VKGC_SHEEP
ID VKGC_SHEEP Reviewed; 758 AA.
AC Q9GL59;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA McCue J.M., Gordy P.W., Cantlon J.D., Baker D.C., Bowen R.A.;
RT "The sequence of the ovine gamma-carboxylase cDNA.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; AF312035; AAG30935.1; -; mRNA.
DR RefSeq; NP_001009750.1; NM_001009750.1.
DR AlphaFoldDB; Q9GL59; -.
DR STRING; 9940.ENSOARP00000022044; -.
DR Ensembl; ENSOART00020004469; ENSOARP00020003673; ENSOARG00020002878.
DR GeneID; 443129; -.
DR KEGG; oas:443129; -.
DR CTD; 2677; -.
DR eggNOG; ENOG502QRU2; Eukaryota.
DR OrthoDB; 304818at2759; -.
DR Proteomes; UP000002356; 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: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 2: Evidence at transcript 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_0000191827"
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..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..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; 87581 MW; 87F8B58C187B9091 CRC64;
MAVSARPARA PRGPDKVKKD KAAQTSGPRQ GSQMGKLLGF EWTDVSSWER LVTLLNRPTD
PASLAVFRFL FGLMMVLDIP QERGLSSLDR RYLDGLEVCR FPLLDALQPL PLDWMYLVYT
IMFLGALGMM LGLCYRISCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFVDAHHYW
SVDGLLRARK RNAHVPLWNY AVLRGQIFIV YFIAGIKKLD ADWVEGYSME YLSRHWLFSP
FKLVLSEEMT SLLVVHWCGL LLDLSAGFLL FFDASRPIGF VFVSYFHCMN SQLFSIGMFP
YVMLASSPLF CSPEWPRKLV AHCPKKLQEL LPLRTAPQPS TSCMYKRSRA RGSQKPGLRH
QLSTAFTLLY 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 RRRNAPFYER FVRFLLRKLF IFRRSFLMTC ISLRNLALGR PSLEQLAQEV
TYANLRPFEP AGEPSPVNTD SSNPNPPEPD SHPVHSEF
