G6PI_MOUSE
ID G6PI_MOUSE Reviewed; 558 AA.
AC P06745; O89062; Q3TEE7; Q3TW50; Q3UUX1; Q3UY84; Q3UZJ1; Q5RJI3; Q8C675;
AC Q9JM07;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000303|PubMed:7545951};
DE Short=GPI {ECO:0000303|PubMed:7545951};
DE EC=5.3.1.9 {ECO:0000269|PubMed:2344351, ECO:0000269|PubMed:8417789};
DE AltName: Full=Autocrine motility factor {ECO:0000303|PubMed:8674049};
DE Short=AMF {ECO:0000303|PubMed:8674049};
DE AltName: Full=Neuroleukin {ECO:0000303|PubMed:3764429};
DE Short=NLK {ECO:0000303|PubMed:3764429};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000303|PubMed:15342241};
DE Short=PGI {ECO:0000303|PubMed:15342241};
DE AltName: Full=Phosphohexose isomerase {ECO:0000303|PubMed:8674049};
DE Short=PHI {ECO:0000303|PubMed:8674049};
GN Name=Gpi {ECO:0000303|PubMed:7545951};
GN Synonyms=Gpi1 {ECO:0000312|MGI:MGI:95797};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Salivary gland;
RX PubMed=3764429; DOI=10.1126/science.3764429;
RA Gurney M.E., Heinrich S.P., Lee M.R., Yin H.-S.;
RT "Molecular cloning and expression of neuroleukin, a neurotrophic factor for
RT spinal and sensory neurons.";
RL Science 234:566-574(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Head, Heart, Olfactory bulb, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PROTEIN SEQUENCE OF 28-36; 63-73; 97-104; 107-124; 148-176; 181-234;
RP 242-252; 255-273; 424-438; 455-461 AND 467-481, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 235-393.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 269-558.
RX PubMed=7545951; DOI=10.1006/geno.1994.1233;
RA Faik P., Walker J.I., Morgan M.J.;
RT "Identification of a novel tandemly repeated sequence present in an intron
RT of the glucose phosphate isomerase (GPI) gene in mouse and man.";
RL Genomics 21:122-127(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 417-543.
RC STRAIN=129;
RA Bauchwitz R.P., Tyagi S., Marras S.A.E.;
RT "Quantitative allelic discrimination of GPI-c and GPI-a using molecular
RT beacons.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND PATHWAY.
RX PubMed=7277315; DOI=10.1530/jrf.0.0630169;
RA Buehr M., McLaren A.;
RT "An electrophoretically detectable modification of glucosephosphate
RT isomerase in mouse spermatozoa.";
RL J. Reprod. Fertil. 63:169-173(1981).
RN [10]
RP IDENTITY OF NEUROLEUKIN AS PGI.
RX PubMed=3352745; DOI=10.1038/332455a0;
RA Faik P., Walker J.I.H., Redmill A.A.M., Morgan M.J.;
RT "Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3'
RT sequences.";
RL Nature 332:455-456(1988).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND PATHWAY.
RX PubMed=2344351; DOI=10.1007/bf00554824;
RA Pretsch W., Merkle S.;
RT "Glucose phosphate isomerase enzyme-activity mutants in Mus musculus:
RT genetical and biochemical characterization.";
RL Biochem. Genet. 28:97-110(1990).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8417789;
RA Merkle S., Pretsch W.;
RT "Glucose-6-phosphate isomerase deficiency associated with nonspherocytic
RT hemolytic anemia in the mouse: an animal model for the human disease.";
RL Blood 81:206-213(1993).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=8922529;
RX DOI=10.1002/(sici)1097-0177(199611)207:3<300::aid-aja7>3.0.co;2-l;
RA Kelly A., West J.D.;
RT "Genetic evidence that glycolysis is necessary for gastrulation in the
RT mouse.";
RL Dev. Dyn. 207:300-308(1996).
RN [14]
RP IDENTITY OF AMF AS PGI.
RX PubMed=8674049;
RA Watanabe H., Takehana K., Date M., Shinozaki T., Raz A.;
RT "Tumor cell autocrine motility factor is the neuroleukin/phosphohexose
RT isomerase polypeptide.";
RL Cancer Res. 56:2960-2963(1996).
RN [15]
RP ISGYLATION.
RX PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT human cells.";
RL Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142 AND LYS-454, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-454, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH G6P, AND ACTIVE SITE.
RX PubMed=15342241; DOI=10.1016/j.jmb.2004.07.085;
RA Solomons J.T.G., Zimmerly E.M., Burns S., Krishnamurthy N., Swan M.K.,
RA Krings S., Muirhead H., Chirgwin J., Davies C.;
RT "The crystal structure of mouse phosphoglucose isomerase at 1.6A resolution
RT and its complex with glucose 6-phosphate reveals the catalytic mechanism of
RT sugar ring opening.";
RL J. Mol. Biol. 342:847-860(2004).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-557 IN COMPLEX WITH INHIBITORS.
RX PubMed=16375918; DOI=10.1016/j.jmb.2005.11.076;
RA Tanaka N., Haga A., Naba N., Shiraiwa K., Kusakabe Y., Hashimoto K.,
RA Funasaka T., Nagase H., Raz A., Nakamura K.T.;
RT "Crystal structures of mouse autocrine motility factor in complex with
RT carbohydrate phosphate inhibitors provide insight into structure-activity
RT relationship of the inhibitors.";
RL J. Mol. Biol. 356:312-324(2006).
CC -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC the reverse reaction during gluconeogenesis (PubMed:7277315,
CC PubMed:2344351, PubMed:8417789). Besides it's role as a glycolytic
CC enzyme, also acts as a secreted cytokine: acts as an angiogenic factor
CC (AMF) that stimulates endothelial cell motility (By similarity). Acts
CC as a neurotrophic factor, neuroleukin, for spinal and sensory neurons
CC (PubMed:3764429, PubMed:3352745). It is secreted by lectin-stimulated
CC T-cells and induces immunoglobulin secretion (PubMed:3352745).
CC {ECO:0000250|UniProtKB:P06744, ECO:0000269|PubMed:2344351,
CC ECO:0000269|PubMed:3352745, ECO:0000269|PubMed:3764429,
CC ECO:0000269|PubMed:7277315, ECO:0000269|PubMed:8417789}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000269|PubMed:2344351,
CC ECO:0000269|PubMed:8417789};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000269|PubMed:2344351, ECO:0000269|PubMed:7277315,
CC ECO:0000269|PubMed:8417789}.
CC -!- SUBUNIT: Homodimer in the catalytically active form, monomer in the
CC secreted form. {ECO:0000269|PubMed:15342241,
CC ECO:0000269|PubMed:16375918, ECO:0000269|PubMed:2344351}.
CC -!- INTERACTION:
CC P06745; Q2EMV9: Parp14; NbExp=4; IntAct=EBI-1534927, EBI-1534943;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06744}.
CC Secreted {ECO:0000250|UniProtKB:P06744}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality caused by impaired
CC gastrulation (PubMed:8922529). During early development, the egg
CC cylinder fails to be divided into the three cavities, suggesting a
CC deficiency in extraembryonic mesoderm formation resulting in the
CC failure to form the amnion or chorionic mesoderm (PubMed:8922529).
CC {ECO:0000269|PubMed:8922529}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36335.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M14220; AAA39825.1; -; mRNA.
DR EMBL; AK076424; BAC36335.1; ALT_INIT; mRNA.
DR EMBL; AK133827; BAE21866.1; -; mRNA.
DR EMBL; AK134890; BAE22329.1; -; mRNA.
DR EMBL; AK137805; BAE23502.1; -; mRNA.
DR EMBL; AK147124; BAE27695.1; -; mRNA.
DR EMBL; AK150341; BAE29481.1; -; mRNA.
DR EMBL; AK159838; BAE35416.1; -; mRNA.
DR EMBL; AK169681; BAE41301.1; -; mRNA.
DR EMBL; BX537302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086640; AAH86640.1; -; mRNA.
DR EMBL; BC088995; AAH88995.1; -; mRNA.
DR EMBL; U89408; AAC36515.1; -; mRNA.
DR EMBL; L09104; AAA65641.1; -; mRNA.
DR EMBL; AF108354; AAF28799.1; -; mRNA.
DR CCDS; CCDS21138.1; -.
DR PIR; A24439; NUMS.
DR RefSeq; NP_032181.2; NM_008155.4.
DR PDB; 1U0E; X-ray; 1.60 A; A/B=1-558.
DR PDB; 1U0F; X-ray; 1.60 A; A/B=1-558.
DR PDB; 1U0G; X-ray; 1.70 A; A/B=1-558.
DR PDB; 2CVP; X-ray; 1.80 A; A/B=1-557.
DR PDB; 2CXN; X-ray; 1.40 A; A/B=1-557.
DR PDB; 2CXO; X-ray; 1.80 A; A/B=1-557.
DR PDB; 2CXP; X-ray; 1.70 A; A/B=1-557.
DR PDB; 2CXQ; X-ray; 1.50 A; A/B=1-557.
DR PDB; 2CXR; X-ray; 1.70 A; A/B=1-557.
DR PDB; 2CXS; X-ray; 1.50 A; A/B=1-557.
DR PDB; 2CXT; X-ray; 1.50 A; A/B=1-557.
DR PDB; 2CXU; X-ray; 1.65 A; A/B=1-557.
DR PDBsum; 1U0E; -.
DR PDBsum; 1U0F; -.
DR PDBsum; 1U0G; -.
DR PDBsum; 2CVP; -.
DR PDBsum; 2CXN; -.
DR PDBsum; 2CXO; -.
DR PDBsum; 2CXP; -.
DR PDBsum; 2CXQ; -.
DR PDBsum; 2CXR; -.
DR PDBsum; 2CXS; -.
DR PDBsum; 2CXT; -.
DR PDBsum; 2CXU; -.
DR AlphaFoldDB; P06745; -.
DR SMR; P06745; -.
DR BioGRID; 200021; 21.
DR IntAct; P06745; 3.
DR STRING; 10090.ENSMUSP00000049355; -.
DR MoonProt; P06745; -.
DR iPTMnet; P06745; -.
DR PhosphoSitePlus; P06745; -.
DR SwissPalm; P06745; -.
DR EPD; P06745; -.
DR jPOST; P06745; -.
DR MaxQB; P06745; -.
DR PaxDb; P06745; -.
DR PeptideAtlas; P06745; -.
DR PRIDE; P06745; -.
DR ProteomicsDB; 272928; -.
DR Antibodypedia; 15715; 721 antibodies from 42 providers.
DR DNASU; 14751; -.
DR Ensembl; ENSMUST00000038027; ENSMUSP00000049355; ENSMUSG00000036427.
DR GeneID; 14751; -.
DR KEGG; mmu:14751; -.
DR UCSC; uc009gix.3; mouse.
DR CTD; 14751; -.
DR MGI; MGI:95797; Gpi1.
DR VEuPathDB; HostDB:ENSMUSG00000036427; -.
DR eggNOG; KOG2446; Eukaryota.
DR GeneTree; ENSGT00390000000707; -.
DR HOGENOM; CLU_017947_3_0_1; -.
DR InParanoid; P06745; -.
DR OMA; VERCKAM; -.
DR OrthoDB; 446616at2759; -.
DR PhylomeDB; P06745; -.
DR TreeFam; TF300436; -.
DR BRENDA; 5.3.1.9; 3474.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR SABIO-RK; P06745; -.
DR UniPathway; UPA00109; UER00181.
DR BioGRID-ORCS; 14751; 29 hits in 74 CRISPR screens.
DR ChiTaRS; Gpi1; mouse.
DR EvolutionaryTrace; P06745; -.
DR PRO; PR:P06745; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P06745; protein.
DR Bgee; ENSMUSG00000036427; Expressed in ileal epithelium and 282 other tissues.
DR ExpressionAtlas; P06745; baseline and differential.
DR Genevisible; P06745; MM.
DR GO; GO:0060170; C:ciliary membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:MGI.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0061621; P:canonical glycolysis; TAS:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR GO; GO:0034101; P:erythrocyte homeostasis; IMP:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0006096; P:glycolytic process; IDA:MGI.
DR GO; GO:0061620; P:glycolytic process through glucose-6-phosphate; IC:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:MGI.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0043278; P:response to morphine; ISO:MGI.
DR GO; GO:0035994; P:response to muscle stretch; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR CDD; cd05015; SIS_PGI_1; 1.
DR CDD; cd05016; SIS_PGI_2; 1.
DR Gene3D; 1.10.1390.10; -; 1.
DR HAMAP; MF_00473; G6P_isomerase; 1.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR023096; G6P_Isomerase_C.
DR InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035476; SIS_PGI_1.
DR InterPro; IPR035482; SIS_PGI_2.
DR PANTHER; PTHR11469; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 1.
DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytokine; Cytoplasm; Direct protein sequencing;
KW Gluconeogenesis; Glycolysis; Growth factor; Isomerase; Phosphoprotein;
KW Reference proteome; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT CHAIN 2..558
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180538"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:15342241"
FT ACT_SITE 389
FT /evidence="ECO:0000269|PubMed:15342241"
FT ACT_SITE 519
FT /evidence="ECO:0000269|PubMed:15342241"
FT BINDING 159..160
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15342241,
FT ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F,
FT ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT"
FT BINDING 210..215
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15342241,
FT ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F,
FT ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT"
FT BINDING 354
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15342241,
FT ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F,
FT ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT"
FT BINDING 358
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15342241,
FT ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F,
FT ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT"
FT BINDING 389
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15342241,
FT ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F,
FT ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT"
FT BINDING 519
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:15342241,
FT ECO:0000269|PubMed:16375918, ECO:0007744|PDB:1U0F,
FT ECO:0007744|PDB:2CXS, ECO:0007744|PDB:2CXT"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6V0"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 185
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P06744"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P6V0"
FT MOD_RES 454
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 454
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 454
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 95
FT /note="N -> D (in Ref. 1; AAA39825/BAE41301)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="M -> K (in Ref. 2; BAE21866)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="H -> R (in Ref. 2; BAE22329)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="A -> E (in Ref. 6; AAC36515)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..266
FT /note="FEF -> LEL (in Ref. 6; AAC36515)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="A -> V (in Ref. 6; AAC36515)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="M -> T (in Ref. 6; AAC36515)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="E -> G (in Ref. 2; BAE35416)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="M -> V (in Ref. 6; AAC36515)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="D -> N (in Ref. 6; AAC36515)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="W -> L (in Ref. 6; AAC36515)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="F -> L (in Ref. 2; BAE23502)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:2CXN"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:2CXN"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 236..241
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:2CXN"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 290..309
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2CXN"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 420..438
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 442..451
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 474..481
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 484..505
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 516..525
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:2CXN"
FT STRAND 530..533
FT /evidence="ECO:0007829|PDB:2CXN"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:2CXN"
SQ SEQUENCE 558 AA; 62767 MW; 7299E98B12B4C375 CRC64;
MAALTRNPQF QKLLEWHRAN SANLKLRELF EADPERFNNF SLNLNTNHGH ILVDYSKNLV
NKEVMQMLVE LAKSRGVEAA RDNMFSGSKI NYTENRAVLH VALRNRSNTP IKVDGKDVMP
EVNRVLDKMK SFCQRVRSGD WKGYTGKSIT DIINIGIGGS DLGPLMVTEA LKPYSKGGPR
VWFVSNIDGT HIAKTLASLS PETSLFIIAS KTFTTQETIT NAETAKEWFL EAAKDPSAVA
KHFVALSTNT AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA
HWMDQHFLKT PLEKNAPVLL ALLGIWYINC YGCETHALLP YDQYMHRFAA YFQQGDMESN
GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL
HHKILLANFL AQTEALMKGK LPEEARKELQ AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT
KLTPFILGAL IAMYEHKIFV QGIMWDINSF DQWGVELGKQ LAKKIEPELE GSSAVTSHDS
STNGLISFIK QQRDTKLE
