VKGC_RAT
ID VKGC_RAT Reviewed; 758 AA.
AC O88496;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Vitamin K-dependent gamma-carboxylase;
DE EC=4.1.1.90;
DE AltName: Full=Gamma-glutamyl carboxylase;
DE AltName: Full=Peptidyl-glutamate 4-carboxylase;
DE AltName: Full=Vitamin K gamma glutamyl carboxylase;
GN Name=Ggcx;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9704005; DOI=10.1006/bbrc.1998.8987;
RA Romero E.E., Deo R., Velazquez-Estades L.J., Roth D.A.;
RT "Cloning, structural organization, and transcriptional activity of the rat
RT vitamin K-dependent gamma-glutamyl carboxylase gene.";
RL Biochem. Biophys. Res. Commun. 248:783-788(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9743593; DOI=10.1006/excr.1998.4151;
RA Romero E.E., Velazquez-Estades L.J., Deo R., Schapiro B., Roth D.A.;
RT "Cloning of rat vitamin K-dependent gamma-glutamyl carboxylase and
RT developmentally regulated gene expression in post-implantation embryos.";
RL Exp. Cell Res. 243:334-346(1998).
RN [3]
RP INTERACTION WITH CALU.
RX PubMed=15075329; DOI=10.1074/jbc.m401645200;
RA Wajih N., Sane D.C., Hutson S.M., Wallin R.;
RT "The inhibitory effect of calumenin on the vitamin K-dependent gamma-
RT carboxylation system. Characterization of the system in normal and
RT warfarin-resistant rats.";
RL J. Biol. Chem. 279:25276-25283(2004).
CC -!- FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate
CC residues to calcium-binding gamma-carboxyglutamate (Gla) residues with
CC the concomitant conversion of the reduced hydroquinone form of vitamin
CC K to vitamin K epoxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+)
CC + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol;
CC Xref=Rhea:RHEA:45140, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:11094,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15759, ChEBI:CHEBI:16526, ChEBI:CHEBI:28433,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:84990; EC=4.1.1.90;
CC -!- SUBUNIT: Monomer (By similarity). Interacts with CALU. {ECO:0000250,
CC ECO:0000269|PubMed:15075329}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: The vitamin K-dependent protein substrates of
CC carboxylase have usually a propeptide that binds to a high-affinity
CC site on the carboxylase. CO(2), O(2) and reduced vitamin K are
CC cosubstrates.
CC -!- SIMILARITY: Belongs to the vitamin K-dependent gamma-carboxylase
CC family. {ECO:0000305}.
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DR EMBL; AF065387; AAC82374.1; -; mRNA.
DR RefSeq; NP_113944.1; NM_031756.1.
DR AlphaFoldDB; O88496; -.
DR STRING; 10116.ENSRNOP00000017928; -.
DR ChEMBL; CHEMBL2744; -.
DR jPOST; O88496; -.
DR PaxDb; O88496; -.
DR GeneID; 81716; -.
DR KEGG; rno:81716; -.
DR UCSC; RGD:68383; rat.
DR CTD; 2677; -.
DR RGD; 68383; Ggcx.
DR eggNOG; ENOG502QRU2; Eukaryota.
DR InParanoid; O88496; -.
DR OrthoDB; 304818at2759; -.
DR PhylomeDB; O88496; -.
DR BRENDA; 4.1.1.90; 5301.
DR Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
DR PRO; PR:O88496; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0008488; F:gamma-glutamyl carboxylase activity; IDA:RGD.
DR GO; GO:0042277; F:peptide binding; IC:RGD.
DR GO; GO:0019842; F:vitamin binding; IDA:RGD.
DR GO; GO:0060437; P:lung growth; IEP:RGD.
DR GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; IDA:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR GO; GO:0010042; P:response to manganese ion; IEP:RGD.
DR GO; GO:0070482; P:response to oxygen levels; IEP:RGD.
DR GO; GO:0071107; P:response to parathyroid hormone; IEP:RGD.
DR GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR GO; GO:0032571; P:response to vitamin K; IEP:RGD.
DR InterPro; IPR011020; HTTM.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR InterPro; IPR007782; VKG_COase.
DR PANTHER; PTHR12639; PTHR12639; 1.
DR Pfam; PF05090; VKG_Carbox; 1.
DR SMART; SM00752; HTTM; 1.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 1: Evidence at protein level;
KW Acetylation; Disulfide bond; Endoplasmic reticulum; Lyase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P38435"
FT CHAIN 2..758
FT /note="Vitamin K-dependent gamma-carboxylase"
FT /id="PRO_0000191826"
FT TOPO_DOM 2..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..113
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..292
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..758
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P38435"
FT DISULFID 99..450
FT /evidence="ECO:0000250"
SQ 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
