
QLESLREVCE LNLACEHMMD TEGIIAAYTA YYGPIPY
