OSTCN_CHICK
ID OSTCN_CHICK Reviewed; 97 AA.
AC P02822; Q90620;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 117.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Bone;
RX PubMed=7747623; DOI=10.1002/jbmr.5650100122;
RA Neugebauer B.M., Moore M.A., Broess M., Gerstenfeld L.C., Hauschka P.V.;
RT "Characterization of structural sequences in the chicken osteocalcin gene:
RT expression of osteocalcin by maturing osteoblasts and by hypertrophic
RT chondrocytes in vitro.";
RL J. Bone Miner. Res. 10:157-163(1995).
RN [2]
RP PROTEIN SEQUENCE OF 49-97, AND GAMMA-CARBOXYGLUTAMATION AT GLU-65; GLU-69
RP AND GLU-72.
RX PubMed=6792200; DOI=10.1016/s0021-9258(19)68721-1;
RA Carr S.A., Hauschka P.V., Biemann K.;
RT "Gas chromatographic mass spectrometric sequence determination of
RT osteocalcin, a gamma-carboxyglutamic acid-containing protein from chicken
RT bone.";
RL J. Biol. Chem. 256:9944-9950(1981).
CC -!- FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly
CC 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:6792200}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; U10578; AAA78809.1; -; mRNA.
DR PIR; I50700; GECH.
DR AlphaFoldDB; P02822; -.
DR SMR; P02822; -.
DR VEuPathDB; HostDB:geneid_396348; -.
DR InParanoid; P02822; -.
DR PhylomeDB; P02822; -.
DR Proteomes; UP000000539; Unplaced.
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 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..48
FT /evidence="ECO:0000269|PubMed:6792200"
FT /id="PRO_0000011094"
FT CHAIN 49..97
FT /note="Osteocalcin"
FT /evidence="ECO:0000269|PubMed:7747623"
FT /id="PRO_0000011095"
FT DOMAIN 49..95
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6792200"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6792200"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6792200"
FT DISULFID 71..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 97 AA; 10707 MW; 768E6885C3327D62 CRC64;
MKAAALLLLA ALLTFSLCRS APDGSDARSA KAFISHRQRA EMVRRQKRHY AQDSGVAGAP
PNPLEAQREV CELSPDCDEL ADQIGFQEAY RRFYGPV
