VKGC_DELLE
ID VKGC_DELLE Reviewed; 758 AA.
AC Q9MYY3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 76.
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 Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10893417; DOI=10.1074/jbc.m003944200;
RA Begley G.S., Furie B.C., Czerwiec E., Taylor K.L., Furie G.L.,
RA Bronstein L., Stenflo J., Furie B.;
RT "A conserved motif within the vitamin K-dependent carboxylase gene is
RT widely distributed across animal phyla.";
RL J. Biol. Chem. 275:36245-36249(2000).
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; AF278713; AAF82125.1; -; mRNA.
DR AlphaFoldDB; Q9MYY3; -.
DR STRING; 9749.Q9MYY3; -.
DR Ensembl; ENSDLET00000024504; ENSDLEP00000022264; ENSDLEG00000016129.
DR OrthoDB; 304818at2759; -.
DR Proteomes; UP000248483; 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_0000191822"
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..31
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 COMPBIAS 734..750
FT /note="Polar residues"
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; 87510 MW; 6F5650A1882B4D3A CRC64;
MAVSARSARS PPDSDKVQKD KAGQTSGRRQ GSRMGKLLGF EWTDVSSWGK LVTLLNRPTD
PASLAVFRFL FGLMMVLDIP QERGLSSLDR RYLDGLEVCR FPLLDALQPL PLDWMYLVYT
IMFLGALGMM LGLRYRISCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFMDANRYW
SVDGLLSARK RNAHVPLWNY AVLRGQIFIV YFIAGVKKLD ADWVEGYSME YLSRHWLFSP
FKFVLSEEMT SLLVVHWCGL LLDLSAGFLL FFDASRSIGL LFVSYFHCMN SQLFSIGMFP
YVMLASSPLF CSPEWPRKLV AHCPKRLQEL LPLRTAPQPS ASCVYKRSRA KGGQKPGLRH
RLGAAFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGRT
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSRLLPKYNV TEPQIYFDIW VSINDRFQQR
IFDPRVDIVQ ATWSPFQRTP WLQPLLMDLS PWRTKLQEIK SSLDNHTEVV FIADFPGLHL
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLQEGEKMQ LPAGEYHKVY TMSPSPSCYM
YIYVNTTELA LEQDLAYLQE LKEKVENGSE TEPLPPELQP LLEGEVKGGP EPTPLVQTFL
RRQQRLQEIE RRRNAPFHER LLRFLLRKLY VFRRSFLMTC ISLRNLVLGR PSLEQLAQEV
TYANLRPFEP VGEPSPSNTD SSNPNPSEPN ADAVHSEF
