ID G6PC1_HUMAN Reviewed; 357 AA. AC P35575; A1L4C0; B4E1C3; K7EL82; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 2. DT 24-JAN-2024, entry version 204. DE RecName: Full=Glucose-6-phosphatase catalytic subunit 1 {ECO:0000312|HGNC:HGNC:4056}; DE EC=3.1.3.9 {ECO:0000269|PubMed:10960498, ECO:0000269|PubMed:12093795, ECO:0000269|PubMed:15542400, ECO:0000269|PubMed:9332655}; DE AltName: Full=Glucose-6-phosphatase; DE Short=G-6-Pase; DE Short=G6Pase; DE AltName: Full=Glucose-6-phosphatase alpha; DE Short=G6Pase-alpha; GN Name=G6PC1 {ECO:0000312|HGNC:HGNC:4056}; Synonyms=G6PC, G6PT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=8211187; DOI=10.1126/science.8211187; RA Lei K.-J., Shelly L.L., Pan C.-J., Sidbury J.B., Chou J.Y.; RT "Mutations in the glucose-6-phosphatase gene that cause glycogen storage RT disease type 1a."; RL Science 262:580-583(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 TOPOLOGY, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-176, ACTIVE RP SITE, AND SUBCELLULAR LOCATION. RX PubMed=9497333; DOI=10.1074/jbc.273.11.6144; RA Pan C.J., Lei K.J., Annabi B., Hemrika W., Chou J.Y.; RT "Transmembrane topology of glucose-6-phosphatase."; RL J. Biol. Chem. 273:6144-6148(1998). RN [6] RP GLYCOSYLATION AT ASN-96. RX PubMed=9705299; DOI=10.1074/jbc.273.34.21658; RA Pan C.J., Lei K.J., Chou J.Y.; RT "Asparagine-linked oligosaccharides are localized to a luminal hydrophilic RT loop in human glucose-6-phosphatase."; RL J. Biol. Chem. 273:21658-21662(1998). RN [7] RP ACTIVE SITES, MUTAGENESIS OF HIS-9; HIS-52; HIS-119; HIS-176; HIS-179; RP HIS-197; HIS-252; HIS-307 AND HIS-353, CHARACTERIZATION OF VARIANTS ASN-76; RP CYS-83 AND GLN-170, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=12093795; DOI=10.1074/jbc.m201853200; RA Ghosh A., Shieh J.-J., Pan C.-J., Sun M.-S., Chou J.Y.; RT "The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile RT forming the phosphohistidine-enzyme intermediate during catalysis."; RL J. Biol. Chem. 277:32837-32842(2002). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-96. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [9] RP VARIANT GSD1A CYS-83. RX PubMed=8182131; DOI=10.1172/jci117192; RA Lei K.J., Pan C.J., Shelly L.L., Liu J.L., Chou J.Y.; RT "Identification of mutations in the gene for glucose-6-phosphatase, the RT enzyme deficient in glycogen storage disease type 1a."; RL J. Clin. Invest. 93:1994-1999(1994). RN [10] RP VARIANTS GSD1A. RX PubMed=7573034; RA Lei K.-J., Chen Y.-T., Chen H., Wong L.-J.C., Liu J.-L., RA McConkie-Rosell A., van Hove J.L.K., Ou H.C.-Y., Yeh N.J., Pan L.Y., RA Chou J.Y.; RT "Genetic basis of glycogen storage disease type 1a: prevalent mutations at RT the glucose-6-phosphatase locus."; RL Am. J. Hum. Genet. 57:766-771(1995). RN [11] RP VARIANTS GSD1A CYS-83 AND GLY-166. RX PubMed=7623438; DOI=10.1007/bf00711368; RA Parvari R., Moses S., Hershkovitz E., Carmi R., Bashan N.; RT "Characterization of the mutations in the glucose-6-phosphatase gene in RT Israeli patients with glycogen storage disease type 1a: R83C in six Jews RT and a novel V166G mutation in a Muslim Arab."; RL J. Inherit. Metab. Dis. 18:21-27(1995). RN [12] RP VARIANT GSD1A ILE-83. RX PubMed=7655466; DOI=10.1093/hmg/4.6.1095; RA Hwu W.-L., Chuang S.-C., Tsai L.-P., Chang M.-H., Chuang S.-M., Wang T.-R.; RT "Glucose-6-phosphatase gene G327A mutation is common in Chinese patients RT with glycogen storage disease type Ia."; RL Hum. Mol. Genet. 4:1095-1096(1995). RN [13] RP VARIANTS GSD1A HIS-83 AND ASN-341. RX PubMed=9001800; DOI=10.1111/j.1399-0004.1996.tb02627.x; RA Lee W.J., Lee H.M., Chi C.S., Shu S.G., Lin L.Y., Lin W.H.; RT "Genetic analysis of the glucose-6-phosphatase mutation of type 1a glycogen RT storage disease in a Chinese family."; RL Clin. Genet. 50:206-211(1996). RN [14] RP VARIANTS GSD1A VAL-38; ARG-77; LYS-110; THR-124; GLU-184; ARG-188 AND RP PRO-211. RX PubMed=8733042; DOI=10.1136/jmg.33.5.358; RA Chevalier-Porst F., Bozon D., Bonardot A.-M., Bruni N., Mithieux G., RA Mathieu M., Maire I.; RT "Mutation analysis in 24 French patients with glycogen storage disease type RT 1a."; RL J. Med. Genet. 33:358-360(1996). RN [15] RP VARIANTS GSD1A CYS-83 AND GLY-166, CHARACTERIZATION OF VARIANT GSD1A RP GLY-166, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9332655; RX DOI=10.1002/(sici)1096-8628(19971031)72:3<286::aid-ajmg6>3.0.co;2-p; RA Parvari R., Lei K.J., Bashan N., Hershkovitz E., Korman S.H., Barash V., RA Lerman-Sagie T., Mandel H., Chou J.Y., Moses S.W.; RT "Glycogen storage disease type 1a in Israel: biochemical, clinical, and RT mutational studies."; RL Am. J. Med. Genet. 72:286-290(1997). RN [16] RP VARIANTS GSD1A CYS-83; GLN-170 AND TRP-270. RX PubMed=9700612; DOI=10.1023/a:1005339616074; RA Huener G., Podskarbi T., Schuetz M., Baykal T., Sarbat G., Shin Y.S., RA Demirkol M.; RT "Molecular aspects of glycogen storage disease type Ia in Turkish patients: RT a novel mutation in the glucose-6-phosphatase gene."; RL J. Inherit. Metab. Dis. 21:445-446(1998). RN [17] RP VARIANT GSD1A ARG-68. RX PubMed=9700613; DOI=10.1023/a:1005391600145; RA Sartorato E.L., Reis F.C., Norato D.Y.J., Hackel C.; RT "A novel mutation in a Brazilian patient with glycogen storage disease type RT 1a."; RL J. Inherit. Metab. Dis. 21:447-447(1998). RN [18] RP VARIANTS GSD1A CYS-83 AND LYS-264. RX PubMed=9506659; DOI=10.1016/s0022-3476(98)70463-9; RA Keller K.M., Schuetz M., Podskarbi T., Bindl L., Lentze M.J., Shin Y.S.; RT "A new mutation of the glucose-6-phosphatase gene in a 4-year-old girl with RT oligosymptomatic glycogen storage disease type 1a."; RL J. Pediatr. 132:360-361(1998). RN [19] RP VARIANTS GSD1A VAL-266 AND PHE-338. RX PubMed=10094563; RX DOI=10.1002/(sici)1098-1004(1999)13:2<173::aid-humu19>3.0.co;2-e; RA Rake J.P., ten Berge A.M., Verlind E., Visser G., Niezen-Koning K.E., RA Buys C.H.C.M., Smit G.P., Scheffer H.; RT "Glycogen storage disease type Ia: four novel mutations (175delGG, R170X, RT G266V and V338F) identified."; RL Hum. Mutat. 13:173-173(1999). RN [20] RP VARIANTS GSD1A PRO-54 AND ILE-108. RX PubMed=10447271; RX DOI=10.1002/(sici)1098-1004(1999)14:1<91::aid-humu21>3.0.co;2-b; RA Trioche P., Francoual J., Chalas J., Capel L., Bernard O., Labrune P.; RT "Identification of three novel mutations (Q54P, W70X and T108I) in the RT glucose-6-phosphatase gene of patients with glycogen storage disease type RT Ia."; RL Hum. Mutat. 14:91-91(1999). RN [21] RP VARIANTS GSD1A VAL-38; ARG-63; CYS-83; VAL-184; ARG-222; VAL-270; CYS-295; RP PRO-298 AND PHE-338. RX PubMed=10070617; DOI=10.1023/a:1005495131118; RA Stroppiano M., Regis S., DiRocco M., Caroli F., Gandullia P., Gatti R.; RT "Mutations in the glucose-6-phosphatase gene of 53 Italian patients with RT glycogen storage disease type Ia."; RL J. Inherit. Metab. Dis. 22:43-49(1999). RN [22] RP VARIANTS GSD1A HIS-83; ASP-122; PRO-179 AND LEU-257. RX PubMed=10748407; RX DOI=10.1002/(sici)1096-8628(20000313)91:2<107::aid-ajmg5>3.3.co;2-p; RA Akanuma J., Nishigaki T., Fujii K., Matsubara Y., Inui K., Takahashi K., RA Kure S., Suzuki Y., Ohura T., Miyabayashi S., Ogawa E., Iinuma K., RA Okada S., Narisawa K.; RT "Glycogen storage disease type Ia: molecular diagnosis of 51 Japanese RT patients and characterization of splicing mutations by analysis of RT ectopically transcribed mRNA from lymphoblastoid cells."; RL Am. J. Med. Genet. 91:107-112(2000). RN [23] RP VARIANTS GSD1A ARG-20; ARG-81; LEU-156 AND ASP-188. RX PubMed=10612834; RX DOI=10.1002/(sici)1098-1004(200001)15:1<115::aid-humu23>3.0.co;2-w; RA Seydewitz H.H., Matern D.; RT "Molecular genetic analysis of 40 patients with glycogen storage disease RT type Ia: 100% mutation detection rate and 5 novel mutations."; RL Hum. Mutat. 15:115-116(2000). RN [24] RP VARIANT GSD1A ALA-16. RX PubMed=10738005; RX DOI=10.1002/(sici)1098-1004(200004)15:4<390::aid-humu32>3.0.co;2-n; RA Wu M.-C., Tsai F.-J., Lee C.-C., Lin S.-P., Wu J.-Y.; RT "Identification of a novel missense mutation (T16A) in the glucose-6- RT phosphatase gene in a Taiwan Chinese patient with glycogen storage disease RT Ia (von Gierke disease)."; RL Hum. Mutat. 15:390-390(2000). RN [25] RP VARIANTS GSD1A ASN-76; ARG-77; CYS-83; ALA-166; ARG-188 AND CYS-295. RX PubMed=10874313; RX DOI=10.1002/1098-1004(200007)16:1<89::aid-humu17>3.0.co;2-a; RA Kozak L., Francova H., Hrabincova E., Stastna S., Peskova K., Elleder M.; RT "Identification of mutations in the glucose-6-phosphatase gene in Czech and RT Slovak patients with glycogen storage disease type Ia, including novel RT mutations K76N, V166A and 540del5."; RL Hum. Mutat. 16:89-89(2000). RN [26] RP VARIANTS GSD1A ARG-5; VAL-38; PRO-54; CYS-83; ILE-108; LYS-110; ILE-111; RP GLU-184; ARG-188; THR-241; ARG-270; VAL-270; LEU-322; PHE-327 DEL AND RP PHE-338. RX PubMed=11058903; RX DOI=10.1002/1098-1004(200011)16:5<444::aid-humu10>3.0.co;2-f; RA Trioche P., Francoual J., Chalas J., Capel L., Lindenbaum A., Odievre M., RA Labrune P.; RT "Genetic heterogeneity of glycogen storage disease type Ia in France: a RT study of 48 patients."; RL Hum. Mutat. 16:444-444(2000). RN [27] RP VARIANT GSD1A LEU-119. RX PubMed=11058910; RX DOI=10.1002/1098-1004(200011)16:5<447::aid-humu17>3.0.co;2-m; RA Wu M.-C., Tsai F.-J., Lee C.-C., Tsai C.-H., Wu J.-Y.; RT "A novel missense mutation (H119L) identified in a Taiwan Chinese family RT with glycogen storage disease Ia (von Gierke disease)."; RL Hum. Mutat. 16:447-447(2000). RN [28] RP VARIANT GSD1A ARG-188, CHARACTERIZATION OF VARIANT GSD1A ARG-188, CATALYTIC RP ACTIVITY, AND FUNCTION. RX PubMed=10960498; DOI=10.1203/00006450-200009000-00011; RA Weston B.W., Lin J.L., Muenzer J., Cameron H.S., Arnold R.R., RA Seydewitz H.H., Mayatepek E., Van Schaftingen E., Veiga-da-Cunha M., RA Matern D., Chen Y.T.; RT "Glucose-6-phosphatase mutation G188R confers an atypical glycogen storage RT disease type 1b phenotype."; RL Pediatr. Res. 48:329-334(2000). RN [29] RP VARIANTS GSD1A ARG-20; VAL-38; PRO-65; ARG-68; ARG-77; ARG-81; CYS-83; RP HIS-83; LYS-110; LEU-113; LEU-156; GLN-170; CYS-177; SER-178; ARG-188; RP SER-188; ARG-236; PRO-265; VAL-270; PHE-327 DEL AND ARG-345. RX PubMed=12373566; DOI=10.1007/s00431-002-0998-5; RA Matern D., Seydewitz H.H., Bali D., Lang C., Chen Y.-T.; RT "Glycogen storage disease type I: diagnosis and phenotype/genotype RT correlation."; RL Eur. J. Pediatr. 161:S10-S19(2002). RN [30] RP VARIANT GSD1A CYS-83. RX PubMed=15316959; DOI=10.1002/ajmg.a.30232; RA Ekstein J., Rubin B.Y., Anderson S.L., Weinstein D.A., Bach G., RA Abeliovich D., Webb M., Risch N.; RT "Mutation frequencies for glycogen storage disease Ia in the Ashkenazi RT Jewish population."; RL Am. J. Med. Genet. A 129:162-164(2004). RN [31] RP VARIANTS GSD1A ASP-122; ALA-178 AND ILE-255. RX PubMed=15151508; DOI=10.1111/j.1399-0004.2004.00260.x; RA Ki C.S., Han S.H., Kim H.J., Lee S.G., Kim E.J., Kim J.W., Choe Y.H., RA Seo J.K., Chang Y.J., Park J.Y.; RT "Mutation spectrum of the glucose-6-phosphatase gene and its implication in RT molecular diagnosis of Korean patients with glycogen storage disease type RT Ia."; RL Clin. Genet. 65:487-489(2004). RN [32] RP VARIANTS GSD1A ARG-16; PRO-54; CYS-83 AND CYS-209, CHARACTERIZATION OF RP VARIANTS GSD1A ARG-16 AND CYS-209, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=15542400; DOI=10.1016/j.ymgme.2004.06.010; RA Angaroni C.J., de Kremer R.D., Argarana C.E., Paschini-Capra A.E., RA Giner-Ayala A.N., Pezza R.J., Pan C.-J., Chou J.Y.; RT "Glycogen storage disease type Ia in Argentina: two novel glucose-6- RT phosphatase mutations affecting protein stability."; RL Mol. Genet. Metab. 83:276-279(2004). RN [33] RP VARIANT [LARGE SCALE ANALYSIS] LEU-116. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). 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:10960498, ECO:0000269|PubMed:12093795, CC ECO:0000269|PubMed:15542400, ECO:0000269|PubMed:9332655, CC ECO:0000269|PubMed:9497333}. 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:10960498, ECO:0000269|PubMed:12093795, CC ECO:0000269|PubMed:15542400, ECO:0000269|PubMed:9332655, CC ECO:0000269|PubMed:9497333}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000305|PubMed:12093795}. CC -!- INTERACTION: CC P35575; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-3906612, EBI-396669; CC P35575; O76024: WFS1; NbExp=3; IntAct=EBI-3906612, EBI-720609; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000303|PubMed:9497333}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P35575-1; Sequence=Displayed; CC Name=2; CC IsoId=P35575-2; Sequence=VSP_047558, VSP_047559; CC -!- DISEASE: Glycogen storage disease 1A (GSD1A) [MIM:232200]: A metabolic CC disorder characterized by impairment of terminal steps of CC glycogenolysis and gluconeogenesis. Patients manifest a wide range of CC clinical symptoms and biochemical abnormalities, including CC hypoglycemia, severe hepatomegaly due to excessive accumulation of CC glycogen, kidney enlargement, growth retardation, lactic acidemia, CC hyperlipidemia, and hyperuricemia. {ECO:0000269|PubMed:10070617, CC ECO:0000269|PubMed:10094563, ECO:0000269|PubMed:10447271, CC ECO:0000269|PubMed:10612834, ECO:0000269|PubMed:10738005, CC ECO:0000269|PubMed:10748407, ECO:0000269|PubMed:10874313, CC ECO:0000269|PubMed:10960498, ECO:0000269|PubMed:11058903, CC ECO:0000269|PubMed:11058910, ECO:0000269|PubMed:12373566, CC ECO:0000269|PubMed:15151508, ECO:0000269|PubMed:15316959, CC ECO:0000269|PubMed:15542400, ECO:0000269|PubMed:7573034, CC ECO:0000269|PubMed:7623438, ECO:0000269|PubMed:7655466, CC ECO:0000269|PubMed:8182131, ECO:0000269|PubMed:8733042, CC ECO:0000269|PubMed:9001800, ECO:0000269|PubMed:9332655, CC ECO:0000269|PubMed:9506659, ECO:0000269|PubMed:9700612, CC ECO:0000269|PubMed:9700613}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the glucose-6-phosphatase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG64735.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U01120; AAA16222.1; -; mRNA. DR EMBL; AK303771; BAG64735.1; ALT_INIT; mRNA. DR EMBL; AK313982; BAG36695.1; -; mRNA. DR EMBL; AC016889; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC130478; AAI30479.1; -; mRNA. DR EMBL; BC136369; AAI36370.1; -; mRNA. DR CCDS; CCDS11446.1; -. [P35575-1] DR CCDS; CCDS59291.1; -. [P35575-2] DR PIR; A48251; A48251. DR RefSeq; NP_000142.2; NM_000151.3. [P35575-1] DR RefSeq; NP_001257326.1; NM_001270397.1. [P35575-2] DR AlphaFoldDB; P35575; -. DR BioGRID; 108813; 5. DR IntAct; P35575; 5. DR STRING; 9606.ENSP00000253801; -. DR BindingDB; P35575; -. DR ChEMBL; CHEMBL2282; -. DR DEPOD; G6PC; -. DR GlyConnect; 1267; 1 N-Linked glycan (1 site). DR GlyCosmos; P35575; 1 site, 1 glycan. DR GlyGen; P35575; 1 site, 1 N-linked glycan (1 site). DR iPTMnet; P35575; -. DR PhosphoSitePlus; P35575; -. DR BioMuta; G6PC; -. DR DMDM; 206729864; -. DR jPOST; P35575; -. DR MassIVE; P35575; -. DR PaxDb; 9606-ENSP00000253801; -. DR PeptideAtlas; P35575; -. DR ProteomicsDB; 55092; -. [P35575-1] DR Antibodypedia; 29454; 194 antibodies from 24 providers. DR DNASU; 2538; -. DR Ensembl; ENST00000253801.7; ENSP00000253801.1; ENSG00000131482.10. [P35575-1] DR Ensembl; ENST00000592383.5; ENSP00000465958.1; ENSG00000131482.10. [P35575-2] DR GeneID; 2538; -. DR KEGG; hsa:2538; -. DR MANE-Select; ENST00000253801.7; ENSP00000253801.1; NM_000151.4; NP_000142.2. DR UCSC; uc002icb.3; human. [P35575-1] DR AGR; HGNC:4056; -. DR CTD; 2538; -. DR DisGeNET; 2538; -. DR GeneCards; G6PC1; -. DR GeneReviews; G6PC1; -. DR HGNC; HGNC:4056; G6PC1. DR HPA; ENSG00000131482; Group enriched (kidney, liver). DR MalaCards; G6PC1; -. DR MIM; 232200; phenotype. DR MIM; 613742; gene. DR neXtProt; NX_P35575; -. DR OpenTargets; ENSG00000131482; -. DR Orphanet; 79258; Glycogen storage disease due to glucose-6-phosphatase deficiency type Ia. DR VEuPathDB; HostDB:ENSG00000131482; -. DR eggNOG; ENOG502QS9B; Eukaryota. DR GeneTree; ENSGT00950000183150; -. DR HOGENOM; CLU_052517_0_0_1; -. DR InParanoid; P35575; -. DR OMA; WFILVSM; -. DR OrthoDB; 4030642at2759; -. DR PhylomeDB; P35575; -. DR TreeFam; TF324388; -. DR BioCyc; MetaCyc:HS05538-MONOMER; -. DR BRENDA; 3.1.3.9; 2681. DR PathwayCommons; P35575; -. DR Reactome; R-HSA-3274531; Glycogen storage disease type Ia (G6PC). DR Reactome; R-HSA-70263; Gluconeogenesis. DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes. DR SABIO-RK; P35575; -. DR SignaLink; P35575; -. DR SIGNOR; P35575; -. DR UniPathway; UPA00138; -. DR BioGRID-ORCS; 2538; 14 hits in 1174 CRISPR screens. DR ChiTaRS; G6PC; human. DR GeneWiki; G6PC; -. DR GenomeRNAi; 2538; -. DR Pharos; P35575; Tchem. DR PRO; PR:P35575; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P35575; Protein. DR Bgee; ENSG00000131482; Expressed in right lobe of liver and 49 other cell types or tissues. DR ExpressionAtlas; P35575; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0004346; F:glucose-6-phosphatase activity; IDA:UniProtKB. DR GO; GO:0042301; F:phosphate ion binding; IMP:UniProtKB. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:Ensembl. DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IMP:UniProtKB. DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB. DR GO; GO:0015760; P:glucose-6-phosphate transport; IEA:Ensembl. DR GO; GO:0005980; P:glycogen catabolic process; IEA:Ensembl. DR GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc. DR GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl. DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl. DR GO; GO:0008202; P:steroid metabolic process; IEA:Ensembl. DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl. DR GO; GO:0046415; P:urate metabolic process; IEA:Ensembl. 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; P35575; HS. PE 1: Evidence at protein level; KW Alternative splicing; Disease variant; Endoplasmic reticulum; KW Gluconeogenesis; Glycogen storage disease; Glycoprotein; Hydrolase; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..357 FT /note="Glucose-6-phosphatase catalytic subunit 1" FT /id="PRO_0000087413" FT TOPO_DOM 1..28 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 29..49 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 50..60 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 61..81 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 82..117 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 118..138 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 139..147 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 148..168 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 169..179 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 180..202 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 203..209 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 210..230 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 231..254 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 255..275 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 276..291 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 292..312 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 313..320 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:9497333" FT TRANSMEM 321..341 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 342..357 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:9497333" FT ACT_SITE 119 FT /note="Proton donor" FT /evidence="ECO:0000255" FT ACT_SITE 176 FT /note="Nucleophile" FT /evidence="ECO:0000269|PubMed:12093795, FT ECO:0000269|PubMed:9497333" 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:0000269|PubMed:19159218, FT ECO:0000269|PubMed:9705299" FT VAR_SEQ 115..175 FT /note="SPSGHAMGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNV FT CLSRIYLAA -> KDKADLQISVLECHFVVGILGCAAECLSVTNLPCCSFSSSSCCWSP FT VRHCCCRNFQPHPQH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047558" FT VAR_SEQ 176..356 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047559" FT VARIANT 5 FT /note="M -> R (in GSD1A; dbSNP:rs1250172816)" FT /evidence="ECO:0000269|PubMed:11058903" FT /id="VAR_046249" FT VARIANT 16 FT /note="T -> A (in GSD1A; dbSNP:rs761839506)" FT /evidence="ECO:0000269|PubMed:10738005" FT /id="VAR_046250" FT VARIANT 16 FT /note="T -> R (in GSD1A; complete loss of FT glucose-6-phosphatase activity and reduced enzyme FT stability; dbSNP:rs1555558914)" FT /evidence="ECO:0000269|PubMed:15542400" FT /id="VAR_046251" FT VARIANT 20 FT /note="Q -> R (in GSD1A; dbSNP:rs2056021410)" FT /evidence="ECO:0000269|PubMed:10612834, FT ECO:0000269|PubMed:12373566" FT /id="VAR_009202" FT VARIANT 38 FT /note="D -> V (in GSD1A; dbSNP:rs104894565)" FT /evidence="ECO:0000269|PubMed:10070617, FT ECO:0000269|PubMed:11058903, ECO:0000269|PubMed:12373566, FT ECO:0000269|PubMed:8733042" FT /id="VAR_005237" FT VARIANT 54 FT /note="Q -> P (in GSD1A; dbSNP:rs1057517008)" FT /evidence="ECO:0000269|PubMed:10447271, FT ECO:0000269|PubMed:11058903, ECO:0000269|PubMed:15542400" FT /id="VAR_009203" FT VARIANT 63 FT /note="W -> R (in GSD1A)" FT /evidence="ECO:0000269|PubMed:10070617" FT /id="VAR_046252" FT VARIANT 65 FT /note="A -> P (in GSD1A; dbSNP:rs369472089)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046253" FT VARIANT 68 FT /note="G -> R (in GSD1A; dbSNP:rs1567702819)" FT /evidence="ECO:0000269|PubMed:12373566, FT ECO:0000269|PubMed:9700613" FT /id="VAR_046254" FT VARIANT 76 FT /note="K -> N (in GSD1A; loss of catalytic activity; FT dbSNP:rs2056023296)" FT /evidence="ECO:0000269|PubMed:10874313, FT ECO:0000269|PubMed:12093795" FT /id="VAR_046255" FT VARIANT 77 FT /note="W -> R (in GSD1A; dbSNP:rs104894566)" FT /evidence="ECO:0000269|PubMed:10874313, FT ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:8733042" FT /id="VAR_005238" FT VARIANT 81 FT /note="G -> R (in GSD1A; dbSNP:rs756632286)" FT /evidence="ECO:0000269|PubMed:10612834, FT ECO:0000269|PubMed:12373566" FT /id="VAR_009204" FT VARIANT 83 FT /note="R -> C (in GSD1A; complete loss of FT glucose-6-phosphatase activity; prevalent mutation in FT Ashkenazi Jewish population; dbSNP:rs1801175)" FT /evidence="ECO:0000269|PubMed:10070617, FT ECO:0000269|PubMed:10874313, ECO:0000269|PubMed:11058903, FT ECO:0000269|PubMed:12093795, ECO:0000269|PubMed:12373566, FT ECO:0000269|PubMed:15316959, ECO:0000269|PubMed:15542400, FT ECO:0000269|PubMed:7623438, ECO:0000269|PubMed:8182131, FT ECO:0000269|PubMed:9332655, ECO:0000269|PubMed:9506659, FT ECO:0000269|PubMed:9700612" FT /id="VAR_005239" FT VARIANT 83 FT /note="R -> H (in GSD1A; dbSNP:rs1801176)" FT /evidence="ECO:0000269|PubMed:10748407, FT ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:9001800" FT /id="VAR_005240" FT VARIANT 83 FT /note="R -> I (in GSD1A)" FT /evidence="ECO:0000269|PubMed:7655466" FT /id="VAR_005241" FT VARIANT 108 FT /note="T -> I (in GSD1A; dbSNP:rs1597988331)" FT /evidence="ECO:0000269|PubMed:10447271, FT ECO:0000269|PubMed:11058903" FT /id="VAR_009205" FT VARIANT 110 FT /note="E -> K (in GSD1A; dbSNP:rs104894567)" FT /evidence="ECO:0000269|PubMed:11058903, FT ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:8733042" FT /id="VAR_005242" FT VARIANT 111 FT /note="T -> I (in GSD1A; dbSNP:rs1203167759)" FT /evidence="ECO:0000269|PubMed:11058903" FT /id="VAR_046256" FT VARIANT 113 FT /note="P -> L (in GSD1A)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046257" FT VARIANT 116 FT /note="P -> L (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035922" FT VARIANT 119 FT /note="H -> L (in GSD1A; dbSNP:rs1401928680)" FT /evidence="ECO:0000269|PubMed:11058910" FT /id="VAR_046258" FT VARIANT 122 FT /note="G -> D (in GSD1A; dbSNP:rs759982943)" FT /evidence="ECO:0000269|PubMed:10748407, FT ECO:0000269|PubMed:15151508" FT /id="VAR_046259" FT VARIANT 124 FT /note="A -> T (in GSD1A; dbSNP:rs104894568)" FT /evidence="ECO:0000269|PubMed:8733042" FT /id="VAR_005243" FT VARIANT 156 FT /note="W -> L (in GSD1A; dbSNP:rs1189630738)" FT /evidence="ECO:0000269|PubMed:10612834, FT ECO:0000269|PubMed:12373566" FT /id="VAR_009206" FT VARIANT 166 FT /note="V -> A (in GSD1A; dbSNP:rs104894571)" FT /evidence="ECO:0000269|PubMed:10874313" FT /id="VAR_046260" FT VARIANT 166 FT /note="V -> G (in GSD1A; complete loss of FT glucose-6-phosphatase activity; dbSNP:rs104894571)" FT /evidence="ECO:0000269|PubMed:7623438, FT ECO:0000269|PubMed:9332655" FT /id="VAR_005244" FT VARIANT 170 FT /note="R -> Q (in GSD1A; loss of catalytic FT glucose-6-phosphatase activity; dbSNP:rs750470654)" FT /evidence="ECO:0000269|PubMed:12093795, FT ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:9700612" FT /id="VAR_046261" FT VARIANT 177 FT /note="F -> C (in GSD1A)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046262" FT VARIANT 178 FT /note="P -> A (in GSD1A; dbSNP:rs763543607)" FT /evidence="ECO:0000269|PubMed:15151508" FT /id="VAR_065164" FT VARIANT 178 FT /note="P -> S (in GSD1A; dbSNP:rs763543607)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046263" FT VARIANT 179 FT /note="H -> P (in GSD1A)" FT /evidence="ECO:0000269|PubMed:10748407" FT /id="VAR_046264" FT VARIANT 184 FT /note="G -> E (in GSD1A; dbSNP:rs104894569)" FT /evidence="ECO:0000269|PubMed:11058903, FT ECO:0000269|PubMed:8733042" FT /id="VAR_005245" FT VARIANT 184 FT /note="G -> V (in GSD1A; dbSNP:rs104894569)" FT /evidence="ECO:0000269|PubMed:10070617" FT /id="VAR_046265" FT VARIANT 188 FT /note="G -> D (in GSD1A; dbSNP:rs760981149)" FT /evidence="ECO:0000269|PubMed:10612834" FT /id="VAR_009207" FT VARIANT 188 FT /note="G -> R (in GSD1A; complete loss of activity; FT dbSNP:rs80356482)" FT /evidence="ECO:0000269|PubMed:10874313, FT ECO:0000269|PubMed:10960498, ECO:0000269|PubMed:11058903, FT ECO:0000269|PubMed:12373566, ECO:0000269|PubMed:8733042" FT /id="VAR_005246" FT VARIANT 188 FT /note="G -> S (in GSD1A; dbSNP:rs80356482)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046266" FT VARIANT 209 FT /note="Y -> C (in GSD1A; complete loss of FT glucose-6-phosphatase activity and reduced enzyme FT stability; dbSNP:rs2056091436)" FT /evidence="ECO:0000269|PubMed:15542400" FT /id="VAR_046268" FT VARIANT 211 FT /note="L -> P (in GSD1A)" FT /evidence="ECO:0000269|PubMed:8733042" FT /id="VAR_005247" FT VARIANT 222 FT /note="G -> R (in GSD1A; dbSNP:rs1410392732)" FT /evidence="ECO:0000269|PubMed:10070617" FT /id="VAR_005248" FT VARIANT 236 FT /note="W -> R (in GSD1A; dbSNP:rs2056092151)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046269" FT VARIANT 241 FT /note="A -> T (in GSD1A)" FT /evidence="ECO:0000269|PubMed:11058903" FT /id="VAR_046270" FT VARIANT 255 FT /note="T -> I (in GSD1A)" FT /evidence="ECO:0000269|PubMed:15151508" FT /id="VAR_065165" FT VARIANT 257 FT /note="P -> L (in GSD1A)" FT /evidence="ECO:0000269|PubMed:10748407" FT /id="VAR_046271" FT VARIANT 264 FT /note="N -> K (in GSD1A; dbSNP:rs1555560149)" FT /evidence="ECO:0000269|PubMed:9506659" FT /id="VAR_046272" FT VARIANT 265 FT /note="L -> P (in GSD1A)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046273" FT VARIANT 266 FT /note="G -> V (in GSD1A)" FT /evidence="ECO:0000269|PubMed:10094563" FT /id="VAR_005249" FT VARIANT 270 FT /note="G -> R (in GSD1A; dbSNP:rs1272803483)" FT /evidence="ECO:0000269|PubMed:11058903" FT /id="VAR_046274" FT VARIANT 270 FT /note="G -> V (in GSD1A; dbSNP:rs80356483)" FT /evidence="ECO:0000269|PubMed:10070617, FT ECO:0000269|PubMed:11058903, ECO:0000269|PubMed:12373566" FT /id="VAR_005250" FT VARIANT 270 FT /note="G -> W (in GSD1A)" FT /evidence="ECO:0000269|PubMed:9700612" FT /id="VAR_046275" FT VARIANT 295 FT /note="R -> C (in GSD1A; dbSNP:rs104894563)" FT /evidence="ECO:0000269|PubMed:10070617, FT ECO:0000269|PubMed:10874313" FT /id="VAR_005251" FT VARIANT 298 FT /note="S -> P (in GSD1A; dbSNP:rs770003650)" FT /evidence="ECO:0000269|PubMed:10070617" FT /id="VAR_046276" FT VARIANT 322 FT /note="F -> L (in GSD1A; dbSNP:rs1399520060)" FT /evidence="ECO:0000269|PubMed:11058903" FT /id="VAR_046277" FT VARIANT 327 FT /note="Missing (in GSD1A)" FT /evidence="ECO:0000269|PubMed:11058903, FT ECO:0000269|PubMed:12373566" FT /id="VAR_005252" FT VARIANT 338 FT /note="V -> F (in GSD1A; dbSNP:rs367727229)" FT /evidence="ECO:0000269|PubMed:10070617, FT ECO:0000269|PubMed:10094563, ECO:0000269|PubMed:11058903" FT /id="VAR_005253" FT VARIANT 341 FT /note="I -> N (in GSD1A; dbSNP:rs387906505)" FT /evidence="ECO:0000269|PubMed:9001800" FT /id="VAR_005254" FT VARIANT 345 FT /note="L -> R (in GSD1A)" FT /evidence="ECO:0000269|PubMed:12373566" FT /id="VAR_046278" FT MUTAGEN 9 FT /note="H->A: Partial loss of glucose-6-phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12093795" FT MUTAGEN 52 FT /note="H->A: Partial loss of glucose-6-phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12093795" FT MUTAGEN 119 FT /note="H->A: Loss of glucose-6-phosphatase activity." FT /evidence="ECO:0000269|PubMed:12093795" FT MUTAGEN 176 FT /note="H->A,I,K,M,N,S,R: Loss of glucose-6-phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12093795, FT ECO:0000269|PubMed:9497333" FT MUTAGEN 179 FT /note="H->A: Loss of glucose-6-phosphatase activity." FT /evidence="ECO:0000269|PubMed:12093795" FT MUTAGEN 197 FT /note="H->T: Partial loss of glucose-6-phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12093795" FT MUTAGEN 252 FT /note="H->A: Partial loss of glucose-6-phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12093795" FT MUTAGEN 307 FT /note="H->A: Partial loss of glucose-6-phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12093795" FT MUTAGEN 353 FT /note="H->A: Partial loss of glucose-6-phosphatase FT activity." FT /evidence="ECO:0000269|PubMed:12093795" FT CONFLICT 109 FT /note="C -> R (in Ref. 2; BAG64735)" FT /evidence="ECO:0000305" FT CONFLICT 192 FT /note="A -> T (in Ref. 1; AAA16222)" FT /evidence="ECO:0000305" SQ 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 //