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Glucose-6-phosphatase 2 (G-6-Pase 2) (G6Pase 2) (EC 3.1.3.9) (Islet-specific glucose-6-phosphatase catalytic subunit-related protein)

 G6PC2_MOUSE             Reviewed;         355 AA.
Q9Z186; A2AUN2; Q2M2M7;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
12-SEP-2018, entry version 124.
RecName: Full=Glucose-6-phosphatase 2;
Short=G-6-Pase 2;
Short=G6Pase 2;
EC=3.1.3.9;
AltName: Full=Islet-specific glucose-6-phosphatase catalytic subunit-related protein;
Name=G6pc2; Synonyms=Igrp;
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] (ISOFORM 1), CHARACTERIZATION,
GLYCOSYLATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Pancreatic islet;
PubMed=10078553; DOI=10.2337/diabetes.48.3.531;
Arden S.D., Zahn T., Steegers S., Webb S., Bergman B., O'Brien R.M.,
Hutton J.C.;
"Molecular cloning of a pancreatic islet-specific glucose-6-
phosphatase catalytic subunit-related protein.";
Diabetes 48:531-542(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10078554; DOI=10.2337/diabetes.48.3.543;
Ebert D.H., Bischof L.J., Streeper R.S., Chapman S.C., Svitek C.A.,
Goldman J.K., Mathews C.E., Leiter E.H., Hutton J.C., O'Brien R.M.;
"Structure and promoter activity of an islet-specific glucose-6-
phosphatase catalytic subunit-related gene.";
Diabetes 48:543-551(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Pancreas;
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).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[6]
TISSUE SPECIFICITY.
PubMed=12878201; DOI=10.1016/S0006-291X(03)01242-7;
Goh B.-H., Efendic S., Khan A., Portwood N.;
"Evidence for the expression of both the hydrolase and translocase
components of hepatic glucose-6-phosphatase in murine pancreatic
islets.";
Biochem. Biophys. Res. Commun. 307:935-941(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION AS AN
AUTOANTIGEN.
PubMed=12815107; DOI=10.1073/pnas.0932778100;
Lieberman S.M., Evans A.M., Han B., Takaki T., Vinnitskaya Y.,
Caldwell J.A., Serreze D.V., Shabanowitz J., Hunt D.F.,
Nathenson S.G., Santamaria P., DiLorenzo T.P.;
"Identification of the beta cell antigen targeted by a prevalent
population of pathogenic CD8+ T cells in autoimmune diabetes.";
Proc. Natl. Acad. Sci. U.S.A. 100:8384-8388(2003).
[8]
CATALYTIC ACTIVITY, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=14722102; DOI=10.1074/jbc.M307756200;
Petrolonis A.J., Yang Q., Tummino P.J., Fish S.M., Prack A.E.,
Jain S., Parsons T.F., Li P., Dales N.A., Ge L., Langston S.P.,
Schuller A.G.P., An W.F., Tartaglia L.A., Chen H., Hong S.-B.;
"Enzymatic characterization of the pancreatic islet-specific glucose-
6-phosphatase-related protein (IGRP).";
J. Biol. Chem. 279:13976-13983(2004).
[9]
IDENTIFICATION AS AN AUTOANTIGEN.
PubMed=15843527; DOI=10.4049/jimmunol.174.9.5306;
Mukherjee R., Wagar D., Stephens T.A., Lee-Chan E., Singh B.;
"Identification of CD4+ T cell-specific epitopes of islet-specific
glucose-6-phosphatase catalytic subunit-related protein: a novel beta
cell autoantigen in type 1 diabetes.";
J. Immunol. 174:5306-5315(2005).
[10]
DISRUPTION PHENOTYPE.
PubMed=17265032; DOI=10.1007/s00125-006-0564-1;
Wang Y., Martin C.C., Oeser J.K., Sarkar S., McGuinness O.P.,
Hutton J.C., O'Brien R.M.;
"Deletion of the gene encoding the islet-specific glucose-6-
phosphatase catalytic subunit-related protein autoantigen results in a
mild metabolic phenotype.";
Diabetologia 50:774-778(2007).
-!- FUNCTION: May hydrolyze glucose-6-phosphate to glucose in the
endoplasmic reticulum. May be responsible for glucose production
through glycogenolysis and gluconeogenesis (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + H(2)O = D-glucose +
phosphate. {ECO:0000269|PubMed:14722102}.
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z186-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z186-2; Sequence=VSP_033650, VSP_033651;
-!- TISSUE SPECIFICITY: Specifically expressed in pancreatic islet
cells, in particular those of beta-cell origin. Not detected in
testis, kidney, muscle, liver, lung, spleen, brain, pituitary,
gastric fundus or heart. {ECO:0000269|PubMed:10078553,
ECO:0000269|PubMed:12878201, ECO:0000269|PubMed:14722102}.
-!- DEVELOPMENTAL STAGE: Initial onset of expression in the pancreas
is at E12 and prominent expression is detected at E14.
{ECO:0000269|PubMed:10078553}.
-!- INDUCTION: Up-regulated in islet cells cultured in hyperglycemic
concentrations of glucose. {ECO:0000269|PubMed:14722102}.
-!- PTM: N-glycosylated; the non-glycosylated form is more unstable
and is degraded through the proteasome. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice are no overt anatomical or behavioral
phenotype but display a mild metabolic phenotype. Upon fasting
those mice exhibit a significant decrease in blood glucose and
triacylglycerol compared to wild type mice.
{ECO:0000269|PubMed:17265032}.
-!- MISCELLANEOUS: G6pc2 is an autoantigen which is the natural target
of a prevalent T-cell population causing insulin-dependent
diabetes mellitus through destruction of pancreatic beta cells.
-!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI11906.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z47787; CAA87708.1; -; mRNA.
EMBL; AF118766; AAD28562.1; -; Genomic_DNA.
EMBL; AF118762; AAD28562.1; JOINED; Genomic_DNA.
EMBL; AF118763; AAD28562.1; JOINED; Genomic_DNA.
EMBL; AF118764; AAD28562.1; JOINED; Genomic_DNA.
EMBL; AF118765; AAD28562.1; JOINED; Genomic_DNA.
EMBL; AK148465; BAE28569.1; -; mRNA.
EMBL; AL929170; CAM24718.1; -; Genomic_DNA.
EMBL; AL929170; CAM24719.1; -; Genomic_DNA.
EMBL; BC111905; AAI11906.1; ALT_SEQ; mRNA.
CCDS; CCDS16089.1; -. [Q9Z186-1]
CCDS; CCDS71066.1; -. [Q9Z186-2]
RefSeq; NP_001276785.1; NM_001289856.1.
RefSeq; NP_001276786.1; NM_001289857.1. [Q9Z186-2]
RefSeq; NP_067306.1; NM_021331.4. [Q9Z186-1]
UniGene; Mm.140768; -.
ProteinModelPortal; Q9Z186; -.
BioGrid; 199788; 1.
STRING; 10090.ENSMUSP00000005364; -.
PhosphoSitePlus; Q9Z186; -.
PaxDb; Q9Z186; -.
PRIDE; Q9Z186; -.
DNASU; 14378; -.
Ensembl; ENSMUST00000005364; ENSMUSP00000005364; ENSMUSG00000005232. [Q9Z186-1]
Ensembl; ENSMUST00000112317; ENSMUSP00000107936; ENSMUSG00000005232. [Q9Z186-2]
GeneID; 14378; -.
KEGG; mmu:14378; -.
UCSC; uc008jxy.2; mouse. [Q9Z186-1]
UCSC; uc008jxz.2; mouse. [Q9Z186-2]
CTD; 57818; -.
MGI; MGI:1277193; G6pc2.
eggNOG; ENOG410IDXG; Eukaryota.
eggNOG; ENOG4110AJ7; LUCA.
GeneTree; ENSGT00510000046465; -.
HOGENOM; HOG000264239; -.
HOVERGEN; HBG003560; -.
InParanoid; Q9Z186; -.
KO; K01084; -.
OMA; ISVCISR; -.
OrthoDB; EOG091G0AXF; -.
PhylomeDB; Q9Z186; -.
TreeFam; TF324388; -.
BRENDA; 3.1.3.9; 3474.
Reactome; R-MMU-70263; Gluconeogenesis.
UniPathway; UPA00138; -.
PRO; PR:Q9Z186; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000005232; Expressed in 36 organ(s), highest expression level in islet of Langerhans.
Genevisible; Q9Z186; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:MGI.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0016311; P:dephosphorylation; IEA:GOC.
GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
GO; GO:0042593; P:glucose homeostasis; ISO:MGI.
GO; GO:0050796; P:regulation of insulin secretion; ISO: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;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Gluconeogenesis; Glycoprotein; Hydrolase; Membrane;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 355 Glucose-6-phosphatase 2.
/FTId=PRO_0000334510.
TOPO_DOM 1 24 Lumenal. {ECO:0000255}.
TRANSMEM 25 45 Helical. {ECO:0000255}.
TOPO_DOM 46 56 Cytoplasmic. {ECO:0000255}.
TRANSMEM 57 77 Helical. {ECO:0000255}.
TOPO_DOM 78 115 Lumenal. {ECO:0000255}.
TRANSMEM 116 136 Helical. {ECO:0000255}.
TOPO_DOM 137 146 Cytoplasmic. {ECO:0000255}.
TRANSMEM 147 167 Helical. {ECO:0000255}.
TOPO_DOM 168 168 Lumenal. {ECO:0000255}.
TRANSMEM 169 189 Helical. {ECO:0000255}.
TOPO_DOM 190 211 Cytoplasmic. {ECO:0000255}.
TRANSMEM 212 232 Helical. {ECO:0000255}.
TOPO_DOM 233 252 Lumenal. {ECO:0000255}.
TRANSMEM 253 273 Helical. {ECO:0000255}.
TOPO_DOM 274 290 Cytoplasmic. {ECO:0000255}.
TRANSMEM 291 307 Helical. {ECO:0000255}.
TOPO_DOM 308 318 Lumenal. {ECO:0000255}.
TRANSMEM 319 339 Helical. {ECO:0000255}.
TOPO_DOM 340 355 Cytoplasmic. {ECO:0000255}.
MOTIF 352 355 Prevents secretion from ER.
{ECO:0000255}.
ACT_SITE 115 115 Proton donor. {ECO:0000255}.
ACT_SITE 174 174 Nucleophile. {ECO:0000250}.
BINDING 79 79 Substrate. {ECO:0000255}.
BINDING 168 168 Substrate. {ECO:0000255}.
CARBOHYD 92 92 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
VAR_SEQ 148 154 LTWSFLW -> DASSRGL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_033650.
VAR_SEQ 155 355 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_033651.
SEQUENCE 355 AA; 40681 MW; C814C27DE44E306A CRC64;
MDFLHRSGVL IIHHLQEDYR TYYGFLNFMS NVGDPRNIFS IYFPLWFQLN QNVGTKMIWV
AVIGDWFNLI FKWILFGHRP YWWIQETEIY PNHSSPCLEQ FPTTCETGPG SPSGHAMGSS
CVWYVMVTAA LSYTISRMEE SSVTLHRLTW SFLWSVFWLI QISVCISRVF IATHFPHQVI
LGVIGGMLVA EAFEHTPGVH MASLSVYLKT NVFLFLFALG FYLLLRLFGI DLLWSVPIAK
KWCANPDWIH IDSTPFAGLV RNLGVLFGLG FAINSEMFLR SCQGENGTKP SFRLLCALTS
LTTMQLYRFI KIPTHAEPLF YLLSFCKSAS IPLMVVALIP YCVHMLMRPG DKKTK


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