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Glucose-6-phosphatase (G-6-Pase) (G6Pase) (EC 3.1.3.9)

 G6PC_MOUSE              Reviewed;         357 AA.
P35576; Q91WV3;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 140.
RecName: Full=Glucose-6-phosphatase;
Short=G-6-Pase;
Short=G6Pase;
EC=3.1.3.9;
Name=G6pc; Synonyms=G6pt;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8407995;
Shelly L.L., Lei K.-J., Pan C.-J., Sakata S.F., Ruppert S., Schutz G.,
Chou J.Y.;
"Isolation of the gene for murine glucose-6-phosphatase, the enzyme
deficient in glycogen storage disease type 1A.";
J. Biol. Chem. 268:21482-21485(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
STRAIN=129/Sv; TISSUE=Liver;
PubMed=9115220; DOI=10.1074/jbc.272.18.11698;
Streeper R.S., Svitek C.A., Chapman S., Greenbaum L.E., Taub R.,
O'Brien R.M.;
"A multicomponent insulin response sequence mediates a strong
repression of mouse glucose-6-phosphatase gene transcription by
insulin.";
J. Biol. Chem. 272:11698-11701(1997).
[6]
FUNCTION.
PubMed=8640227; DOI=10.1038/ng0696-203;
Lei K.-J., Chen H., Pan C.-J., Ward J.M., Mosinger B. Jr., Lee E.J.,
Westphal H., Mansfield B.C., Chou J.Y.;
"Glucose-6-phosphatase dependent substrate transport in the glycogen
storage disease type-1a mouse.";
Nat. Genet. 13:203-209(1996).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the
endoplasmic reticulum. Forms with the glucose-6-phosphate
transporter (SLC37A4/G6PT) the complex responsible for glucose
production through glycogenolysis and gluconeogenesis. Hence, it
is the key enzyme in homeostatic regulation of blood glucose
levels. {ECO:0000269|PubMed:8640227}.
-!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + H(2)O = D-glucose +
phosphate.
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- TISSUE SPECIFICITY: Liver and kidney.
-!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
{ECO:0000305}.
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EMBL; U00445; AAC52122.1; -; mRNA.
EMBL; U91573; AAC53166.1; -; Genomic_DNA.
EMBL; AK050279; BAC34162.1; -; mRNA.
EMBL; AK052656; BAC35084.1; -; mRNA.
EMBL; AL590969; CAM19548.1; -; Genomic_DNA.
EMBL; BC013448; AAH13448.1; -; mRNA.
CCDS; CCDS25466.1; -.
PIR; A48589; A48589.
RefSeq; NP_032087.2; NM_008061.4.
UniGene; Mm.18064; -.
ProteinModelPortal; P35576; -.
STRING; 10090.ENSMUSP00000019469; -.
PhosphoSitePlus; P35576; -.
SwissPalm; P35576; -.
MaxQB; P35576; -.
PaxDb; P35576; -.
PRIDE; P35576; -.
Ensembl; ENSMUST00000019469; ENSMUSP00000019469; ENSMUSG00000078650.
GeneID; 14377; -.
KEGG; mmu:14377; -.
UCSC; uc007lor.1; mouse.
CTD; 2538; -.
MGI; MGI:95607; G6pc.
eggNOG; ENOG410IDXG; Eukaryota.
eggNOG; ENOG4110AJ7; LUCA.
GeneTree; ENSGT00510000046465; -.
HOGENOM; HOG000264239; -.
HOVERGEN; HBG003560; -.
InParanoid; P35576; -.
KO; K01084; -.
OMA; YLQVNYQ; -.
OrthoDB; EOG091G0AXF; -.
TreeFam; TF324388; -.
BRENDA; 3.1.3.9; 3474.
Reactome; R-MMU-70263; Gluconeogenesis.
UniPathway; UPA00138; -.
ChiTaRS; G6pc; mouse.
PRO; PR:P35576; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000078650; Expressed in 44 organ(s), highest expression level in adult mammalian kidney.
CleanEx; MM_G6PC; -.
Genevisible; P35576; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:MGI.
GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:MGI.
GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
GO; GO:0006094; P:gluconeogenesis; ISO:MGI.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0015760; P:glucose-6-phosphate transport; IDA:MGI.
GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:MGI.
GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0008202; P:steroid metabolic process; IMP:MGI.
GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
GO; GO:0046415; P:urate metabolic process; IMP:MGI.
InterPro; IPR016275; Glucose-6-phosphatase.
InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
Pfam; PF01569; PAP2; 1.
PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
SMART; SM00014; acidPPc; 1.
SUPFAM; SSF48317; SSF48317; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Gluconeogenesis;
Glycoprotein; Hydrolase; Membrane; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 357 Glucose-6-phosphatase.
/FTId=PRO_0000087414.
TOPO_DOM 1 28 Lumenal. {ECO:0000255}.
TRANSMEM 29 49 Helical. {ECO:0000255}.
TOPO_DOM 50 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical. {ECO:0000255}.
TOPO_DOM 82 117 Lumenal. {ECO:0000255}.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TOPO_DOM 139 147 Cytoplasmic. {ECO:0000255}.
TRANSMEM 148 168 Helical. {ECO:0000255}.
TOPO_DOM 169 179 Lumenal. {ECO:0000255}.
TRANSMEM 180 202 Helical. {ECO:0000255}.
TOPO_DOM 203 211 Cytoplasmic. {ECO:0000255}.
TRANSMEM 212 232 Helical. {ECO:0000255}.
TOPO_DOM 233 254 Lumenal. {ECO:0000255}.
TRANSMEM 255 275 Helical. {ECO:0000255}.
TOPO_DOM 276 291 Cytoplasmic. {ECO:0000255}.
TRANSMEM 292 312 Helical. {ECO:0000255}.
TOPO_DOM 313 320 Lumenal. {ECO:0000255}.
TRANSMEM 321 341 Helical. {ECO:0000255}.
TOPO_DOM 342 357 Cytoplasmic. {ECO:0000255}.
MOTIF 354 357 Prevents secretion from ER.
{ECO:0000255}.
ACT_SITE 119 119 Proton donor. {ECO:0000255}.
ACT_SITE 176 176 Nucleophile. {ECO:0000250}.
BINDING 83 83 Substrate. {ECO:0000255}.
BINDING 170 170 Substrate. {ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CONFLICT 291 292 LL -> SF (in Ref. 1; AAC52122).
{ECO:0000305}.
SEQUENCE 357 AA; 40473 MW; 292163ACA7A44402 CRC64;
MEEGMNILHD FGIQSTRYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLKETVGIN
LLWVAVVGDW FNLVFKWILF GQRPYWWVLD TDYYSNSSVP IIKQFPVTCE TGPGSPSGHA
MGAAGVYYVM VTSTLAIFRG KKKPTYGFRC LNVILWLGFW AVQLNVCLSR IYLAAHFPHQ
VVAGVLSGIA VAETFSHIRG IYNASLRKYC LITIFLFGFA LGFYLLLKGL GVDLLWTLEK
AKRWCERPEW VHLDTTPFAS LFKNLGTLLG LGLALNSSMY RKSCKGELSK LLPFRFACIV
ASLVLLHLFD SLKPPSQVEL IFYILSFCKS ATVPFASVSL IPYCLARILG QTHKKSL


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