ID   OSTCN_XENLA             Reviewed;         101 AA.
AC   P40147; Q8JFA8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Osteocalcin;
DE   AltName: Full=Bone Gla protein;
DE            Short=BGP;
DE            Short=xBGP;
DE   AltName: Full=Gamma-carboxyglutamic acid-containing protein;
DE   Flags: Precursor;
GN   Name=bglap;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Bone;
RX   PubMed=12036588; DOI=10.1016/s0378-1119(02)00480-8;
RA   Viegas C.S.B., Pinto J.P., Conceicao N., Simes D.C., Cancela M.L.;
RT   "Cloning and characterization of the cDNA and gene encoding Xenopus laevis
RT   osteocalcin.";
RL   Gene 289:97-107(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 53-101, AND GAMMA-CARBOXYGLUTAMATION AT GLU-69; GLU-73
RP   AND GLU-76.
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}.
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DR   EMBL; AY043179; AAL07511.1; -; Genomic_DNA.
DR   EMBL; AF055576; AAM53434.1; -; mRNA.
DR   RefSeq; NP_001084212.1; NM_001090743.1.
DR   AlphaFoldDB; P40147; -.
DR   SMR; P40147; -.
DR   GeneID; 399370; -.
DR   KEGG; xla:399370; -.
DR   CTD; 399370; -.
DR   Xenbase; XB-GENE-1018471; bglap.S.
DR   OrthoDB; 1520921at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 399370; Expressed in internal ear and 3 other tissues.
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:0030500; P:regulation of bone mineralization; 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   InterPro; IPR002384; Osteocalcin/MGP.
DR   PANTHER; PTHR14235; PTHR14235; 1.
DR   PRINTS; PR00002; GLABONE.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..52
FT                   /evidence="ECO:0000269|PubMed:8567186"
FT                   /id="PRO_0000011100"
FT   CHAIN           53..101
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000011101"
FT   DOMAIN          53..99
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   BINDING         69
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
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   BINDING         76
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         69
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:8567186"
FT   MOD_RES         73
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:8567186"
FT   MOD_RES         76
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:8567186"
FT   DISULFID        75..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ   SEQUENCE   101 AA;  10858 MW;  D8D888BFB6AB9B1E CRC64;
     MKLAILTVLL LGAAVLCLGS KDADHSNSVG ESHSSEAFIS RQESASFARL KRSYGNNVGQ
     GAAVGSPLES QREVCELNPD CDELADHIGF QEAYRRFYGP V