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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_HUMAN             Reviewed;         355 AA.
Q9NQR9; E9PAX2; Q6AHZ0;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
20-JUN-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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND TISSUE
SPECIFICITY.
PubMed=11297555; DOI=10.1074/jbc.M101549200;
Martin C.C., Bischof L.J., Bergman B., Hornbuckle L.A., Hilliker C.,
Frigeri C., Wahl D., Svitek C.A., Wong R., Goldman J.K., Oeser J.K.,
Lepretre F., Froguel P., O'Brien R.M., Hutton J.C.;
"Cloning and characterization of the human and rat islet-specific
glucose-6-phosphatase catalytic subunit-related protein (IGRP)
genes.";
J. Biol. Chem. 276:25197-25207(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Pancreas;
Melton D., Brown J., Kenty G., Permutt A., Lee C., Kaestner K.,
Lemishka I., Scearce M., Brestelli J., Gradwohl G., Clifton S.,
Hillier L., Marra M., Pape D., Wylie T., Martin J., Blistain A.,
Schmitt A., Theising B., Ritter E., Ronko I., Bennett J., Cardenas M.,
Gibbons M., McCann R., Cole R., Tsagareishvili R., Williams T.,
Jackson Y., Bowers Y.;
"Endocrine pancreas consortium.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
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).
[7]
SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF ASN-50; ASN-92 AND
ASN-287, AND GLYCOSYLATION AT ASN-92.
PubMed=15044018; DOI=10.1016/S0014-5793(04)00223-6;
Shieh J.-J., Pan C.-J., Mansfield B.C., Chou J.Y.;
"The islet-specific glucose-6-phosphatase-related protein, implicated
in diabetes, is a glycoprotein embedded in the endoplasmic reticulum
membrane.";
FEBS Lett. 562:160-164(2004).
[8]
CATALYTIC ACTIVITY.
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]
ALTERNATIVE SPLICING.
PubMed=16520917; DOI=10.1007/s00125-006-0185-8;
Dogra R.S., Vaidyanathan P., Prabakar K.R., Marshall K.E.,
Hutton J.C., Pugliese A.;
"Alternative splicing of G6PC2, the gene coding for the islet-specific
glucose-6-phosphatase catalytic subunit-related protein (IGRP),
results in differential expression in human thymus and spleen compared
with pancreas.";
Diabetologia 49:953-957(2006).
[10]
INVOLVEMENT IN FGQTL1.
PubMed=18451265; DOI=10.1126/science.1156849;
Bouatia-Naji N., Rocheleau G., Van Lommel L., Lemaire K., Schuit F.,
Cavalcanti-Proenca C., Marchand M., Hartikainen A.-L., Sovio U.,
De Graeve F., Rung J., Vaxillaire M., Tichet J., Marre M., Balkau B.,
Weill J., Elliott P., Jarvelin M.-R., Meyre D., Polychronakos C.,
Dina C., Sladek R., Froguel P.;
"A polymorphism within the G6PC2 gene is associated with fasting
plasma glucose levels.";
Science 320:1085-1088(2008).
-!- 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}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.45 mM for glucose-6-phosphate (at pH 6.5);
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:15044018}; Multi-pass membrane protein
{ECO:0000269|PubMed:15044018}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NQR9-1; Sequence=Displayed;
Name=2;
IsoId=Q9NQR9-2; Sequence=VSP_033648, VSP_033649;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NQR9-3; Sequence=VSP_046180, VSP_046181;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Specifically expressed in pancreas and also
detected to a lower extent in testis. Expressed by most islet
cells in the pancreas (at protein level).
{ECO:0000269|PubMed:11297555}.
-!- PTM: N-glycosylated; the non-glycosylated form is more unstable
and is degraded through the proteasome.
{ECO:0000269|PubMed:15044018}.
-!- POLYMORPHISM: Genetic variations in G6PC2 define the fasting
plasma glucose levels quantitative trait locus 1 (FGQTL1)
[MIM:612108]. The normal fasting plasma glucose level in the
plasma is defined as less than 100 mg per deciliter (5.55 mmol per
liter). Higher fasting plasma glucose levels predict type 2
diabetes in young adults and increases the risk of mortality.
-!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF283835; AAF82810.1; -; Genomic_DNA.
EMBL; BQ777188; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CR627438; CAH10524.1; -; mRNA.
EMBL; AC069137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471058; EAX11291.1; -; Genomic_DNA.
EMBL; BC104778; AAI04779.1; -; mRNA.
EMBL; BC113376; AAI13377.1; -; mRNA.
CCDS; CCDS2230.1; -. [Q9NQR9-1]
CCDS; CCDS46443.1; -. [Q9NQR9-3]
RefSeq; NP_001075155.1; NM_001081686.1. [Q9NQR9-3]
RefSeq; NP_066999.1; NM_021176.2. [Q9NQR9-1]
UniGene; Hs.283963; -.
ProteinModelPortal; Q9NQR9; -.
STRING; 9606.ENSP00000364512; -.
DEPOD; Q9NQR9; -.
iPTMnet; Q9NQR9; -.
PhosphoSitePlus; Q9NQR9; -.
BioMuta; G6PC2; -.
DMDM; 74725272; -.
PaxDb; Q9NQR9; -.
PeptideAtlas; Q9NQR9; -.
PRIDE; Q9NQR9; -.
ProteomicsDB; 82175; -.
ProteomicsDB; 82176; -. [Q9NQR9-2]
DNASU; 57818; -.
Ensembl; ENST00000282075; ENSP00000282075; ENSG00000152254. [Q9NQR9-2]
Ensembl; ENST00000375363; ENSP00000364512; ENSG00000152254. [Q9NQR9-1]
Ensembl; ENST00000429379; ENSP00000396939; ENSG00000152254. [Q9NQR9-3]
Ensembl; ENST00000612807; ENSP00000481098; ENSG00000278373. [Q9NQR9-3]
Ensembl; ENST00000617403; ENSP00000483899; ENSG00000278373. [Q9NQR9-2]
Ensembl; ENST00000622133; ENSP00000482583; ENSG00000278373. [Q9NQR9-1]
GeneID; 57818; -.
KEGG; hsa:57818; -.
UCSC; uc002uem.4; human. [Q9NQR9-1]
CTD; 57818; -.
DisGeNET; 57818; -.
EuPathDB; HostDB:ENSG00000152254.10; -.
GeneCards; G6PC2; -.
HGNC; HGNC:28906; G6PC2.
MIM; 608058; gene.
MIM; 612108; phenotype.
neXtProt; NX_Q9NQR9; -.
OpenTargets; ENSG00000152254; -.
PharmGKB; PA134944773; -.
eggNOG; ENOG410IDXG; Eukaryota.
eggNOG; ENOG4110AJ7; LUCA.
GeneTree; ENSGT00510000046465; -.
HOGENOM; HOG000264239; -.
HOVERGEN; HBG003560; -.
InParanoid; Q9NQR9; -.
KO; K01084; -.
OMA; ISVCISR; -.
OrthoDB; EOG091G0AXF; -.
PhylomeDB; Q9NQR9; -.
TreeFam; TF324388; -.
BioCyc; MetaCyc:HS14422-MONOMER; -.
BRENDA; 3.1.3.9; 2681.
Reactome; R-HSA-70263; Gluconeogenesis.
SABIO-RK; Q9NQR9; -.
UniPathway; UPA00138; -.
GeneWiki; G6PC2; -.
GenomeRNAi; 57818; -.
PRO; PR:Q9NQR9; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000152254; -.
CleanEx; HS_G6PC2; -.
ExpressionAtlas; Q9NQR9; baseline and differential.
Genevisible; Q9NQR9; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
GO; GO:0004346; F:glucose-6-phosphatase activity; EXP:Reactome.
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; IMP:BHF-UCL.
GO; GO:0050796; P:regulation of insulin secretion; IMP:BHF-UCL.
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; Polymorphism;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 355 Glucose-6-phosphatase 2.
/FTId=PRO_0000334509.
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 233 261 Lumenal. {ECO:0000255}.
TRANSMEM 262 282 Helical. {ECO:0000255}.
TOPO_DOM 283 293 Cytoplasmic. {ECO:0000255}.
TRANSMEM 294 314 Helical. {ECO:0000255}.
TOPO_DOM 315 318 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:0000269|PubMed:15044018}.
VAR_SEQ 74 102 ILFGHRPYWWVQETQIYPNHSSPCLEQFP -> KSIWPCNG
RILCLVCHGNRCPEPHCLWDG (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_033648.
VAR_SEQ 103 355 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_033649.
VAR_SEQ 148 154 LTWSFLW -> HAGGRGL (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_046180.
VAR_SEQ 155 355 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_046181.
VARIANT 171 171 I -> V (in dbSNP:rs2232322).
/FTId=VAR_043372.
VARIANT 207 207 Y -> S (in dbSNP:rs2232323).
/FTId=VAR_043373.
VARIANT 219 219 V -> L (in dbSNP:rs492594).
/FTId=VAR_043374.
VARIANT 324 324 S -> P (in dbSNP:rs2232326).
/FTId=VAR_043375.
VARIANT 340 340 P -> L (in dbSNP:rs2232327).
/FTId=VAR_043376.
VARIANT 342 342 S -> C (in dbSNP:rs2232328).
/FTId=VAR_043377.
MUTAGEN 50 50 N->A: No effect on N-glycosylation.
{ECO:0000269|PubMed:15044018}.
MUTAGEN 92 92 N->A: Loss of N-glycosylation.
{ECO:0000269|PubMed:15044018}.
MUTAGEN 287 287 N->A: No effect on N-glycosylation.
{ECO:0000269|PubMed:15044018}.
SEQUENCE 355 AA; 40580 MW; D642C37496B6C4EB CRC64;
MDFLHRNGVL IIQHLQKDYR AYYTFLNFMS NVGDPRNIFF IYFPLCFQFN QTVGTKMIWV
AVIGDWLNLI FKWILFGHRP YWWVQETQIY PNHSSPCLEQ FPTTCETGPG SPSGHAMGAS
CVWYVMVTAA LSHTVCGMDK FSITLHRLTW SFLWSVFWLI QISVCISRVF IATHFPHQVI
LGVIGGMLVA EAFEHTPGIQ TASLGTYLKT NLFLFLFAVG FYLLLRVLNI DLLWSVPIAK
KWCANPDWIH IDTTPFAGLV RNLGVLFGLG FAINSEMFLL SCRGGNNYTL SFRLLCALTS
LTILQLYHFL QIPTHEEHLF YVLSFCKSAS IPLTVVAFIP YSVHMLMKQS GKKSQ


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