VKGC_PONAB
ID VKGC_PONAB Reviewed; 758 AA.
AC Q5RF50;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857311; CAH89607.1; -; mRNA.
DR RefSeq; NP_001124716.1; NM_001131244.1.
DR AlphaFoldDB; Q5RF50; -.
DR STRING; 9601.ENSPPYP00000013637; -.
DR GeneID; 100171564; -.
DR KEGG; pon:100171564; -.
DR CTD; 2677; -.
DR eggNOG; ENOG502QRU2; Eukaryota.
DR InParanoid; Q5RF50; -.
DR OrthoDB; 304818at2759; -.
DR Proteomes; UP000001595; 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 Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR011020; HTTM.
DR InterPro; IPR014710; RmlC-like_jellyroll.
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_0000191825"
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..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..751
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; 87629 MW; B6F41E539BB578BC CRC64;
MAVSARSART SPGSDKVQKD KAELISGPRQ DSLMGKLLGF EWTDLSSWRR LVTLLNRPTD
PASLAVFRFL FGFLMVLDIP QERGLSSLDR KYLDGLDVCR FPLLDALRPL PLDWMYLVYT
IMFLGALGMM LGLCYRISCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW
SVDGLLNARR RNAHVPLWNY AVLRGQIFIV YFIAGVKKLD ADWVEGYSME YLSRHWLFSP
FKLLLSEELT SLLVVHWGGL LLDLSAGFLL FFDASRSIGL FFVSYFHCMN SQLFSIGMFS
YVMLASSPLF CSPEWPRKLV SYCPQRLQEL LPLKAAPQPS VSCVYKRSRG KSGQKPGLRH
QLGAAFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGRT
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSRLLPKYNV TEPQIYFDIW VSINDRFQQR
IFDPRVDIVQ AAWSPFQRTS WVQPLLMDLS PWRAKLQEIK SSLDNHTEVV FIADFPGLHL
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLREGEKMQ LPAGEYHKVY TTSPSPSCYM
YVYVNTTELA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP EPTPLVQTFL
RRQQRLQEIE RRRNTPFHER FFRFLLRKLY VFRRSFLMTC ISLRNLILGR PSLEQLAQEV
TYANLRPFEQ VGELSPSNMD SSHSNPPESN PDPVHSEF
