VKGC_MOUSE
ID VKGC_MOUSE Reviewed; 757 AA.
AC Q9QYC7; Q3UXN5; Q8CCB3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhu A., Zheng X., Ginsburg D.;
RT "Characterization of the mouse gamma-carboxylase genomic locus and its
RT promoter.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, Colon, and Muellerian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AF087938; AAF21291.1; -; mRNA.
DR EMBL; AK033496; BAC28319.1; -; mRNA.
DR EMBL; AK036577; BAC29487.1; -; mRNA.
DR EMBL; AK135425; BAE22528.1; -; mRNA.
DR CCDS; CCDS20242.1; -.
DR RefSeq; NP_062776.1; NM_019802.5.
DR AlphaFoldDB; Q9QYC7; -.
DR BioGRID; 207897; 5.
DR STRING; 10090.ENSMUSP00000070109; -.
DR iPTMnet; Q9QYC7; -.
DR PhosphoSitePlus; Q9QYC7; -.
DR jPOST; Q9QYC7; -.
DR MaxQB; Q9QYC7; -.
DR PaxDb; Q9QYC7; -.
DR PRIDE; Q9QYC7; -.
DR ProteomicsDB; 297960; -.
DR Antibodypedia; 16941; 287 antibodies from 35 providers.
DR DNASU; 56316; -.
DR Ensembl; ENSMUST00000065906; ENSMUSP00000070109; ENSMUSG00000053460.
DR GeneID; 56316; -.
DR KEGG; mmu:56316; -.
DR UCSC; uc009cio.2; mouse.
DR CTD; 2677; -.
DR MGI; MGI:1927655; Ggcx.
DR VEuPathDB; HostDB:ENSMUSG00000053460; -.
DR eggNOG; ENOG502QRU2; Eukaryota.
DR GeneTree; ENSGT00390000014909; -.
DR HOGENOM; CLU_020495_0_0_1; -.
DR InParanoid; Q9QYC7; -.
DR OMA; TYLNHYY; -.
DR OrthoDB; 304818at2759; -.
DR PhylomeDB; Q9QYC7; -.
DR TreeFam; TF323879; -.
DR Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
DR BioGRID-ORCS; 56316; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q9QYC7; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QYC7; protein.
DR Bgee; ENSMUSG00000053460; Expressed in humerus cartilage element and 107 other tissues.
DR ExpressionAtlas; Q9QYC7; baseline and differential.
DR Genevisible; Q9QYC7; MM.
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; ISO:MGI.
DR GO; GO:0008488; F:gamma-glutamyl carboxylase activity; ISS:MGI.
DR GO; GO:0019842; F:vitamin binding; ISO:MGI.
DR GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; ISO:MGI.
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..757
FT /note="Vitamin K-dependent gamma-carboxylase"
FT /id="PRO_0000191824"
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..757
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 729..757
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"
FT CONFLICT 525
FT /note="N -> K (in Ref. 2; BAC28319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 87195 MW; 178CDDCEE5CFBA34 CRC64;
MAVHRGSALV APASDKVQKN KSAQTSGLKQ GSRMEKILGF EWTDLSSWQS VVTLLNKPTD
PANLAVFRFL FAFLMLLDIP QERGLSSLDR KYLDGLDVCR FPLLDALRPL PLDWMYLVYT
IMFLGALGMM LGLCYRLSCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW
SVDGLLNARK KNAHVPLWNY TVLRGQIFIV YFIAGVKKLD ADWVGGYSME HLSRHWLFSP
FKLVLSEELT SLLVVHWCGL LLDLSAGFLL FFDASRPVGL FFVSYFHCMN SQLFSIGMFP
YVMLASSPLF CSAEWPRKLV ARCPKRLQEL LPTKAAPRPS ASCVYKRSRG KAGPKPGLRH
QLGAIFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGLT
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSLLLPKYNV TEPQIYFDIW VSINDRFQQR
LFDPRVDIVQ AVWSPFQRTP WVQPLLMDLS PWRTKLQDIK SSLDNHTEVV FIADFPGLHL
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLQEGEKMQ LPAGEYHKVY TVSSSPSCYM
YVYVNTTEVA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP EPTPLVQTFL
RRQRKLQEIE RRRNSPFHER FLRFVLRKLY VFRRSFLMTR ISLRNLLLGR PSLEQLAQEV
TYANLRPFEP VDESSASNTD SSNHPSEPDS EHVHSEF
