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Database: UniProt
Entry: P83005
LinkDB: P83005
Original site: P83005 
ID   OSTCN_HORSE             Reviewed;          49 AA.
AC   P83005;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 73.
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   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-9, AND GAMMA-CARBOXYGLUTAMATION
RP   AT GLU-17; GLU-21 AND GLU-24.
RC   TISSUE=Bone;
RA   Carstanjen B., Wattiez R., Amory H., Lepage O.M., Remy B.;
RT   "Isolation and characterization of equine osteocalcin.";
RL   Ann. Med. Vet. 146:31-38(2002).
CC   -!- FUNCTION: Constitutes 1-2% of the total bone protein. It binds
CC       strongly to apatite and calcium.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K
CC       dependent carboxylation. These residues are essential for the
CC       binding of calcium. {ECO:0000255|PROSITE-ProRule:PRU00463,
CC       ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
DR   SMR; P83005; -.
DR   PaxDb; P83005; -.
DR   eggNOG; ENOG410J11Z; Eukaryota.
DR   eggNOG; ENOG410ZS6W; LUCA.
DR   HOGENOM; HOG000115820; -.
DR   InParanoid; P83005; -.
DR   Proteomes; UP000002281; 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:0001503; P:ossification; 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; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW   Hydroxylation; Metal-binding; Reference proteome; Secreted.
FT   CHAIN         1     49       Osteocalcin.
FT                                /FTId=PRO_0000148900.
FT   DOMAIN        1     47       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   METAL        17     17       Calcium 3. {ECO:0000250}.
FT   METAL        21     21       Calcium 2. {ECO:0000250}.
FT   METAL        24     24       Calcium 1. {ECO:0000250}.
FT   METAL        24     24       Calcium 2. {ECO:0000250}.
FT   METAL        30     30       Calcium 1. {ECO:0000250}.
FT   MOD_RES       9      9       Hydroxyproline. {ECO:0000269|Ref.1}.
FT   MOD_RES      17     17       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463, ECO:0000269|Ref.1}.
FT   MOD_RES      21     21       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463, ECO:0000269|Ref.1}.
FT   MOD_RES      24     24       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463, ECO:0000269|Ref.1}.
FT   DISULFID     23     29       {ECO:0000255|PROSITE-ProRule:PRU00463}.
SQ   SEQUENCE   49 AA;  5732 MW;  A5B826014D12857F CRC64;
     YLDHWLGAPA PYPDPLEPRR EVCELNPDCD ELADHIGFQE AYRRFYGPV
//
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