G6PC1_HUMAN
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 03-AUG-2022, entry version 196.
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>3.0.co;2-y;
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};
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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; 3.
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 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; P35575; -.
DR PeptideAtlas; P35575; -.
DR PRIDE; P35575; -.
DR ProteomicsDB; 55092; -. [P35575-1]
DR Antibodypedia; 29454; 137 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 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; RRWCERP; -.
DR OrthoDB; 743717at2759; -.
DR PhylomeDB; P35575; -.
DR TreeFam; TF324388; -.
DR BioCyc; MetaCyc:HS05538-MON; -.
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; 12 hits in 1073 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 tissues.
DR ExpressionAtlas; P35575; baseline and differential.
DR Genevisible; P35575; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; TAS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 InterPro; IPR016275; Glucose-6-phosphatase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR PIRSF; PIRSF000905; Glucose-6-phosphatase; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
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 glucose-6-
FT phosphatase activity and reduced enzyme stability;
FT dbSNP:rs1555558914)"
FT /evidence="ECO:0000269|PubMed:15542400"
FT /id="VAR_046251"
FT VARIANT 20
FT /note="Q -> R (in GSD1A)"
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 /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 glucose-6-
FT phosphatase activity; prevalent mutation in Ashkenazi
FT 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 glucose-6-
FT 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 glucose-6-
FT 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 glucose-6-
FT phosphatase activity and reduced enzyme stability)"
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)"
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
