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   24-JAN-2024, entry version 167.
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   GlyCosmos; P35576; 1 site, No reported glycans.
DR   GlyGen; P35576; 1 site.
DR   PhosphoSitePlus; P35576; -.
DR   SwissPalm; P35576; -.
DR   jPOST; P35576; -.
DR   MaxQB; P35576; -.
DR   PaxDb; 10090-ENSMUSP00000019469; -.
DR   ProteomicsDB; 271629; -.
DR   Antibodypedia; 29454; 194 antibodies from 24 providers.
DR   DNASU; 14377; -.
DR   Ensembl; ENSMUST00000019469.3; ENSMUSP00000019469.3; ENSMUSG00000078650.3.
DR   GeneID; 14377; -.
DR   KEGG; mmu:14377; -.
DR   UCSC; uc007lor.1; mouse.
DR   AGR; MGI:95607; -.
DR   CTD; 2538; -.
DR   MGI; MGI:95607; G6pc1.
DR   VEuPathDB; HostDB:ENSMUSG00000078650; -.
DR   eggNOG; ENOG502QS9B; Eukaryota.
DR   GeneTree; ENSGT00950000183150; -.
DR   HOGENOM; CLU_052517_0_0_1; -.
DR   InParanoid; P35576; -.
DR   OMA; WFILVSM; -.
DR   OrthoDB; 4030642at2759; -.
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 78 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 cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
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: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   CDD; cd03381; PAP2_glucose_6_phosphatase; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR016275; Glucose-6-phosphatase.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   PANTHER; PTHR12591; GLUCOSE-6-PHOSPHATASE; 1.
DR   PANTHER; PTHR12591:SF3; GLUCOSE-6-PHOSPHATASE CATALYTIC SUBUNIT 1; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   Genevisible; P35576; MM.
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
//