G6PC1_MOUSE
ID G6PC1_MOUSE Reviewed; 357 AA.
AC P35576; Q91WV3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Glucose-6-phosphatase catalytic subunit 1;
DE EC=3.1.3.9 {ECO:0000269|PubMed:8407995};
DE AltName: Full=Glucose-6-phosphatase;
DE Short=G-6-Pase;
DE Short=G6Pase;
GN Name=G6pc1; Synonyms=G6pc, G6pt;
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], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=8407995; DOI=10.1016/s0021-9258(20)80563-8;
RA Shelly L.L., Lei K.-J., Pan C.-J., Sakata S.F., Ruppert S., Schutz G.,
RA Chou J.Y.;
RT "Isolation of the gene for murine glucose-6-phosphatase, the enzyme
RT deficient in glycogen storage disease type 1A.";
RL J. Biol. Chem. 268:21482-21485(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
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=Kidney;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=9115220; DOI=10.1074/jbc.272.18.11698;
RA Streeper R.S., Svitek C.A., Chapman S., Greenbaum L.E., Taub R.,
RA O'Brien R.M.;
RT "A multicomponent insulin response sequence mediates a strong repression of
RT mouse glucose-6-phosphatase gene transcription by insulin.";
RL J. Biol. Chem. 272:11698-11701(1997).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8640227; DOI=10.1038/ng0696-203;
RA Lei K.-J., Chen H., Pan C.-J., Ward J.M., Mosinger B. Jr., Lee E.J.,
RA Westphal H., Mansfield B.C., Chou J.Y.;
RT "Glucose-6-phosphatase dependent substrate transport in the glycogen
RT storage disease type-1a mouse.";
RL Nat. Genet. 13:203-209(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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. Forms with the glucose-6-phosphate transporter
CC (SLC37A4/G6PT) the complex responsible for glucose production in the
CC terminal step of glycogenolysis and gluconeogenesis. Hence, it is the
CC key enzyme in homeostatic regulation of blood glucose levels.
CC {ECO:0000269|PubMed:8407995, ECO:0000269|PubMed:8640227}.
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:8407995};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000305|PubMed:8407995}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P35575}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver and kidney.
CC -!- DISRUPTION PHENOTYPE: Deficient mice display hypoglycaemia, growth
CC retardation, hepatomegaly, kidney enlargement, hyperlipidaemia, and
CC hyperuricaemia. {ECO:0000269|PubMed:8640227}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}.
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DR EMBL; U00445; AAC52122.1; -; mRNA.
DR EMBL; U91573; AAC53166.1; -; Genomic_DNA.
DR EMBL; AK050279; BAC34162.1; -; mRNA.
DR EMBL; AK052656; BAC35084.1; -; mRNA.
DR EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013448; AAH13448.1; -; mRNA.
DR CCDS; CCDS25466.1; -.
DR PIR; A48589; A48589.
DR RefSeq; NP_032087.2; NM_008061.4.
DR AlphaFoldDB; P35576; -.
DR STRING; 10090.ENSMUSP00000019469; -.
DR GlyGen; P35576; 1 site.
DR PhosphoSitePlus; P35576; -.
DR SwissPalm; P35576; -.
DR jPOST; P35576; -.
DR MaxQB; P35576; -.
DR PaxDb; P35576; -.
DR PRIDE; P35576; -.
DR ProteomicsDB; 271629; -.
DR Antibodypedia; 29454; 137 antibodies from 24 providers.
DR DNASU; 14377; -.
DR Ensembl; ENSMUST00000019469; ENSMUSP00000019469; ENSMUSG00000078650.
DR GeneID; 14377; -.
DR KEGG; mmu:14377; -.
DR UCSC; uc007lor.1; mouse.
DR CTD; 14377; -.
DR MGI; MGI:95607; G6pc.
DR VEuPathDB; HostDB:ENSMUSG00000078650; -.
DR eggNOG; ENOG502QS9B; Eukaryota.
DR GeneTree; ENSGT00950000183150; -.
DR HOGENOM; CLU_052517_0_0_1; -.
DR InParanoid; P35576; -.
DR OMA; RRWCERP; -.
DR OrthoDB; 743717at2759; -.
DR PhylomeDB; P35576; -.
DR TreeFam; TF324388; -.
DR BRENDA; 3.1.3.9; 3474.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR UniPathway; UPA00138; -.
DR BioGRID-ORCS; 14377; 2 hits in 73 CRISPR screens.
DR ChiTaRS; G6pc; mouse.
DR PRO; PR:P35576; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P35576; protein.
DR Bgee; ENSMUSG00000078650; Expressed in right kidney and 31 other tissues.
DR Genevisible; P35576; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:MGI.
DR GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IMP:MGI.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0015760; P:glucose-6-phosphate transport; IDA:MGI.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
DR GO; GO:0055088; P:lipid homeostasis; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:MGI.
DR GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0008202; P:steroid metabolic process; IMP:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR GO; GO:0046415; P:urate metabolic process; IMP: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; Glycoprotein; Hydrolase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..357
FT /note="Glucose-6-phosphatase catalytic subunit 1"
FT /id="PRO_0000087414"
FT TOPO_DOM 1..28
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..117
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..179
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..254
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..320
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT MOTIF 354..357
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT ACT_SITE 176
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P35575"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CONFLICT 291..292
FT /note="LL -> SF (in Ref. 1; AAC52122)"
FT /evidence="ECO:0000305"
SQ 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
