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

 G6PC_HUMAN              Reviewed;         357 AA.
P35575; A1L4C0; B4E1C3; K7EL82;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 2.
22-NOV-2017, entry version 170.
RecName: Full=Glucose-6-phosphatase;
Short=G-6-Pase;
Short=G6Pase;
EC=3.1.3.9;
AltName: Full=Glucose-6-phosphatase alpha;
Short=G6Pase-alpha;
Name=G6PC; Synonyms=G6PT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8211187; DOI=10.1126/science.8211187;
Lei K.-J., Shelly L.L., Pan C.-J., Sidbury J.B., Chou J.Y.;
"Mutations in the glucose-6-phosphatase gene that cause glycogen
storage disease type 1a.";
Science 262:580-583(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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]
GLYCOSYLATION AT ASN-96.
PubMed=9705299; DOI=10.1074/jbc.273.34.21658;
Pan C.J., Lei K.J., Chou J.Y.;
"Asparagine-linked oligosaccharides are localized to a luminal
hydrophilic loop in human glucose-6-phosphatase.";
J. Biol. Chem. 273:21658-21662(1998).
[6]
ACTIVE SITES, MUTAGENESIS OF HIS-9; HIS-52; HIS-119; HIS-176; HIS-179;
HIS-197; HIS-252; HIS-307 AND HIS-353, AND CHARACTERIZATION OF
VARIANTS ASN-76; CYS-83 AND GLN-170.
PubMed=12093795; DOI=10.1074/jbc.M201853200;
Ghosh A., Shieh J.-J., Pan C.-J., Sun M.-S., Chou J.Y.;
"The catalytic center of glucose-6-phosphatase. HIS176 is the
nucleophile forming the phosphohistidine-enzyme intermediate during
catalysis.";
J. Biol. Chem. 277:32837-32842(2002).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[8]
VARIANT GSD1A CYS-83.
PubMed=8182131; DOI=10.1172/JCI117192;
Lei K.J., Pan C.J., Shelly L.L., Liu J.L., Chou J.Y.;
"Identification of mutations in the gene for glucose-6-phosphatase,
the enzyme deficient in glycogen storage disease type 1a.";
J. Clin. Invest. 93:1994-1999(1994).
[9]
VARIANTS GSD1A.
PubMed=7573034;
Lei K.-J., Chen Y.-T., Chen H., Wong L.-J.C., Liu J.-L.,
McConkie-Rosell A., van Hove J.L.K., Ou H.C.-Y., Yeh N.J., Pan L.Y.,
Chou J.Y.;
"Genetic basis of glycogen storage disease type 1a: prevalent
mutations at the glucose-6-phosphatase locus.";
Am. J. Hum. Genet. 57:766-771(1995).
[10]
VARIANTS GSD1A CYS-83 AND GLY-166.
PubMed=7623438; DOI=10.1007/BF00711368;
Parvari R., Moses S., Hershkovitz E., Carmi R., Bashan N.;
"Characterization of the mutations in the glucose-6-phosphatase gene
in Israeli patients with glycogen storage disease type 1a: R83C in six
Jews and a novel V166G mutation in a Muslim Arab.";
J. Inherit. Metab. Dis. 18:21-27(1995).
[11]
VARIANT GSD1A ILE-83.
PubMed=7655466; DOI=10.1093/hmg/4.6.1095;
Hwu W.-L., Chuang S.-C., Tsai L.-P., Chang M.-H., Chuang S.-M.,
Wang T.-R.;
"Glucose-6-phosphatase gene G327A mutation is common in Chinese
patients with glycogen storage disease type Ia.";
Hum. Mol. Genet. 4:1095-1096(1995).
[12]
VARIANTS GSD1A HIS-83 AND ASN-341.
PubMed=9001800;
Lee W.J., Lee H.M., Chi C.S., Shu S.G., Lin L.Y., Lin W.H.;
"Genetic analysis of the glucose-6-phosphatase mutation of type 1a
glycogen storage disease in a Chinese family.";
Clin. Genet. 50:206-211(1996).
[13]
VARIANTS GSD1A VAL-38; ARG-77; LYS-110; THR-124; GLU-184; ARG-188 AND
PRO-211.
PubMed=8733042; DOI=10.1136/jmg.33.5.358;
Chevalier-Porst F., Bozon D., Bonardot A.-M., Bruni N., Mithieux G.,
Mathieu M., Maire I.;
"Mutation analysis in 24 French patients with glycogen storage disease
type 1a.";
J. Med. Genet. 33:358-360(1996).
[14]
VARIANTS GSD1A CYS-83 AND GLY-166.
PubMed=9332655;
DOI=10.1002/(SICI)1096-8628(19971031)72:3<286::AID-AJMG6>3.0.CO;2-P;
Parvari R., Lei K.J., Bashan N., Hershkovitz E., Korman S.H.,
Barash V., Lerman-Sagie T., Mandel H., Chou J.Y., Moses S.W.;
"Glycogen storage disease type 1a in Israel: biochemical, clinical,
and mutational studies.";
Am. J. Med. Genet. 72:286-290(1997).
[15]
VARIANTS GSD1A CYS-83; GLN-170 AND TRP-270.
PubMed=9700612; DOI=10.1023/A:1005339616074;
Huener G., Podskarbi T., Schuetz M., Baykal T., Sarbat G., Shin Y.S.,
Demirkol M.;
"Molecular aspects of glycogen storage disease type Ia in Turkish
patients: a novel mutation in the glucose-6-phosphatase gene.";
J. Inherit. Metab. Dis. 21:445-446(1998).
[16]
VARIANT GSD1A ARG-68.
PubMed=9700613; DOI=10.1023/A:1005391600145;
Sartorato E.L., Reis F.C., Norato D.Y.J., Hackel C.;
"A novel mutation in a Brazilian patient with glycogen storage disease
type 1a.";
J. Inherit. Metab. Dis. 21:447-447(1998).
[17]
VARIANTS GSD1A CYS-83 AND LYS-264.
PubMed=9506659; DOI=10.1016/S0022-3476(98)70463-9;
Keller K.M., Schuetz M., Podskarbi T., Bindl L., Lentze M.J.,
Shin Y.S.;
"A new mutation of the glucose-6-phosphatase gene in a 4-year-old girl
with oligosymptomatic glycogen storage disease type 1a.";
J. Pediatr. 132:360-361(1998).
[18]
VARIANTS GSD1A VAL-266 AND PHE-338.
PubMed=10094563;
DOI=10.1002/(SICI)1098-1004(1999)13:2<173::AID-HUMU19>3.0.CO;2-E;
Rake J.P., ten Berge A.M., Verlind E., Visser G., Niezen-Koning K.E.,
Buys C.H.C.M., Smit G.P., Scheffer H.;
"Glycogen storage disease type Ia: four novel mutations (175delGG,
R170X, G266V and V338F) identified.";
Hum. Mutat. 13:173-173(1999).
[19]
VARIANTS GSD1A PRO-54 AND ILE-108.
PubMed=10447271;
DOI=10.1002/(SICI)1098-1004(1999)14:1<91::AID-HUMU21>3.0.CO;2-B;
Trioche P., Francoual J., Chalas J., Capel L., Bernard O., Labrune P.;
"Identification of three novel mutations (Q54P, W70X and T108I) in the
glucose-6-phosphatase gene of patients with glycogen storage disease
type Ia.";
Hum. Mutat. 14:91-91(1999).
[20]
VARIANTS GSD1A VAL-38; ARG-63; CYS-83; VAL-184; ARG-222; VAL-270;
CYS-295; PRO-298 AND PHE-338.
PubMed=10070617; DOI=10.1023/A:1005495131118;
Stroppiano M., Regis S., DiRocco M., Caroli F., Gandullia P.,
Gatti R.;
"Mutations in the glucose-6-phosphatase gene of 53 Italian patients
with glycogen storage disease type Ia.";
J. Inherit. Metab. Dis. 22:43-49(1999).
[21]
VARIANTS GSD1A HIS-83; ASP-122; PRO-179 AND LEU-257.
PubMed=10748407;
DOI=10.1002/(SICI)1096-8628(20000313)91:2<107::AID-AJMG5>3.0.CO;2-Y;
Akanuma J., Nishigaki T., Fujii K., Matsubara Y., Inui K.,
Takahashi K., Kure S., Suzuki Y., Ohura T., Miyabayashi S., Ogawa E.,
Iinuma K., Okada S., Narisawa K.;
"Glycogen storage disease type Ia: molecular diagnosis of 51 Japanese
patients and characterization of splicing mutations by analysis of
ectopically transcribed mRNA from lymphoblastoid cells.";
Am. J. Med. Genet. 91:107-112(2000).
[22]
VARIANTS GSD1A ARG-20; ARG-81; LEU-156 AND ASP-188.
PubMed=10612834;
DOI=10.1002/(SICI)1098-1004(200001)15:1<115::AID-HUMU23>3.0.CO;2-W;
Seydewitz H.H., Matern D.;
"Molecular genetic analysis of 40 patients with glycogen storage
disease type Ia: 100% mutation detection rate and 5 novel mutations.";
Hum. Mutat. 15:115-116(2000).
[23]
VARIANT GSD1A ALA-16.
PubMed=10738005;
DOI=10.1002/(SICI)1098-1004(200004)15:4<390::AID-HUMU32>3.0.CO;2-N;
Wu M.-C., Tsai F.-J., Lee C.-C., Lin S.-P., Wu J.-Y.;
"Identification of a novel missense mutation (T16A) in the glucose-6-
phosphatase gene in a Taiwan Chinese patient with glycogen storage
disease Ia (von Gierke disease).";
Hum. Mutat. 15:390-390(2000).
[24]
VARIANTS GSD1A ASN-76; ARG-77; CYS-83; ALA-166; ARG-188 AND CYS-295.
PubMed=10874313;
DOI=10.1002/1098-1004(200007)16:1<89::AID-HUMU17>3.3.CO;2-1;
Kozak L., Francova H., Hrabincova E., Stastna S., Peskova K.,
Elleder M.;
"Identification of mutations in the glucose-6-phosphatase gene in
Czech and Slovak patients with glycogen storage disease type Ia,
including novel mutations K76N, V166A and 540del5.";
Hum. Mutat. 16:89-89(2000).
[25]
VARIANTS GSD1A ARG-5; VAL-38; PRO-54; CYS-83; ILE-108; LYS-110;
ILE-111; GLU-184; ARG-188; THR-241; ARG-270; VAL-270; LEU-322; PHE-327
DEL AND PHE-338.
PubMed=11058903;
DOI=10.1002/1098-1004(200011)16:5<444::AID-HUMU10>3.0.CO;2-F;
Trioche P., Francoual J., Chalas J., Capel L., Lindenbaum A.,
Odievre M., Labrune P.;
"Genetic heterogeneity of glycogen storage disease type Ia in France:
a study of 48 patients.";
Hum. Mutat. 16:444-444(2000).
[26]
VARIANT GSD1A LEU-119.
PubMed=11058910;
DOI=10.1002/1098-1004(200011)16:5<447::AID-HUMU17>3.0.CO;2-M;
Wu M.-C., Tsai F.-J., Lee C.-C., Tsai C.-H., Wu J.-Y.;
"A novel missense mutation (H119L) identified in a Taiwan Chinese
family with glycogen storage disease Ia (von Gierke disease).";
Hum. Mutat. 16:447-447(2000).
[27]
VARIANT GSD1A ARG-188.
PubMed=10960498; DOI=10.1203/00006450-200009000-00011;
Weston B.W., Lin J.L., Muenzer J., Cameron H.S., Arnold R.R.,
Seydewitz H.H., Mayatepek E., Van Schaftingen E., Veiga-da-Cunha M.,
Matern D., Chen Y.T.;
"Glucose-6-phosphatase mutation G188R confers an atypical glycogen
storage disease type 1b phenotype.";
Pediatr. Res. 48:329-334(2000).
[28]
VARIANTS GSD1A ARG-20; VAL-38; PRO-65; ARG-68; ARG-77; ARG-81; CYS-83;
HIS-83; LYS-110; LEU-113; LEU-156; GLN-170; CYS-177; SER-178; ARG-188;
SER-188; ARG-236; PRO-265; VAL-270; PHE-327 DEL AND ARG-345.
PubMed=12373566; DOI=10.1007/BF02679989;
Matern D., Seydewitz H.H., Bali D., Lang C., Chen Y.-T.;
"Glycogen storage disease type I: diagnosis and phenotype/genotype
correlation.";
Eur. J. Pediatr. 161:S10-S19(2002).
[29]
VARIANT GSD1A CYS-83.
PubMed=15316959; DOI=10.1002/ajmg.a.30232;
Ekstein J., Rubin B.Y., Anderson S.L., Weinstein D.A., Bach G.,
Abeliovich D., Webb M., Risch N.;
"Mutation frequencies for glycogen storage disease Ia in the Ashkenazi
Jewish population.";
Am. J. Med. Genet. A 129:162-164(2004).
[30]
VARIANTS GSD1A ASP-122; ALA-178 AND ILE-255.
PubMed=15151508; DOI=10.1111/j.1399-0004.2004.00260.x;
Ki C.S., Han S.H., Kim H.J., Lee S.G., Kim E.J., Kim J.W., Choe Y.H.,
Seo J.K., Chang Y.J., Park J.Y.;
"Mutation spectrum of the glucose-6-phosphatase gene and its
implication in molecular diagnosis of Korean patients with glycogen
storage disease type Ia.";
Clin. Genet. 65:487-489(2004).
[31]
VARIANTS GSD1A ARG-16; PRO-54; CYS-83 AND CYS-209, AND
CHARACTERIZATION OF VARIANTS GSD1A ARG-16 AND CYS-209.
PubMed=15542400; DOI=10.1016/j.ymgme.2004.06.010;
Angaroni C.J., de Kremer R.D., Argarana C.E., Paschini-Capra A.E.,
Giner-Ayala A.N., Pezza R.J., Pan C.-J., Chou J.Y.;
"Glycogen storage disease type Ia in Argentina: two novel glucose-6-
phosphatase mutations affecting protein stability.";
Mol. Genet. Metab. 83:276-279(2004).
[32]
VARIANT [LARGE SCALE ANALYSIS] LEU-116.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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.
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35575-1; Sequence=Displayed;
Name=2;
IsoId=P35575-2; Sequence=VSP_047558, VSP_047559;
Note=No experimental confirmation available.;
-!- DISEASE: Glycogen storage disease 1A (GSD1A) [MIM:232200]: A
metabolic disorder characterized by impairment of terminal steps
of glycogenolysis and gluconeogenesis. Patients manifest a wide
range of clinical symptoms and biochemical abnormalities,
including hypoglycemia, severe hepatomegaly due to excessive
accumulation of glycogen, kidney enlargement, growth retardation,
lactic acidemia, hyperlipidemia, and hyperuricemia.
{ECO:0000269|PubMed:10070617, ECO:0000269|PubMed:10094563,
ECO:0000269|PubMed:10447271, ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:10738005, ECO:0000269|PubMed:10748407,
ECO:0000269|PubMed:10874313, ECO:0000269|PubMed:10960498,
ECO:0000269|PubMed:11058903, ECO:0000269|PubMed:11058910,
ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:15151508,
ECO:0000269|PubMed:15316959, ECO:0000269|PubMed:15542400,
ECO:0000269|PubMed:7573034, ECO:0000269|PubMed:7623438,
ECO:0000269|PubMed:7655466, ECO:0000269|PubMed:8182131,
ECO:0000269|PubMed:8733042, ECO:0000269|PubMed:9001800,
ECO:0000269|PubMed:9332655, ECO:0000269|PubMed:9506659,
ECO:0000269|PubMed:9700612, ECO:0000269|PubMed:9700613}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the glucose-6-phosphatase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG64735.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U01120; AAA16222.1; -; mRNA.
EMBL; AK303771; BAG64735.1; ALT_INIT; mRNA.
EMBL; AK313982; BAG36695.1; -; mRNA.
EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC130478; AAI30479.1; -; mRNA.
EMBL; BC136369; AAI36370.1; -; mRNA.
CCDS; CCDS11446.1; -. [P35575-1]
CCDS; CCDS59291.1; -. [P35575-2]
PIR; A48251; A48251.
RefSeq; NP_000142.2; NM_000151.3. [P35575-1]
RefSeq; NP_001257326.1; NM_001270397.1. [P35575-2]
UniGene; Hs.212293; -.
UniGene; Hs.742566; -.
ProteinModelPortal; P35575; -.
BioGrid; 108813; 3.
IntAct; P35575; 3.
STRING; 9606.ENSP00000253801; -.
BindingDB; P35575; -.
ChEMBL; CHEMBL2282; -.
DEPOD; P35575; -.
iPTMnet; P35575; -.
PhosphoSitePlus; P35575; -.
BioMuta; G6PC; -.
DMDM; 206729864; -.
PaxDb; P35575; -.
PeptideAtlas; P35575; -.
PRIDE; P35575; -.
DNASU; 2538; -.
Ensembl; ENST00000253801; ENSP00000253801; ENSG00000131482. [P35575-1]
Ensembl; ENST00000592383; ENSP00000465958; ENSG00000131482. [P35575-2]
GeneID; 2538; -.
KEGG; hsa:2538; -.
UCSC; uc002icb.3; human. [P35575-1]
CTD; 2538; -.
DisGeNET; 2538; -.
EuPathDB; HostDB:ENSG00000131482.9; -.
GeneCards; G6PC; -.
GeneReviews; G6PC; -.
HGNC; HGNC:4056; G6PC.
HPA; HPA052324; -.
MalaCards; G6PC; -.
MIM; 232200; phenotype.
MIM; 613742; gene.
neXtProt; NX_P35575; -.
OpenTargets; ENSG00000131482; -.
Orphanet; 79258; Glycogen storage disease due to glucose-6-phosphatase deficiency type a.
PharmGKB; PA28468; -.
eggNOG; ENOG410IDXG; Eukaryota.
eggNOG; ENOG4110AJ7; LUCA.
GeneTree; ENSGT00510000046465; -.
HOGENOM; HOG000264239; -.
HOVERGEN; HBG003560; -.
InParanoid; P35575; -.
KO; K01084; -.
OMA; YLQVNYQ; -.
OrthoDB; EOG091G0AXF; -.
PhylomeDB; P35575; -.
TreeFam; TF324388; -.
BioCyc; MetaCyc:HS05538-MONOMER; -.
BRENDA; 3.1.3.9; 2681.
Reactome; R-HSA-3274531; Glycogen storage disease type Ia (G6PC).
Reactome; R-HSA-70263; Gluconeogenesis.
SABIO-RK; P35575; -.
SIGNOR; P35575; -.
UniPathway; UPA00138; -.
ChiTaRS; G6PC; human.
GeneWiki; G6PC; -.
GenomeRNAi; 2538; -.
PRO; PR:P35575; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131482; -.
CleanEx; HS_G6PC; -.
ExpressionAtlas; P35575; baseline and differential.
Genevisible; P35575; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:UniProtKB.
GO; GO:0042301; F:phosphate ion binding; IMP:UniProtKB.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0006094; P:gluconeogenesis; IMP:UniProtKB.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0015760; P:glucose-6-phosphate transport; IEA:Ensembl.
GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl.
GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0032094; P:response to food; IEA:Ensembl.
GO; GO:0008202; P:steroid metabolic process; IEA:Ensembl.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0046415; P:urate metabolic process; IEA:Ensembl.
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; Disease mutation;
Endoplasmic reticulum; Gluconeogenesis; Glycogen storage disease;
Glycoprotein; Hydrolase; Membrane; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 357 Glucose-6-phosphatase.
/FTId=PRO_0000087413.
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 203 209 Cytoplasmic. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TOPO_DOM 231 254 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}.
ACT_SITE 119 119 Proton donor. {ECO:0000255}.
ACT_SITE 176 176 Nucleophile.
{ECO:0000269|PubMed:12093795}.
BINDING 83 83 Substrate. {ECO:0000255}.
BINDING 170 170 Substrate. {ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:9705299}.
VAR_SEQ 115 175 SPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVIL
WLGFWAVQLNVCLSRIYLAA -> KDKADLQISVLECHFVV
GILGCAAECLSVTNLPCCSFSSSSCCWSPVRHCCCRNFQPH
PQH (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047558.
VAR_SEQ 176 356 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047559.
VARIANT 5 5 M -> R (in GSD1A).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046249.
VARIANT 16 16 T -> A (in GSD1A; dbSNP:rs761839506).
{ECO:0000269|PubMed:10738005}.
/FTId=VAR_046250.
VARIANT 16 16 T -> R (in GSD1A; complete loss of
activity and reduced enzyme stability).
{ECO:0000269|PubMed:15542400}.
/FTId=VAR_046251.
VARIANT 20 20 Q -> R (in GSD1A).
{ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_009202.
VARIANT 38 38 D -> V (in GSD1A; dbSNP:rs104894565).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005237.
VARIANT 54 54 Q -> P (in GSD1A).
{ECO:0000269|PubMed:10447271,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:15542400}.
/FTId=VAR_009203.
VARIANT 63 63 W -> R (in GSD1A).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_046252.
VARIANT 65 65 A -> P (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046253.
VARIANT 68 68 G -> R (in GSD1A).
{ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:9700613}.
/FTId=VAR_046254.
VARIANT 76 76 K -> N (in GSD1A; loss of catalytic
activity). {ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:12093795}.
/FTId=VAR_046255.
VARIANT 77 77 W -> R (in GSD1A; dbSNP:rs104894566).
{ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005238.
VARIANT 81 81 G -> R (in GSD1A; dbSNP:rs756632286).
{ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_009204.
VARIANT 83 83 R -> C (in GSD1A; complete loss of
activity; prevalent mutation in Ashkenazi
Jewish population; dbSNP:rs1801175).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12093795,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:15316959,
ECO:0000269|PubMed:15542400,
ECO:0000269|PubMed:7623438,
ECO:0000269|PubMed:8182131,
ECO:0000269|PubMed:9332655,
ECO:0000269|PubMed:9506659,
ECO:0000269|PubMed:9700612}.
/FTId=VAR_005239.
VARIANT 83 83 R -> H (in GSD1A; dbSNP:rs1801176).
{ECO:0000269|PubMed:10748407,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:9001800}.
/FTId=VAR_005240.
VARIANT 83 83 R -> I (in GSD1A).
{ECO:0000269|PubMed:7655466}.
/FTId=VAR_005241.
VARIANT 108 108 T -> I (in GSD1A).
{ECO:0000269|PubMed:10447271,
ECO:0000269|PubMed:11058903}.
/FTId=VAR_009205.
VARIANT 110 110 E -> K (in GSD1A; dbSNP:rs104894567).
{ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005242.
VARIANT 111 111 T -> I (in GSD1A).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046256.
VARIANT 113 113 P -> L (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046257.
VARIANT 116 116 P -> L (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035922.
VARIANT 119 119 H -> L (in GSD1A).
{ECO:0000269|PubMed:11058910}.
/FTId=VAR_046258.
VARIANT 122 122 G -> D (in GSD1A; dbSNP:rs759982943).
{ECO:0000269|PubMed:10748407,
ECO:0000269|PubMed:15151508}.
/FTId=VAR_046259.
VARIANT 124 124 A -> T (in GSD1A; dbSNP:rs104894568).
{ECO:0000269|PubMed:8733042}.
/FTId=VAR_005243.
VARIANT 156 156 W -> L (in GSD1A).
{ECO:0000269|PubMed:10612834,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_009206.
VARIANT 166 166 V -> A (in GSD1A).
{ECO:0000269|PubMed:10874313}.
/FTId=VAR_046260.
VARIANT 166 166 V -> G (in GSD1A; complete loss of
activity; dbSNP:rs104894571).
{ECO:0000269|PubMed:7623438,
ECO:0000269|PubMed:9332655}.
/FTId=VAR_005244.
VARIANT 170 170 R -> Q (in GSD1A; loss of catalytic
activity; dbSNP:rs750470654).
{ECO:0000269|PubMed:12093795,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:9700612}.
/FTId=VAR_046261.
VARIANT 177 177 F -> C (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046262.
VARIANT 178 178 P -> A (in GSD1A; dbSNP:rs763543607).
{ECO:0000269|PubMed:15151508}.
/FTId=VAR_065164.
VARIANT 178 178 P -> S (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046263.
VARIANT 179 179 H -> P (in GSD1A).
{ECO:0000269|PubMed:10748407}.
/FTId=VAR_046264.
VARIANT 184 184 G -> E (in GSD1A; dbSNP:rs104894569).
{ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005245.
VARIANT 184 184 G -> V (in GSD1A).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_046265.
VARIANT 188 188 G -> D (in GSD1A; dbSNP:rs760981149).
{ECO:0000269|PubMed:10612834}.
/FTId=VAR_009207.
VARIANT 188 188 G -> R (in GSD1A; complete loss of
activity; dbSNP:rs80356482).
{ECO:0000269|PubMed:10874313,
ECO:0000269|PubMed:10960498,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566,
ECO:0000269|PubMed:8733042}.
/FTId=VAR_005246.
VARIANT 188 188 G -> S (in GSD1A; dbSNP:rs80356482).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046266.
VARIANT 209 209 Y -> C (in GSD1A; complete loss of
activity and reduced enzyme stability).
{ECO:0000269|PubMed:15542400}.
/FTId=VAR_046268.
VARIANT 211 211 L -> P (in GSD1A).
{ECO:0000269|PubMed:8733042}.
/FTId=VAR_005247.
VARIANT 222 222 G -> R (in GSD1A).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_005248.
VARIANT 236 236 W -> R (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046269.
VARIANT 241 241 A -> T (in GSD1A).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046270.
VARIANT 255 255 T -> I (in GSD1A).
{ECO:0000269|PubMed:15151508}.
/FTId=VAR_065165.
VARIANT 257 257 P -> L (in GSD1A).
{ECO:0000269|PubMed:10748407}.
/FTId=VAR_046271.
VARIANT 264 264 N -> K (in GSD1A).
{ECO:0000269|PubMed:9506659}.
/FTId=VAR_046272.
VARIANT 265 265 L -> P (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046273.
VARIANT 266 266 G -> V (in GSD1A).
{ECO:0000269|PubMed:10094563}.
/FTId=VAR_005249.
VARIANT 270 270 G -> R (in GSD1A).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046274.
VARIANT 270 270 G -> V (in GSD1A; dbSNP:rs80356483).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_005250.
VARIANT 270 270 G -> W (in GSD1A).
{ECO:0000269|PubMed:9700612}.
/FTId=VAR_046275.
VARIANT 295 295 R -> C (in GSD1A; dbSNP:rs104894563).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:10874313}.
/FTId=VAR_005251.
VARIANT 298 298 S -> P (in GSD1A; dbSNP:rs770003650).
{ECO:0000269|PubMed:10070617}.
/FTId=VAR_046276.
VARIANT 322 322 F -> L (in GSD1A).
{ECO:0000269|PubMed:11058903}.
/FTId=VAR_046277.
VARIANT 327 327 Missing (in GSD1A).
{ECO:0000269|PubMed:11058903,
ECO:0000269|PubMed:12373566}.
/FTId=VAR_005252.
VARIANT 338 338 V -> F (in GSD1A; dbSNP:rs367727229).
{ECO:0000269|PubMed:10070617,
ECO:0000269|PubMed:10094563,
ECO:0000269|PubMed:11058903}.
/FTId=VAR_005253.
VARIANT 341 341 I -> N (in GSD1A; dbSNP:rs387906505).
{ECO:0000269|PubMed:9001800}.
/FTId=VAR_005254.
VARIANT 345 345 L -> R (in GSD1A).
{ECO:0000269|PubMed:12373566}.
/FTId=VAR_046278.
MUTAGEN 9 9 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 52 52 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 119 119 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 176 176 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 179 179 H->A: Loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 197 197 H->T: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 252 252 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 307 307 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
MUTAGEN 353 353 H->A: Partial loss of catalytic activity.
{ECO:0000269|PubMed:12093795}.
CONFLICT 109 109 C -> R (in Ref. 2; BAG64735).
{ECO:0000305}.
CONFLICT 192 192 A -> T (in Ref. 1; AAA16222).
{ECO:0000305}.
SEQUENCE 357 AA; 40484 MW; 2FEA1C78928A9919 CRC64;
MEEGMNVLHD FGIQSTHYLQ VNYQDSQDWF ILVSVIADLR NAFYVLFPIW FHLQEAVGIK
LLWVAVIGDW LNLVFKWILF GQRPYWWVLD TDYYSNTSVP LIKQFPVTCE TGPGSPSGHA
MGTAGVYYVM VTSTLSIFQG KIKPTYRFRC LNVILWLGFW AVQLNVCLSR IYLAAHFPHQ
VVAGVLSGIA VAETFSHIHS IYNASLKKYF LITFFLFSFA IGFYLLLKGL GVDLLWTLEK
AQRWCEQPEW VHIDTTPFAS LLKNLGTLFG LGLALNSSMY RESCKGKLSK WLPFRLSSIV
ASLVLLHVFD SLKPPSQVEL VFYVLSFCKS AVVPLASVSV IPYCLAQVLG QPHKKSL


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