OSTCN_XIPGL
ID OSTCN_XIPGL Reviewed; 47 AA.
AC P02823;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Osteocalcin;
DE AltName: Full=Bone Gla protein;
DE Short=BGP;
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein;
GN Name=bglap;
OS Xiphias gladius (Swordfish) (Tetrapterus imperator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Istiophoriformes; Xiphiidae; Xiphias.
OX NCBI_TaxID=8245;
RN [1]
RP PROTEIN SEQUENCE.
RA Price P.A., Otsuka A.S., Poser J.W.;
RT "Comparison of gamma-carboxyglutamic acid-containing proteins from bovine
RT and swordfish bone: primary structure and Ca++ binding.";
RL (In) Wasserman R.H., Corradino R.A., Carafoli E., Kretsinger R.H.,
RL Maclennan D.H., Siegel F.L. (eds.);
RL Calcium-binding proteins and calcium function, pp.333-337, Elsevier, New
RL York (1977).
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 -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR PIR; A03306; GEWF.
DR AlphaFoldDB; P02823; -.
DR SMR; P02823; -.
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 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; Direct protein sequencing; Disulfide bond;
KW Gamma-carboxyglutamic acid; Metal-binding; Secreted.
FT CHAIN 1..47
FT /note="Osteocalcin"
FT /id="PRO_0000148911"
FT DOMAIN 1..43
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 13
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 17
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 20
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 19..25
SQ SEQUENCE 47 AA; 5080 MW; 8D93FE1787B09223 CRC64;
ATRAGDLTPL QLESLREVCE LNVSCDEMAD TAGIVAAYIA YYGPIQF
