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Vitamin K-dependent gamma-carboxylase (EC 4.1.1.90) (Gamma-glutamyl carboxylase) (Peptidyl-glutamate 4-carboxylase) (Vitamin K gamma glutamyl carboxylase)

 VKGC_RAT                Reviewed;         758 AA.
O88496;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
28-FEB-2018, entry version 111.
RecName: Full=Vitamin K-dependent gamma-carboxylase;
EC=4.1.1.90;
AltName: Full=Gamma-glutamyl carboxylase;
AltName: Full=Peptidyl-glutamate 4-carboxylase;
AltName: Full=Vitamin K gamma glutamyl carboxylase;
Name=Ggcx;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9704005; DOI=10.1006/bbrc.1998.8987;
Romero E.E., Deo R., Velazquez-Estades L.J., Roth D.A.;
"Cloning, structural organization, and transcriptional activity of the
rat vitamin K-dependent gamma-glutamyl carboxylase gene.";
Biochem. Biophys. Res. Commun. 248:783-788(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=9743593; DOI=10.1006/excr.1998.4151;
Romero E.E., Velazquez-Estades L.J., Deo R., Schapiro B., Roth D.A.;
"Cloning of rat vitamin K-dependent gamma-glutamyl carboxylase and
developmentally regulated gene expression in post-implantation
embryos.";
Exp. Cell Res. 243:334-346(1998).
[3]
INTERACTION WITH CALU.
PubMed=15075329; DOI=10.1074/jbc.M401645200;
Wajih N., Sane D.C., Hutson S.M., Wallin R.;
"The inhibitory effect of calumenin on the vitamin K-dependent gamma-
carboxylation system. Characterization of the system in normal and
warfarin-resistant rats.";
J. Biol. Chem. 279:25276-25283(2004).
-!- FUNCTION: Mediates the vitamin K-dependent carboxylation of
glutamate residues to calcium-binding gamma-carboxyglutamate (Gla)
residues with the concomitant conversion of the reduced
hydroquinone form of vitamin K to vitamin K epoxide.
-!- CATALYTIC ACTIVITY: [Peptidyl]-4-carboxyglutamate + 2,3-
epoxyphylloquinone + H(2)O = [peptidyl]-glutamate + CO(2) + O(2) +
phylloquinol.
-!- SUBUNIT: Monomer (By similarity). Interacts with CALU.
{ECO:0000250, ECO:0000269|PubMed:15075329}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- MISCELLANEOUS: The vitamin K-dependent protein substrates of
carboxylase have usually a propeptide that binds to a high-
affinity site on the carboxylase. CO(2), O(2) and reduced vitamin
K are cosubstrates.
-!- SIMILARITY: Belongs to the vitamin K-dependent gamma-carboxylase
family. {ECO:0000305}.
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EMBL; AF065387; AAC82374.1; -; mRNA.
RefSeq; NP_113944.1; NM_031756.1.
UniGene; Rn.22410; -.
SMR; O88496; -.
STRING; 10116.ENSRNOP00000017928; -.
ChEMBL; CHEMBL2744; -.
PaxDb; O88496; -.
PRIDE; O88496; -.
GeneID; 81716; -.
KEGG; rno:81716; -.
UCSC; RGD:68383; rat.
CTD; 2677; -.
RGD; 68383; Ggcx.
eggNOG; ENOG410IHG2; Eukaryota.
eggNOG; ENOG410XR5Q; LUCA.
HOGENOM; HOG000007593; -.
HOVERGEN; HBG012798; -.
InParanoid; O88496; -.
KO; K10106; -.
PhylomeDB; O88496; -.
BRENDA; 4.1.1.90; 5301.
PRO; PR:O88496; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0008488; F:gamma-glutamyl carboxylase activity; IDA:RGD.
GO; GO:0042277; F:peptide binding; IC:RGD.
GO; GO:0019842; F:vitamin binding; IDA:RGD.
GO; GO:0060437; P:lung growth; IEP:RGD.
GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; IDA:RGD.
GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
GO; GO:0010042; P:response to manganese ion; IEP:RGD.
GO; GO:0070482; P:response to oxygen levels; IEP:RGD.
GO; GO:0071107; P:response to parathyroid hormone; IEP:RGD.
GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
GO; GO:0032571; P:response to vitamin K; IEP:RGD.
InterPro; IPR011020; HTTM.
InterPro; IPR011051; RmlC_Cupin_sf.
InterPro; IPR007782; VKG_COase.
PANTHER; PTHR12639; PTHR12639; 1.
Pfam; PF05090; VKG_Carbox; 1.
SMART; SM00752; HTTM; 1.
SUPFAM; SSF51182; SSF51182; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Disulfide bond; Endoplasmic reticulum;
Lyase; Membrane; Reference proteome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P38435}.
CHAIN 2 758 Vitamin K-dependent gamma-carboxylase.
/FTId=PRO_0000191826.
TOPO_DOM 2 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TOPO_DOM 82 113 Lumenal. {ECO:0000255}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TOPO_DOM 135 136 Cytoplasmic. {ECO:0000255}.
TRANSMEM 137 157 Helical. {ECO:0000255}.
TOPO_DOM 158 292 Lumenal. {ECO:0000255}.
TRANSMEM 293 313 Helical. {ECO:0000255}.
TOPO_DOM 314 361 Cytoplasmic. {ECO:0000255}.
TRANSMEM 362 382 Helical. {ECO:0000255}.
TOPO_DOM 383 758 Lumenal. {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P38435}.
DISULFID 99 450 {ECO:0000250}.
SEQUENCE 758 AA; 87479 MW; 6CF2FC8DC96A71A1 CRC64;
MAVHRGSARA APASDKVQKN KPAQTSGLEQ GSRMARIFGF EWADLSSWQS VVTLLNRPTD
PANLAVFRFL FAFLMLLDIP QERGLSSLDR KYLDGLDVCR FPLLDALRPL PLDWMYLVYT
IMFLGALGMM LGLWYRLSCM LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW
SVDGLLSAQK KNAHVPLWNY TVLRGQIFIV YFIAGVKKLD ADWVEGYSME HLSRHWLFSP
FKLVLSEELT SLLVVHWCGL LLDLSAGFLL FFDASRPIGL VFVSYFHCMN SQLFSIGMFP
YVMLASSPLF CSAEWPRKLV ARCPKRLQEL LPAKAAPRPS ASCVYKRARA KAGQKPGLRH
HLGTVFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGLT
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSLLLPKYNV TEPQIYFDIW VSINDRFQQR
LFDPRVDIVQ AVWSPFRRTP WVQPLLMDLS PWRTKLQDIK SSLDNHTEVV FIADFPGLHL
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLREGEKMQ LPAGEYHKVY TVSSSPSCYM
YIYVNTTEVA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP EPTPLVQTFL
RRQRKLQEIE RRRNSPLHER FLRFVLRKLY VFRRSFLMTR ISLRNLLFGR PSLEQLAQEV
TYANLRPFEP VDESSASNTD SSDPHPSEPD SEHVHSEL


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