OSTC1_DIPSG
ID OSTC1_DIPSG Reviewed; 45 AA.
AC P86867;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Osteocalcin 1 {ECO:0000303|PubMed:24185858};
DE Short=DsaOC1 {ECO:0000303|PubMed:24185858};
DE AltName: Full=Bone Gla protein {ECO:0000303|PubMed:24185858};
DE Short=BGP {ECO:0000250|UniProtKB:Q800Y1};
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein {ECO:0000250|UniProtKB:Q800Y1};
GN Name=bglap {ECO:0000250|UniProtKB:Q800Y1};
OS Diplodus sargus (White seabream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Diplodus.
OX NCBI_TaxID=38941 {ECO:0000303|PubMed:24185858};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Bone {ECO:0000303|PubMed:24185858};
RX PubMed=24185858; DOI=10.1007/s10695-013-9880-9;
RA Cavaco S., Williamson M.K., Rosa J., Roberto V., Cordeiro O., Price P.A.,
RA Leonor Cancela M., Laize V., Simes D.C.;
RT "Teleost fish osteocalcin 1 and 2 share the ability to bind the calcium
RT mineral phase.";
RL Fish Physiol. Biochem. 40:731-738(2014).
CC -!- FUNCTION: Binds strongly to apatite and calcium. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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}.
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 AlphaFoldDB; P86867; -.
DR SMR; P86867; -.
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: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 PANTHER; PTHR14235; PTHR14235; 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; Metal-binding; Secreted.
FT CHAIN 1..45
FT /note="Osteocalcin 1"
FT /evidence="ECO:0000269|PubMed:24185858"
FT /id="PRO_0000436919"
FT DOMAIN 1..41
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 15
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT MOD_RES 11
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q800Y1"
FT MOD_RES 15
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 18
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 17..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 45 AA; 4951 MW; 5BAEE6A1D0CB4A18 CRC64;
AAGQLSLTQL ESLREVCELN LACEHMMDTE GIIAAYTAYY GPIPY
