OSTC1_SOLSE
ID OSTC1_SOLSE Reviewed; 95 AA.
AC Q1EG28; P86865;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Osteocalcin 1 {ECO:0000303|PubMed:16458082};
DE Short=SseOC1 {ECO:0000303|PubMed:16458082};
DE AltName: Full=Bone Gla protein {ECO:0000312|EMBL:AAW30003.1};
DE Short=BGL {ECO:0000250|UniProtKB:Q800Y1};
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein {ECO:0000250|UniProtKB:Q800Y1};
DE Flags: Precursor;
GN Name=bglapBGP {ECO:0000250|UniProtKB:Q800Y1};
GN Synonyms=BGP {ECO:0000312|EMBL:AAW30003.1};
OS Solea senegalensis (Senegalese sole).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Soleidae; Solea.
OX NCBI_TaxID=28829 {ECO:0000312|EMBL:AAW30003.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Bone {ECO:0000303|PubMed:16458082};
RX PubMed=16458082; DOI=10.1016/j.modgep.2005.11.010;
RA Gavaia P.J., Simes D.C., Ortiz-Delgado J.B., Viegas C.S., Pinto J.P.,
RA Kelsh R.N., Sarasquete M.C., Cancela M.L.;
RT "Osteocalcin and matrix Gla protein in zebrafish (Danio rerio) and Senegal
RT sole (Solea senegalensis): comparative gene and protein expression during
RT larval development through adulthood.";
RL Gene Expr. Patterns 6:637-652(2006).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 51-75.
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 -!- DEVELOPMENTAL STAGE: Detected in cleithrum from 8 days post
CC fertilization (DPF) onwards and in basioccipital articulatory process,
CC vertebrae and hypurals from 16, 15 and 22 DPF, respectively.
CC {ECO:0000269|PubMed:16458082}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAW30003.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AY823525; AAW30003.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q1EG28; -.
DR SMR; Q1EG28; -.
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 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; Metal-binding; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..50
FT /evidence="ECO:0000305|PubMed:24185858"
FT /id="PRO_0000436923"
FT CHAIN 51..95
FT /note="Osteocalcin 1"
FT /evidence="ECO:0000305"
FT /id="PRO_5007208183"
FT DOMAIN 45..91
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT MOD_RES 61
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q800Y1"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 68
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 67..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 95 AA; 10252 MW; 92F8333A42A4FCB7 CRC64;
MKTLSVLVLC SLAVLCLTSD ASFSSQPAVD TPAQEGLFVE QEQASSVVRQ APKELSLSQL
ESLREVCELN LACEDMMDTS GIIAAYTTYY GPIPF
