OSTCN_ARGRE
ID OSTCN_ARGRE Reviewed; 97 AA.
AC Q800Y1;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 Argyrosomus regius (Meagre).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Argyrosomus.
OX NCBI_TaxID=172269;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO48725.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-81, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Cartilage;
RX PubMed=12568402; DOI=10.1359/jbmr.2003.18.2.244;
RA Simes D.C., Williamson M.K., Ortiz-Delgado J.B., Viegas C.S., Price P.A.,
RA Cancela M.L.;
RT "Purification of matrix Gla protein from a marine teleost fish, Argyrosomus
RT regius: calcified cartilage and not bone as the primary site of MGP
RT accumulation in fish.";
RL J. Bone Miner. Res. 18:244-259(2003).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 53-88, AND GAMMA-CARBOXYGLUTAMATION AT GLU-63; GLU-67
RP AND GLU-70.
RC TISSUE=Cartilage;
RX PubMed=14668966; DOI=10.1007/s00223-003-0079-4;
RA Simes D.C., Williamson M.K., Schaff B.J., Gavaia P.J., Ingleton P.M.,
RA Price P.A., Cancela M.L.;
RT "Characterization of osteocalcin (BGP) and matrix Gla protein (MGP) fish
RT specific antibodies: validation for immunodetection studies in lower
RT vertebrates.";
RL Calcif. Tissue Int. 74:170-180(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 53-97, DISULFIDE BOND, AND
RP GAMMA-CARBOXYGLUTAMATION AT GLU-63; GLU-67; GLU-70 AND GLU-77.
RX PubMed=15667217; DOI=10.1021/bi048336z;
RA Frazao C., Simes D.C., Coelho R., Alves D., Williamson M.K., Price P.A.,
RA Cancela M.L., Carrondo M.A.;
RT "Structural evidence of a fourth Gla residue in fish osteocalcin:
RT biological implications.";
RL Biochemistry 44:1234-1242(2005).
CC -!- FUNCTION: Binds strongly to apatite and calcium. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: In the branchial arches, BGP is found outside the
CC chondrocyte-containing zone. It is found in some cells in the basal
CC zone of the branchial filaments, near the branchial arches, and within
CC the extracellular matrix in the medial zone. In the vertebra, BGP is
CC found in the mineralized bone matrix. {ECO:0000269|PubMed:12568402}.
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:14668966,
CC ECO:0000269|PubMed:15667217}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF459030; AAO48725.1; -; mRNA.
DR PDB; 1VZM; X-ray; 1.40 A; A/B/C=53-97.
DR PDBsum; 1VZM; -.
DR AlphaFoldDB; Q800Y1; -.
DR SMR; Q800Y1; -.
DR EvolutionaryTrace; Q800Y1; -.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IEA:InterPro.
DR GO; GO:0030282; P:bone mineralization; TAS:UniProtKB.
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 3D-structure; Biomineralization; Calcium; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Metal-binding; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..52
FT /evidence="ECO:0000255, ECO:0000269|PubMed:12568402,
FT ECO:0000269|PubMed:14668966"
FT /id="PRO_0000011096"
FT CHAIN 53..97
FT /note="Osteocalcin"
FT /evidence="ECO:0000269|PubMed:12568402"
FT /id="PRO_0000011097"
FT DOMAIN 53..93
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 70
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 MOD_RES 63
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14668966, ECO:0000269|PubMed:15667217"
FT MOD_RES 67
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14668966, ECO:0000269|PubMed:15667217"
FT MOD_RES 70
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14668966, ECO:0000269|PubMed:15667217"
FT MOD_RES 77
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:15667217"
FT DISULFID 69..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:15667217"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:1VZM"
FT HELIX 73..92
FT /evidence="ECO:0007829|PDB:1VZM"
SQ SEQUENCE 97 AA; 10115 MW; BCDE8480EE9E7843 CRC64;
MKTLAILVLC SLAAICLTSS ASAGAQPAGD SPVQGGLFME KDQASAVVRQ TRAAKELTLA
QTESLREVCE TNMACDEMAD AQGIVAAYQA FYGPIPF
