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Q9QYC7 (VKGC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ggcx
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Subunit structure

Monomer By similarity. May interact with CALU By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

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.

Sequence similarities

Belongs to the vitamin K-dependent gamma-carboxylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 757756Vitamin K-dependent gamma-carboxylase
PRO_0000191824

Regions

Topological domain2 – 6059Cytoplasmic Potential
Transmembrane61 – 8121Helical; Potential
Topological domain82 – 11332Lumenal Potential
Transmembrane114 – 13421Helical; Potential
Topological domain135 – 1362Cytoplasmic Potential
Transmembrane137 – 15721Helical; Potential
Topological domain158 – 292135Lumenal Potential
Transmembrane293 – 31321Helical; Potential
Topological domain314 – 36148Cytoplasmic Potential
Transmembrane362 – 38221Helical; Potential
Topological domain383 – 757375Lumenal Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Disulfide bond99 ↔ 450 By similarity

Experimental info

Sequence conflict5251N → K in BAC28319. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9QYC7 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 178CDDCEE5CFBA34

FASTA75787,195
        10         20         30         40         50         60 
MAVHRGSALV APASDKVQKN KSAQTSGLKQ GSRMEKILGF EWTDLSSWQS VVTLLNKPTD 

        70         80         90        100        110        120 
PANLAVFRFL FAFLMLLDIP QERGLSSLDR KYLDGLDVCR FPLLDALRPL PLDWMYLVYT 

       130        140        150        160        170        180 
IMFLGALGMM LGLCYRLSCV LFLLPYWYVF LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW 

       190        200        210        220        230        240 
SVDGLLNARK KNAHVPLWNY TVLRGQIFIV YFIAGVKKLD ADWVGGYSME HLSRHWLFSP 

       250        260        270        280        290        300 
FKLVLSEELT SLLVVHWCGL LLDLSAGFLL FFDASRPVGL FFVSYFHCMN SQLFSIGMFP 

       310        320        330        340        350        360 
YVMLASSPLF CSAEWPRKLV ARCPKRLQEL LPTKAAPRPS ASCVYKRSRG KAGPKPGLRH 

       370        380        390        400        410        420 
QLGAIFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD MMVHSRSHQH VKITYRDGLT 

       430        440        450        460        470        480 
GELGYLNPGV FTQSRRWKDH ADMLKQYATC LSLLLPKYNV TEPQIYFDIW VSINDRFQQR 

       490        500        510        520        530        540 
LFDPRVDIVQ AVWSPFQRTP WVQPLLMDLS PWRTKLQDIK SSLDNHTEVV FIADFPGLHL 

       550        560        570        580        590        600 
ENFVSEDLGN TSIQLLQGEV TVELVAEQKN QTLQEGEKMQ LPAGEYHKVY TVSSSPSCYM 

       610        620        630        640        650        660 
YVYVNTTEVA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP EPTPLVQTFL 

       670        680        690        700        710        720 
RRQRKLQEIE RRRNSPFHER FLRFVLRKLY VFRRSFLMTR ISLRNLLLGR PSLEQLAQEV 

       730        740        750 
TYANLRPFEP VDESSASNTD SSNHPSEPDS EHVHSEF

« Hide

References

« Hide 'large scale' references
[1]"Characterization of the mouse gamma-carboxylase genomic locus and its promoter."
Zhu A., Zheng X., Ginsburg D.
Submitted (AUG-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. expand/collapse author list , 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(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone, Colon and Muellerian duct.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF087938 mRNA. Translation: AAF21291.1.
AK033496 mRNA. Translation: BAC28319.1.
AK036577 mRNA. Translation: BAC29487.1.
AK135425 mRNA. Translation: BAE22528.1.
IPIIPI00136012.
RefSeqNP_062776.1. NM_019802.5.
UniGeneMm.19937.

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ9QYC7.

Proteomic databases

PaxDbQ9QYC7.
PRIDEQ9QYC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000065906; ENSMUSP00000070109; ENSMUSG00000053460.
GeneID56316.
KEGGmmu:56316.

Organism-specific databases

CTD2677.
MGIMGI:1927655. Ggcx.

Phylogenomic databases

eggNOGNOG83578.
GeneTreeENSGT00390000014909.
HOGENOMHOG000007593.
HOVERGENHBG012798.
InParanoidQ9QYC7.
KOK10106.
OMAMYVYVNT.
OrthoDBEOG4KH2TJ.

Gene expression databases

ArrayExpressQ9QYC7.
BgeeQ9QYC7.
CleanExMM_GGCX.
GenevestigatorQ9QYC7.
GermOnlineENSMUSG00000053460. Mus musculus.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
InterProIPR011020. HTTM.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
IPR007782. VKG_COase.
[Graphical view]
PANTHERPTHR12639. PTHR12639. 1 hit.
PfamPF05090. VKG_Carbox. 1 hit.
[Graphical view]
SMARTSM00752. HTTM. 1 hit.
[Graphical view]
SUPFAMSSF51182. RmlC_like_cupin. 1 hit.
ProtoNetSearch...

Other

NextBio312268.
SOURCESearch...

Entry information

Entry nameVKGC_MOUSE
AccessionPrimary (citable) accession number: Q9QYC7
Secondary accession number(s): Q3UXN5, Q8CCB3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 1, 2000
Last modified: April 3, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents