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Q9QYC7

- VKGC_MOUSE

UniProt

Q9QYC7 - VKGC_MOUSE

Protein

Vitamin K-dependent gamma-carboxylase

Gene

Ggcx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Lyase

    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: Chromosome 6

    Organism-specific databases

    MGIiMGI:1927655. Ggcx.

    Subcellular locationi

    GO - Cellular componenti

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

    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

    PaxDbiQ9QYC7.
    PRIDEiQ9QYC7.

    PTM databases

    PhosphoSiteiQ9QYC7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9QYC7.
    BgeeiQ9QYC7.
    CleanExiMM_GGCX.
    GenevestigatoriQ9QYC7.

    Interactioni

    Subunit structurei

    Monomer. May interact with CALU.By similarity

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 6059CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini82 – 11332LumenalSequence AnalysisAdd
    BLAST
    Topological domaini135 – 1362CytoplasmicSequence Analysis
    Topological domaini158 – 292135LumenalSequence AnalysisAdd
    BLAST
    Topological domaini314 – 36148CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini383 – 757375LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei61 – 8121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei114 – 13421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei137 – 15721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei293 – 31321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei362 – 38221HelicalSequence AnalysisAdd
    BLAST

    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

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    MAVHRGSALV APASDKVQKN KSAQTSGLKQ GSRMEKILGF EWTDLSSWQS    50
    VVTLLNKPTD PANLAVFRFL FAFLMLLDIP QERGLSSLDR KYLDGLDVCR 100
    FPLLDALRPL PLDWMYLVYT IMFLGALGMM LGLCYRLSCV LFLLPYWYVF 150
    LLDKTSWNNH SYLYGLLAFQ LTFMDANHYW SVDGLLNARK KNAHVPLWNY 200
    TVLRGQIFIV YFIAGVKKLD ADWVGGYSME HLSRHWLFSP FKLVLSEELT 250
    SLLVVHWCGL LLDLSAGFLL FFDASRPVGL FFVSYFHCMN SQLFSIGMFP 300
    YVMLASSPLF CSAEWPRKLV ARCPKRLQEL LPTKAAPRPS ASCVYKRSRG 350
    KAGPKPGLRH QLGAIFTLLY LLEQLFLPYS HFLTQGYNNW TNGLYGYSWD 400
    MMVHSRSHQH VKITYRDGLT GELGYLNPGV FTQSRRWKDH ADMLKQYATC 450
    LSLLLPKYNV TEPQIYFDIW VSINDRFQQR LFDPRVDIVQ AVWSPFQRTP 500
    WVQPLLMDLS PWRTKLQDIK SSLDNHTEVV FIADFPGLHL ENFVSEDLGN 550
    TSIQLLQGEV TVELVAEQKN QTLQEGEKMQ LPAGEYHKVY TVSSSPSCYM 600
    YVYVNTTEVA LEQDLAYLQE LKEKVENGSE TGPLPPELQP LLEGEVKGGP 650
    EPTPLVQTFL RRQRKLQEIE RRRNSPFHER FLRFVLRKLY VFRRSFLMTR 700
    ISLRNLLLGR PSLEQLAQEV TYANLRPFEP VDESSASNTD SSNHPSEPDS 750
    EHVHSEF 757
    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:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi56316.
    KEGGimmu:56316.
    UCSCiuc009cio.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087938 mRNA. Translation: AAF21291.1 .
    AK033496 mRNA. Translation: BAC28319.1 .
    AK036577 mRNA. Translation: BAC29487.1 .
    AK135425 mRNA. Translation: BAE22528.1 .
    CCDSi CCDS20242.1.
    RefSeqi NP_062776.1. NM_019802.5.
    UniGenei Mm.19937.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9QYC7.

    Proteomic databases

    PaxDbi Q9QYC7.
    PRIDEi Q9QYC7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000065906 ; ENSMUSP00000070109 ; ENSMUSG00000053460 .
    GeneIDi 56316.
    KEGGi mmu:56316.
    UCSCi uc009cio.1. mouse.

    Organism-specific databases

    CTDi 2677.
    MGIi MGI:1927655. Ggcx.

    Phylogenomic databases

    eggNOGi NOG83578.
    GeneTreei ENSGT00390000014909.
    HOGENOMi HOG000007593.
    HOVERGENi HBG012798.
    InParanoidi Q9QYC7.
    KOi K10106.
    OMAi SPSCYMY.
    OrthoDBi EOG7B5WV9.
    PhylomeDBi Q9QYC7.
    TreeFami TF323879.

    Miscellaneous databases

    NextBioi 312268.
    PROi Q9QYC7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QYC7.
    Bgeei Q9QYC7.
    CleanExi MM_GGCX.
    Genevestigatori Q9QYC7.

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    InterProi IPR011020. HTTM.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    IPR007782. VKG_COase.
    [Graphical view ]
    PANTHERi PTHR12639. PTHR12639. 1 hit.
    Pfami PF05090. VKG_Carbox. 1 hit.
    [Graphical view ]
    SMARTi SM00752. HTTM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51182. SSF51182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 98 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