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Q6NSQ9

- G6PC3_MOUSE

UniProt

Q6NSQ9 - G6PC3_MOUSE

Protein

Glucose-6-phosphatase 3

Gene

G6pc3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. May form with the glucose-6-phosphate transporter (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose production through glycogenolysis and gluconeogenesis. Probably required for normal neutrophil function.4 Publications

    Catalytic activityi

    D-glucose 6-phosphate + H2O = D-glucose + phosphate.

    Enzyme regulationi

    Inhibited by vanadate.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791SubstrateSequence Analysis
    Active sitei114 – 1141Proton donorSequence Analysis
    Binding sitei161 – 1611SubstrateSequence Analysis
    Active sitei167 – 1671NucleophileBy similarity

    GO - Molecular functioni

    1. glucose-6-phosphatase activity Source: MGI

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. gluconeogenesis Source: UniProtKB-UniPathway
    3. glucose 6-phosphate metabolic process Source: Ensembl
    4. glucose-6-phosphate transport Source: MGI

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Gluconeogenesis

    Enzyme and pathway databases

    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucose-6-phosphatase 3 (EC:3.1.3.9)
    Short name:
    G-6-Pase 3
    Short name:
    G6Pase 3
    Alternative name(s):
    Ubiquitous glucose-6-phosphatase catalytic subunit-related protein
    Gene namesi
    Name:G6pc3
    Synonyms:Ugrp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1915651. G6pc3.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice display reduced glucose-6-phosphate hydrolytic activity in the brain. No phenotypic difference was noted at birth but 4 months old female mice display growth retardation. Mutant mice exhibit a decreased plasma cholesterol concentration and an increased plasma glucagon concentration but no difference in blood glucose concentration (PubMed:17023421). Mice display neutropenia and neutrophil dysfunctions.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 346346Glucose-6-phosphatase 3PRO_0000334513Add
    BLAST

    Proteomic databases

    PaxDbiQ6NSQ9.
    PRIDEiQ6NSQ9.

    PTM databases

    PhosphoSiteiQ6NSQ9.

    Expressioni

    Tissue specificityi

    Widely expressed. Highly expressed in heart, brain, kidney and testis and to a lower extent in lung, spleen, stomach, small intestine, skeletal muscle and uterus. Expressed in muscle, brain, thymus, lung, kidney, spleen and pancreas (at protein level).3 Publications

    Gene expression databases

    BgeeiQ6NSQ9.
    GenevestigatoriQ6NSQ9.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000077995.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NSQ9.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2424LumenalSequence AnalysisAdd
    BLAST
    Topological domaini46 – 5611CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini78 – 10831LumenalSequence AnalysisAdd
    BLAST
    Topological domaini130 – 1389CytoplasmicSequence Analysis
    Topological domaini160 – 1678LumenalSequence Analysis
    Topological domaini187 – 19711CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini219 – 25436LumenalSequence AnalysisAdd
    BLAST
    Topological domaini274 – 28310CytoplasmicSequence Analysis
    Topological domaini305 – 3073LumenalSequence Analysis
    Topological domaini329 – 34618CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei25 – 4521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei57 – 7721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei109 – 12921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei139 – 15921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei168 – 18619HelicalSequence AnalysisAdd
    BLAST
    Transmembranei198 – 21821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei255 – 27319HelicalSequence AnalysisAdd
    BLAST
    Transmembranei284 – 30421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei308 – 32821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glucose-6-phosphatase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG82628.
    GeneTreeiENSGT00510000046465.
    HOGENOMiHOG000264239.
    HOVERGENiHBG003560.
    InParanoidiQ6NSQ9.
    KOiK01084.
    OMAiKWFLFGD.
    OrthoDBiEOG73NG4N.
    PhylomeDBiQ6NSQ9.
    TreeFamiTF324388.

    Family and domain databases

    Gene3Di1.20.144.10. 1 hit.
    InterProiIPR016275. Glucose-6-phosphatase.
    IPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view]
    PfamiPF01569. PAP2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000905. Glucose-6-phosphatase. 1 hit.
    SMARTiSM00014. acidPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48317. SSF48317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q6NSQ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MESTLSAGII MAEALQNRLP GLENMWLWVT FLGDPKNLFQ FCFPAAYYAS    50
    RRLGISVLWI TFIAEWLNLV FKWFLFGDRP FWWVHESGYS TQTPIQIHQF 100
    PSSCETGPGS PSGHCMITGA ALWPVMTAIS SQVASRSRSP WVRVIPGLAY 150
    CTFLLAVGLS RVFLLAHFPH QVLGGLIVGA ALGWLMSPRV PMERELSFYG 200
    LTALALMLGA SLMYWTLFTL GLDLSWSINL ASKWCERPEW VHMDSRPFAS 250
    LSRDSGSALG LGIALHTPCY AQIRRAHLGN GQKIACFVLA MGLLVFLEWL 300
    GYPPQISLFY IFNFLKYTLW PCLVLALVPW VVHTLSDQEA PPIRSS 346
    Length:346
    Mass (Da):38,782
    Last modified:July 5, 2004 - v1
    Checksum:i50CDA634BCABA014
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361R → Q in BAE38159. (PubMed:16141072)Curated
    Sequence conflicti207 – 2071M → L in AAO39164. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY186239 mRNA. Translation: AAO39164.1.
    AK165395 mRNA. Translation: BAE38159.1.
    AL954730 Genomic DNA. Translation: CAM25070.1.
    BC069959 mRNA. Translation: AAH69959.1.
    CCDSiCCDS25491.1.
    RefSeqiNP_787949.2. NM_175935.3.
    UniGeneiMm.22385.

    Genome annotation databases

    EnsembliENSMUST00000070334; ENSMUSP00000064276; ENSMUSG00000034793.
    ENSMUST00000078975; ENSMUSP00000077995; ENSMUSG00000034793.
    GeneIDi68401.
    KEGGimmu:68401.
    UCSCiuc007lqt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY186239 mRNA. Translation: AAO39164.1 .
    AK165395 mRNA. Translation: BAE38159.1 .
    AL954730 Genomic DNA. Translation: CAM25070.1 .
    BC069959 mRNA. Translation: AAH69959.1 .
    CCDSi CCDS25491.1.
    RefSeqi NP_787949.2. NM_175935.3.
    UniGenei Mm.22385.

    3D structure databases

    ProteinModelPortali Q6NSQ9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000077995.

    PTM databases

    PhosphoSitei Q6NSQ9.

    Proteomic databases

    PaxDbi Q6NSQ9.
    PRIDEi Q6NSQ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000070334 ; ENSMUSP00000064276 ; ENSMUSG00000034793 .
    ENSMUST00000078975 ; ENSMUSP00000077995 ; ENSMUSG00000034793 .
    GeneIDi 68401.
    KEGGi mmu:68401.
    UCSCi uc007lqt.2. mouse.

    Organism-specific databases

    CTDi 92579.
    MGIi MGI:1915651. G6pc3.

    Phylogenomic databases

    eggNOGi NOG82628.
    GeneTreei ENSGT00510000046465.
    HOGENOMi HOG000264239.
    HOVERGENi HBG003560.
    InParanoidi Q6NSQ9.
    KOi K01084.
    OMAi KWFLFGD.
    OrthoDBi EOG73NG4N.
    PhylomeDBi Q6NSQ9.
    TreeFami TF324388.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .

    Miscellaneous databases

    NextBioi 327124.
    PROi Q6NSQ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6NSQ9.
    Genevestigatori Q6NSQ9.

    Family and domain databases

    Gene3Di 1.20.144.10. 1 hit.
    InterProi IPR016275. Glucose-6-phosphatase.
    IPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view ]
    Pfami PF01569. PAP2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000905. Glucose-6-phosphatase. 1 hit.
    SMARTi SM00014. acidPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48317. SSF48317. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a glucose-6-phosphatase catalytic subunit-related sequence expressed in rodent tissues."
      Middleditch C., Darakhshan F., Bonnefont J., Guionie O., Burchell A., Clottes E.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CD-1.
    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: Kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.
    5. "A potential new role for muscle in blood glucose homeostasis."
      Shieh J.-J., Pan C.-J., Mansfield B.C., Chou J.Y.
      J. Biol. Chem. 279:26215-26219(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    6. "Identification and characterization of a cDNA and the gene encoding the mouse ubiquitously expressed glucose-6-phosphatase catalytic subunit-related protein."
      Boustead J.N., Martin C.C., Oeser J.K., Svitek C.A., Hunter S.I., Hutton J.C., O'Brien R.M.
      J. Mol. Endocrinol. 32:33-53(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
    7. "Brain contains a functional glucose-6-phosphatase complex capable of endogenous glucose production."
      Ghosh A., Cheung Y.Y., Mansfield B.C., Chou J.Y.
      J. Biol. Chem. 280:11114-11119(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Deletion of the gene encoding the ubiquitously expressed glucose-6-phosphatase catalytic subunit-related protein (UGRP)/glucose-6-phosphatase catalytic subunit-beta results in lowered plasma cholesterol and elevated glucagon."
      Wang Y., Oeser J.K., Yang C., Sarkar S., Hackl S.I., Hasty A.H., McGuinness O.P., Paradee W., Hutton J.C., Powell D.R., O'Brien R.M.
      J. Biol. Chem. 281:39982-39989(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "Impaired neutrophil activity and increased susceptibility to bacterial infection in mice lacking glucose-6-phosphatase-beta."
      Cheung Y.Y., Kim S.Y., Yiu W.H., Pan C.-J., Jun H.-S., Ruef R.A., Lee E.J., Westphal H., Mansfield B.C., Chou J.Y.
      J. Clin. Invest. 117:784-793(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiG6PC3_MOUSE
    AccessioniPrimary (citable) accession number: Q6NSQ9
    Secondary accession number(s): Q3TND0, Q811R8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 20, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3