ID   OSTCN_XENTR             Reviewed;         101 AA.
AC   Q6DJ00;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds strongly to apatite and calcium. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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}.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
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DR   EMBL; BC075385; AAH75385.1; -; mRNA.
DR   RefSeq; NP_001006689.1; NM_001006688.1.
DR   AlphaFoldDB; Q6DJ00; -.
DR   SMR; Q6DJ00; -.
DR   DNASU; 448310; -.
DR   Ensembl; ENSXETT00000005554; ENSXETP00000005554; ENSXETG00000002605.
DR   GeneID; 448310; -.
DR   KEGG; xtr:448310; -.
DR   CTD; 632; -.
DR   Xenbase; XB-GENE-1018467; bglap.
DR   eggNOG; ENOG502S85I; Eukaryota.
DR   InParanoid; Q6DJ00; -.
DR   OrthoDB; 1520921at2759; -.
DR   Reactome; R-XTR-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-XTR-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000002605; Expressed in bone element and 5 other tissues.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0046848; F:hydroxyapatite binding; IBA:GO_Central.
DR   GO; GO:0008147; F:structural constituent of bone; IBA:GO_Central.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0060348; P:bone development; IBA:GO_Central.
DR   GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
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   3: Inferred from homology;
KW   Biomineralization; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; Gamma-carboxyglutamic acid; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..52
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000011102"
FT   CHAIN           53..101
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000011103"
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   MOD_RES         73
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         76
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DISULFID        75..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ   SEQUENCE   101 AA;  11160 MW;  8BD1C845E0CBD02C CRC64;
     MKLAIVLLLL GLAVLCLGGK DSQHSASAGD SRSSEAFISR QDSANFARRH KRSYRYNVAR
     GAAVTSPLES QREVCELNPD CDELADHIGF QEAYRRFYGP V