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Protein

Vitamin K-dependent gamma-carboxylase

Gene

Ggcx

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide.

Catalytic activityi

[Peptidyl]-4-carboxyglutamate + 2,3-epoxyphylloquinone + H2O = [peptidyl]-glutamate + CO2 + O2 + phylloquinone.

GO - Molecular functioni

  1. gamma-glutamyl carboxylase activity Source: MGI

GO - Biological processi

  1. peptidyl-glutamic acid carboxylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

ReactomeiREACT_281620. Gamma-carboxylation of protein precursors.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitamin K-dependent gamma-carboxylase (EC:4.1.1.90)
Alternative name(s):
Gamma-glutamyl carboxylase
Peptidyl-glutamate 4-carboxylase
Vitamin K gamma glutamyl carboxylase
Gene namesi
Name:Ggcx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1927655. Ggcx.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 6059CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Topological domaini82 – 11332LumenalSequence AnalysisAdd
BLAST
Transmembranei114 – 13421HelicalSequence AnalysisAdd
BLAST
Topological domaini135 – 1362CytoplasmicSequence Analysis
Transmembranei137 – 15721HelicalSequence AnalysisAdd
BLAST
Topological domaini158 – 292135LumenalSequence AnalysisAdd
BLAST
Transmembranei293 – 31321HelicalSequence AnalysisAdd
BLAST
Topological domaini314 – 36148CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei362 – 38221HelicalSequence AnalysisAdd
BLAST
Topological domaini383 – 757375LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 757756Vitamin K-dependent gamma-carboxylasePRO_0000191824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Disulfide bondi99 ↔ 450By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiQ9QYC7.
PaxDbiQ9QYC7.
PRIDEiQ9QYC7.

PTM databases

PhosphoSiteiQ9QYC7.

Expressioni

Gene expression databases

BgeeiQ9QYC7.
CleanExiMM_GGCX.
ExpressionAtlasiQ9QYC7. baseline and differential.
GenevestigatoriQ9QYC7.

Interactioni

Subunit structurei

Monomer. May interact with CALU.By similarity

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG83578.
GeneTreeiENSGT00390000014909.
HOGENOMiHOG000007593.
HOVERGENiHBG012798.
InParanoidiQ9QYC7.
KOiK10106.
OMAiSPSCYMY.
OrthoDBiEOG7B5WV9.
PhylomeDBiQ9QYC7.
TreeFamiTF323879.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR011020. HTTM.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR007782. VKG_COase.
[Graphical view]
PANTHERiPTHR12639. PTHR12639. 1 hit.
PfamiPF05090. VKG_Carbox. 1 hit.
[Graphical view]
SMARTiSM00752. HTTM. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QYC7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVHRGSALV APASDKVQKN KSAQTSGLKQ GSRMEKILGF EWTDLSSWQS
60 70 80 90 100
VVTLLNKPTD PANLAVFRFL FAFLMLLDIP QERGLSSLDR KYLDGLDVCR
110 120 130 140 150
FPLLDALRPL PLDWMYLVYT IMFLGALGMM LGLCYRLSCV LFLLPYWYVF
160 170 180 190 200
LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW SVDGLLNARK KNAHVPLWNY
210 220 230 240 250
TVLRGQIFIV YFIAGVKKLD ADWVGGYSME HLSRHWLFSP FKLVLSEELT
260 270 280 290 300
SLLVVHWCGL LLDLSAGFLL FFDASRPVGL FFVSYFHCMN SQLFSIGMFP
310 320 330 340 350
YVMLASSPLF CSAEWPRKLV ARCPKRLQEL LPTKAAPRPS ASCVYKRSRG
360 370 380 390 400
KAGPKPGLRH QLGAIFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD
410 420 430 440 450
MMVHSRSHQH VKITYRDGLT GELGYLNPGV FTQSRRWKDH ADMLKQYATC
460 470 480 490 500
LSLLLPKYNV TEPQIYFDIW VSINDRFQQR LFDPRVDIVQ AVWSPFQRTP
510 520 530 540 550
WVQPLLMDLS PWRTKLQDIK SSLDNHTEVV FIADFPGLHL ENFVSEDLGN
560 570 580 590 600
TSIQLLQGEV TVELVAEQKN QTLQEGEKMQ LPAGEYHKVY TVSSSPSCYM
610 620 630 640 650
YVYVNTTEVA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP
660 670 680 690 700
EPTPLVQTFL RRQRKLQEIE RRRNSPFHER FLRFVLRKLY VFRRSFLMTR
710 720 730 740 750
ISLRNLLLGR PSLEQLAQEV TYANLRPFEP VDESSASNTD SSNHPSEPDS

EHVHSEF
Length:757
Mass (Da):87,195
Last modified:May 1, 2000 - v1
Checksum:i178CDDCEE5CFBA34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti525 – 5251N → K in BAC28319 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087938 mRNA. Translation: AAF21291.1.
AK033496 mRNA. Translation: BAC28319.1.
AK036577 mRNA. Translation: BAC29487.1.
AK135425 mRNA. Translation: BAE22528.1.
CCDSiCCDS20242.1.
RefSeqiNP_062776.1. NM_019802.5.
UniGeneiMm.19937.

Genome annotation databases

EnsembliENSMUST00000065906; ENSMUSP00000070109; ENSMUSG00000053460.
ENSMUST00000194207; ENSMUSP00000141277; ENSMUSG00000103019.
GeneIDi56316.
KEGGimmu:56316.
UCSCiuc009cio.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087938 mRNA. Translation: AAF21291.1.
AK033496 mRNA. Translation: BAC28319.1.
AK036577 mRNA. Translation: BAC29487.1.
AK135425 mRNA. Translation: BAE22528.1.
CCDSiCCDS20242.1.
RefSeqiNP_062776.1. NM_019802.5.
UniGeneiMm.19937.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9QYC7.

Proteomic databases

MaxQBiQ9QYC7.
PaxDbiQ9QYC7.
PRIDEiQ9QYC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065906; ENSMUSP00000070109; ENSMUSG00000053460.
ENSMUST00000194207; ENSMUSP00000141277; ENSMUSG00000103019.
GeneIDi56316.
KEGGimmu:56316.
UCSCiuc009cio.1. mouse.

Organism-specific databases

CTDi2677.
MGIiMGI:1927655. Ggcx.

Phylogenomic databases

eggNOGiNOG83578.
GeneTreeiENSGT00390000014909.
HOGENOMiHOG000007593.
HOVERGENiHBG012798.
InParanoidiQ9QYC7.
KOiK10106.
OMAiSPSCYMY.
OrthoDBiEOG7B5WV9.
PhylomeDBiQ9QYC7.
TreeFamiTF323879.

Enzyme and pathway databases

ReactomeiREACT_281620. Gamma-carboxylation of protein precursors.

Miscellaneous databases

NextBioi312268.
PROiQ9QYC7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYC7.
CleanExiMM_GGCX.
ExpressionAtlasiQ9QYC7. baseline and differential.
GenevestigatoriQ9QYC7.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR011020. HTTM.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR007782. VKG_COase.
[Graphical view]
PANTHERiPTHR12639. PTHR12639. 1 hit.
PfamiPF05090. VKG_Carbox. 1 hit.
[Graphical view]
SMARTiSM00752. HTTM. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the mouse gamma-carboxylase genomic locus and its promoter."
    Zhu A., Zheng X., Ginsburg D.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone, Colon and Muellerian duct.

Entry informationi

Entry nameiVKGC_MOUSE
AccessioniPrimary (citable) accession number: Q9QYC7
Secondary accession number(s): Q3UXN5, Q8CCB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The vitamin K-dependent protein substrates of carboxylase have usually a propeptide that binds to a high-affinity site on the carboxylase. CO2, O2 and reduced vitamin K are cosubstrates.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.