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OSTCN_FELCA
ID   OSTCN_FELCA             Reviewed;          49 AA.
AC   P02821;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 110.
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   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-9, AND GAMMA-CARBOXYGLUTAMATION AT
RP   GLU-17; GLU-21 AND GLU-24.
RX   PubMed=6334077; DOI=10.1093/oxfordjournals.jbchem.a134851;
RA   Shimomura H., Kanai Y., Sanada K.;
RT   "Primary structure of cat osteocalcin.";
RL   J. Biochem. 96:405-411(1984).
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:6334077}.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
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DR   PIR; A03304; GECT.
DR   AlphaFoldDB; P02821; -.
DR   SMR; P02821; -.
DR   STRING; 9685.ENSFCAP00000018678; -.
DR   eggNOG; ENOG502S85I; Eukaryota.
DR   HOGENOM; CLU_3146896_0_0_1; -.
DR   InParanoid; P02821; -.
DR   Proteomes; UP000011712; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Hydroxylation; Metal-binding;
KW   Reference proteome; Secreted.
FT   CHAIN           1..49
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000148897"
FT   DOMAIN          1..47
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         9
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000269|PubMed:6334077"
FT   MOD_RES         17
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6334077"
FT   MOD_RES         21
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6334077"
FT   MOD_RES         24
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6334077"
FT   DISULFID        23..29
SQ   SEQUENCE   49 AA;  5495 MW;  93D2131FA9F656D3 CRC64;
     YLAPGLGAPA PYPDPLEPKR EICELNPDCD ELADHIGFQD AYRRFYGTV
 
 
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