VKGC_BOVIN
ID VKGC_BOVIN Reviewed; 758 AA.
AC Q07175;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 131.
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; Synonyms=GC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8506307; DOI=10.1073/pnas.90.10.4611;
RA Rehemtulla A., Roth D.A., Wasley L.C., Kuliopulos A., Walsh C.T., Furie B.,
RA Furie B.C., Kaufman R.J.;
RT "In vitro and in vivo functional characterization of bovine vitamin K-
RT dependent gamma-carboxylase expressed in Chinese hamster ovary cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4611-4615(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-758, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1749935; DOI=10.1126/science.1749935;
RA Wu S.-M., Cheung W.-F., Frazier D., Stafford D.W.;
RT "Cloning and expression of the cDNA for human gamma-glutamyl carboxylase.";
RL Science 254:1634-1636(1991).
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. May interact with CALU. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
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.
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DR EMBL; L09726; AAA30425.1; -; mRNA.
DR EMBL; M81593; AAA30410.1; -; mRNA.
DR PIR; A47439; A47439.
DR RefSeq; NP_776491.1; NM_174066.2.
DR AlphaFoldDB; Q07175; -.
DR STRING; 9913.ENSBTAP00000027811; -.
DR PaxDb; Q07175; -.
DR PeptideAtlas; Q07175; -.
DR PRIDE; Q07175; -.
DR Ensembl; ENSBTAT00000027811; ENSBTAP00000027811; ENSBTAG00000038477.
DR GeneID; 281190; -.
DR KEGG; bta:281190; -.
DR CTD; 2677; -.
DR VEuPathDB; HostDB:ENSBTAG00000038477; -.
DR VGNC; VGNC:29339; GGCX.
DR eggNOG; ENOG502QRU2; Eukaryota.
DR GeneTree; ENSGT00390000014909; -.
DR HOGENOM; CLU_020495_0_0_1; -.
DR InParanoid; Q07175; -.
DR OMA; TYLNHYY; -.
DR OrthoDB; 304818at2759; -.
DR TreeFam; TF323879; -.
DR BRENDA; 4.1.1.90; 908.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000038477; Expressed in liver and 106 other tissues.
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:0008488; F:gamma-glutamyl carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; IEA:InterPro.
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; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Lyase; Membrane; Reference proteome; Transmembrane;
KW 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_0000191821"
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..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..758
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..34
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; 87557 MW; 9B7F47B809D1A873 CRC64;
MAVSARPARA PRGSDKVKKD KAAQTSGPRQ GSRMGKLLGF EWTDVSSWER LVTLLNRPTD
PAGLAVFRFL FGLMMVLDIP QERGLSSLDR RYLDGLEVCR FPLLDALQPL PLDWMYLIYT
IMFLGALGMM LGLCYRISCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFVDAHHYW
SVDGLLRARK RNAHVPLWNY AVLRGQIFIV YFIAGIKKLD ADWVEGYSME YLSRHWLFSP
FKLVLSEEMT SLLVVHWCGL LLDLSAGFLL FFDASRPIGF VFVSYFHCMN SQLFSIGMFP
YVMLASSPLF CSPEWPRKLV AHCPKKLQEL LPLRTAPQPS TSCMYKRSRA RGSQKPGLRH
KLSTAFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGRT
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSRLLPKYNV TEPQIYFDIW VSINDRFQQR
IFDPRVDIVQ AAWSPFQRTP WLQPLLMDLS PWRTKLQEIK SSLDNHTEVV FIADFPGLHL
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLQEGEKMQ LPAGEYHKVY TVSSSPSCYM
YIYVNTTEVA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP EPTPLVQTFL
RRQQRLQEIE RRRNAPFHER LVRFLLRKLF IFRRSFLMTC ISLRNLAFGR PSLEQLAQEV
TYANLRPFEP AGEPSPVNTD SSNPNPPEPD SHPVHSEF
