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Reviewed, UniProtKB/Swiss-Prot Q6NSQ9 (G6PC3_MOUSE)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucose-6-phosphatase 3
      Short name=G-6-Pase 3
      Short name=G6Pase 3
    EC=3.1.3.9
Alternative name(s):
    Ubiquitous glucose-6-phosphatase catalytic subunit-related protein
Gene names
Name: G6pc3
Synonyms: Ugrp
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.5 Ref.7 Ref.8 Ref.9

Catalytic activity

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

Enzyme regulation

Inhibited by vanadate By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subcellular location

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

Tissue specificity

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). Ref.5 Ref.7 Ref.6

Disruption phenotype

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 (Ref.8). Mice display neutropenia and neutrophil dysfunctions. Ref.8 Ref.9

Sequence similarities

Belongs to the glucose-6-phosphatase family.

Ontologies

Keywords
   Biological processGluconeogenesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   Molecular functionHydrolase
Gene Ontology (GO)
   Biological processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glucose-6-phosphate transport Ref.7

Inferred from genetic interaction. Source: MGI

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglucose-6-phosphatase activity Ref.7

Inferred from direct assay. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Glucose-6-phosphatase 3
PRO_0000334513

Regions

Topological domain1 – 2424Lumenal Potential
Transmembrane25 – 4521 Potential
Topological domain46 – 5611Cytoplasmic Potential
Transmembrane57 – 7721 Potential
Topological domain78 – 10831Lumenal Potential
Transmembrane109 – 12921 Potential
Topological domain130 – 1389Cytoplasmic Potential
Transmembrane139 – 15921 Potential
Topological domain160 – 1678Lumenal Potential
Transmembrane168 – 18619 Potential
Topological domain187 – 19711Cytoplasmic Potential
Transmembrane198 – 21821 Potential
Topological domain219 – 25436Lumenal Potential
Transmembrane255 – 27319 Potential
Topological domain274 – 28310Cytoplasmic Potential
Transmembrane284 – 30421 Potential
Topological domain305 – 3073Lumenal Potential
Transmembrane308 – 32821 Potential
Topological domain329 – 34618Cytoplasmic Potential

Sites

Active site1141Proton donor Potential
Active site1671Nucleophile By similarity
Binding site791Substrate Potential
Binding site1611Substrate Potential

Experimental info

Sequence conflict1361R → Q in BAE38159. Ref.2
Sequence conflict2071M → L in AAO39164. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6NSQ9-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 50CDA634BCABA014

FASTA34638,782
        10         20         30         40         50         60 
MESTLSAGII MAEALQNRLP GLENMWLWVT FLGDPKNLFQ FCFPAAYYAS RRLGISVLWI 

        70         80         90        100        110        120 
TFIAEWLNLV FKWFLFGDRP FWWVHESGYS TQTPIQIHQF PSSCETGPGS PSGHCMITGA 

       130        140        150        160        170        180 
ALWPVMTAIS SQVASRSRSP WVRVIPGLAY CTFLLAVGLS RVFLLAHFPH QVLGGLIVGA 

       190        200        210        220        230        240 
ALGWLMSPRV PMERELSFYG LTALALMLGA SLMYWTLFTL GLDLSWSINL ASKWCERPEW 

       250        260        270        280        290        300 
VHMDSRPFAS LSRDSGSALG LGIALHTPCY AQIRRAHLGN GQKIACFVLA MGLLVFLEWL 

       310        320        330        340 
GYPPQISLFY IFNFLKYTLW PCLVLALVPW VVHTLSDQEA PPIRSS 

« Hide

References

« Hide 'large scale' references
[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. 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[3]The mouse genome sequencing consortium
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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: 15087461] [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: 14765991] [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: 15661744] [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: 17023421] [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: 17318259] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

AY186239 mRNA. Translation: AAO39164.1.
AK165395 mRNA. Translation: BAE38159.1.
AL954730 Genomic DNA. Translation: CAM25070.1.
BC069959 mRNA. Translation: AAH69959.1.
IPIIPI00421041.
RefSeqNP_787949.2.
UniGeneMm.22385

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000034793. Mus musculus. [Contig view]
GeneID68401.
KEGGmmu:68401.

Organism-specific databases

MGIMGI:1915651. G6pc3.

Phylogenomic databases

HOVERGENQ6NSQ9.
OMAQ6NSQ9. GIAVLWI.

Gene expression databases

ArrayExpressQ6NSQ9.
BgeeQ6NSQ9.

Family and domain databases

InterProIPR016275. Glucose-6-phosphatase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
PIRSFPIRSF000905. Glucose-6-phosphatase. 1 hit.
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio327124.
SOURCESearch...

Entry information

Entry nameG6PC3_MOUSE
AccessionPrimary (citable) accession number: Q6NSQ9
Secondary accession number(s): Q3TND0, Q811R8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 5, 2004
Last modified: June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents