G6PC3_MOUSE
ID G6PC3_MOUSE Reviewed; 346 AA.
AC Q6NSQ9; Q3TND0; Q811R8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glucose-6-phosphatase 3;
DE Short=G-6-Pase 3;
DE Short=G6Pase 3;
DE EC=3.1.3.9 {ECO:0000269|PubMed:15661744};
DE AltName: Full=Ubiquitous glucose-6-phosphatase catalytic subunit-related protein;
DE AltName: Full=glucose-6-phosphatase-beta {ECO:0000303|PubMed:15661744};
DE Short=Glc-6-Pase-beta {ECO:0000303|PubMed:15661744};
GN Name=G6pc3; Synonyms=Ugrp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1;
RA Middleditch C., Darakhshan F., Bonnefont J., Guionie O., Burchell A.,
RA Clottes E.;
RT "Cloning of a glucose-6-phosphatase catalytic subunit-related sequence
RT expressed in rodent tissues.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15087461; DOI=10.1074/jbc.m402036200;
RA Shieh J.-J., Pan C.-J., Mansfield B.C., Chou J.Y.;
RT "A potential new role for muscle in blood glucose homeostasis.";
RL J. Biol. Chem. 279:26215-26219(2004).
RN [6]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=14765991; DOI=10.1677/jme.0.0320033;
RA Boustead J.N., Martin C.C., Oeser J.K., Svitek C.A., Hunter S.I.,
RA Hutton J.C., O'Brien R.M.;
RT "Identification and characterization of a cDNA and the gene encoding the
RT mouse ubiquitously expressed glucose-6-phosphatase catalytic subunit-
RT related protein.";
RL J. Mol. Endocrinol. 32:33-53(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=15661744; DOI=10.1074/jbc.m410894200;
RA Ghosh A., Cheung Y.Y., Mansfield B.C., Chou J.Y.;
RT "Brain contains a functional glucose-6-phosphatase complex capable of
RT endogenous glucose production.";
RL J. Biol. Chem. 280:11114-11119(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17023421; DOI=10.1074/jbc.m605858200;
RA Wang Y., Oeser J.K., Yang C., Sarkar S., Hackl S.I., Hasty A.H.,
RA McGuinness O.P., Paradee W., Hutton J.C., Powell D.R., O'Brien R.M.;
RT "Deletion of the gene encoding the ubiquitously expressed glucose-6-
RT phosphatase catalytic subunit-related protein (UGRP)/glucose-6-phosphatase
RT catalytic subunit-beta results in lowered plasma cholesterol and elevated
RT glucagon.";
RL J. Biol. Chem. 281:39982-39989(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17318259; DOI=10.1172/jci30443;
RA Cheung Y.Y., Kim S.Y., Yiu W.H., Pan C.-J., Jun H.-S., Ruef R.A., Lee E.J.,
RA Westphal H., Mansfield B.C., Chou J.Y.;
RT "Impaired neutrophil activity and increased susceptibility to bacterial
RT infection in mice lacking glucose-6-phosphatase-beta.";
RL J. Clin. Invest. 117:784-793(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic
CC reticulum. May form with the glucose-6-phosphate transporter
CC (SLC37A4/G6PT) a ubiquitously expressed complex responsible for glucose
CC production through glycogenolysis and gluconeogenesis. Probably
CC required for normal neutrophil function. {ECO:0000269|PubMed:15087461,
CC ECO:0000269|PubMed:15661744, ECO:0000269|PubMed:17023421,
CC ECO:0000269|PubMed:17318259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + H2O = D-glucose + phosphate;
CC Xref=Rhea:RHEA:16689, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:61548; EC=3.1.3.9;
CC Evidence={ECO:0000269|PubMed:15661744};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16690;
CC Evidence={ECO:0000269|PubMed:15661744};
CC -!- ACTIVITY REGULATION: Inhibited by vanadate.
CC {ECO:0000269|PubMed:15661744}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:15661744};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15661744};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in heart and
CC testis and to a lower extent in spleen, stomach, small intestine,
CC skeletal muscle and uterus. Expressed in muscle, brain, thymus, lung,
CC kidney, spleen and pancreas (at protein level). In the brain, expressed
CC in astrocytes (at protein level) (PubMed:15661744).
CC {ECO:0000269|PubMed:14765991, ECO:0000269|PubMed:15087461,
CC ECO:0000269|PubMed:15661744}.
CC -!- DISRUPTION PHENOTYPE: Mice display reduced glucose-6-phosphate
CC hydrolytic activity in the brain. No phenotypic difference was noted at
CC birth but 4 months old female mice display growth retardation. Mutant
CC mice exhibit a decreased plasma cholesterol concentration and an
CC increased plasma glucagon concentration but no difference in blood
CC glucose concentration (PubMed:17023421). Mice display neutropenia and
CC neutrophil dysfunctions. {ECO:0000269|PubMed:17023421,
CC ECO:0000269|PubMed:17318259}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}.
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DR EMBL; AY186239; AAO39164.1; -; mRNA.
DR EMBL; AK165395; BAE38159.1; -; mRNA.
DR EMBL; AL954730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069959; AAH69959.1; -; mRNA.
DR CCDS; CCDS25491.1; -.
DR RefSeq; NP_787949.2; NM_175935.3.
DR AlphaFoldDB; Q6NSQ9; -.
DR SMR; Q6NSQ9; -.
DR STRING; 10090.ENSMUSP00000077995; -.
DR iPTMnet; Q6NSQ9; -.
DR PhosphoSitePlus; Q6NSQ9; -.
DR SwissPalm; Q6NSQ9; -.
DR EPD; Q6NSQ9; -.
DR jPOST; Q6NSQ9; -.
DR MaxQB; Q6NSQ9; -.
DR PaxDb; Q6NSQ9; -.
DR PeptideAtlas; Q6NSQ9; -.
DR PRIDE; Q6NSQ9; -.
DR ProteomicsDB; 271628; -.
DR Antibodypedia; 59289; 80 antibodies from 17 providers.
DR DNASU; 68401; -.
DR Ensembl; ENSMUST00000070334; ENSMUSP00000064276; ENSMUSG00000034793.
DR Ensembl; ENSMUST00000078975; ENSMUSP00000077995; ENSMUSG00000034793.
DR GeneID; 68401; -.
DR KEGG; mmu:68401; -.
DR UCSC; uc007lqt.2; mouse.
DR CTD; 92579; -.
DR MGI; MGI:1915651; G6pc3.
DR VEuPathDB; HostDB:ENSMUSG00000034793; -.
DR eggNOG; ENOG502QS5D; Eukaryota.
DR GeneTree; ENSGT00950000183150; -.
DR HOGENOM; CLU_052517_0_0_1; -.
DR InParanoid; Q6NSQ9; -.
DR OMA; KKWCSRA; -.
DR OrthoDB; 743717at2759; -.
DR PhylomeDB; Q6NSQ9; -.
DR TreeFam; TF324388; -.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 68401; 2 hits in 71 CRISPR screens.
DR ChiTaRS; G6pc3; mouse.
DR PRO; PR:Q6NSQ9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6NSQ9; protein.
DR Bgee; ENSMUSG00000034793; Expressed in choroid plexus of fourth ventricle and 234 other tissues.
DR Genevisible; Q6NSQ9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:MGI.
DR GO; GO:0006094; P:gluconeogenesis; ISO:MGI.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IGI:MGI.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:MGI.
DR InterPro; IPR016275; Glucose-6-phosphatase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Gluconeogenesis; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..346
FT /note="Glucose-6-phosphatase 3"
FT /id="PRO_0000334513"
FT TOPO_DOM 1..24
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..108
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..167
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..254
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..307
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CONFLICT 136
FT /note="R -> Q (in Ref. 2; BAE38159)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="M -> L (in Ref. 1; AAO39164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38782 MW; 50CDA634BCABA014 CRC64;
MESTLSAGII MAEALQNRLP GLENMWLWVT FLGDPKNLFQ FCFPAAYYAS RRLGISVLWI
TFIAEWLNLV FKWFLFGDRP FWWVHESGYS TQTPIQIHQF PSSCETGPGS PSGHCMITGA
ALWPVMTAIS SQVASRSRSP WVRVIPGLAY CTFLLAVGLS RVFLLAHFPH QVLGGLIVGA
ALGWLMSPRV PMERELSFYG LTALALMLGA SLMYWTLFTL GLDLSWSINL ASKWCERPEW
VHMDSRPFAS LSRDSGSALG LGIALHTPCY AQIRRAHLGN GQKIACFVLA MGLLVFLEWL
GYPPQISLFY IFNFLKYTLW PCLVLALVPW VVHTLSDQEA PPIRSS
