(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 176.
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;
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;
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=aldehydo-D-glucose 6-phosphate = keto-D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57579, ChEBI:CHEBI:57584;
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       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};
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   SMR; P06745; -.
DR   BioGrid; 200021; 6.
DR   IntAct; P06745; 7.
DR   MINT; P06745; -.
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   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   eggNOG; KOG2446; Eukaryota.
DR   eggNOG; COG0166; LUCA.
DR   GeneTree; ENSGT00390000000707; -.
DR   InParanoid; P06745; -.
DR   KO; K01810; -.
DR   OMA; TNSQHAF; -.
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   ChiTaRS; Gpi1; mouse.
DR   EvolutionaryTrace; P06745; -.
DR   PRO; PR:P06745; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P06745; protein.
DR   Bgee; ENSMUSG00000036427; Expressed in 338 organ(s), highest expression level in CA1 field of hippocampus.
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; ISO: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: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:0016866; F:intramolecular transferase activity; ISO:MGI.
DR   GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0046185; P:aldehyde catabolic process; 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; IBA:GO_Central.
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:0019242; P:methylglyoxal biosynthetic process; ISO: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:0051024; P:positive regulation of immunoglobulin secretion; 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; 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   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;
DR   PRODOM; Q9JM07.
DR   SWISS-2DPAGE; Q9JM07.
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   REGION          159..160
FT                   /note="Glucose-6-phosphate binding"
FT                   /evidence="ECO:0000244|PDB:1U0F, ECO:0000244|PDB:2CXS,
FT                   ECO:0000244|PDB:2CXT, ECO:0000269|PubMed:15342241,
FT                   ECO:0000269|PubMed:16375918"
FT   REGION          210..215
FT                   /note="Glucose-6-phosphate binding"
FT                   /evidence="ECO:0000244|PDB:1U0F, ECO:0000244|PDB:2CXS,
FT                   ECO:0000244|PDB:2CXT, ECO:0000269|PubMed:15342241,
FT                   ECO:0000269|PubMed:16375918"
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         354
FT                   /note="Glucose-6-phosphate"
FT                   /evidence="ECO:0000244|PDB:1U0F, ECO:0000244|PDB:2CXS,
FT                   ECO:0000244|PDB:2CXT, ECO:0000269|PubMed:15342241,
FT                   ECO:0000269|PubMed:16375918"
FT   BINDING         358
FT                   /note="Glucose-6-phosphate"
FT                   /evidence="ECO:0000244|PDB:1U0F, ECO:0000244|PDB:2CXS,
FT                   ECO:0000244|PDB:2CXT, ECO:0000269|PubMed:15342241,
FT                   ECO:0000269|PubMed:16375918"
FT   BINDING         389
FT                   /note="Glucose-6-phosphate"
FT                   /evidence="ECO:0000244|PDB:1U0F, ECO:0000244|PDB:2CXS,
FT                   ECO:0000244|PDB:2CXT, ECO:0000269|PubMed:15342241,
FT                   ECO:0000269|PubMed:16375918"
FT   BINDING         519
FT                   /note="Glucose-6-phosphate"
FT                   /evidence="ECO:0000244|PDB:1U0F, ECO:0000244|PDB:2CXS,
FT                   ECO:0000244|PDB:2CXT, ECO:0000269|PubMed:15342241,
FT                   ECO:0000269|PubMed:16375918"
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:0000244|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:0000244|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:0000244|PubMed:23806337"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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:0000244|PDB:2CXN"
FT   HELIX           8..20
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           21..23
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           26..32
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           36..39
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          41..45
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          50..54
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           62..74
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           77..85
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   TURN            92..95
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           100..103
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          116..118
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           119..137
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          151..155
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           158..160
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           162..170
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           172..175
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          180..184
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           189..196
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   TURN            201..203
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          204..209
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          211..213
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           216..233
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           236..241
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          243..248
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           250..256
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           260..262
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          263..265
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           272..274
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   TURN            276..278
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           279..281
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           282..288
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           290..309
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           312..314
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           316..329
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          335..341
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           343..345
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           348..360
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          378..380
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   TURN            384..387
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           388..397
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          404..411
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           417..419
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           420..438
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           442..451
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           456..462
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           463..466
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          474..481
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           484..505
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           513..515
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           516..525
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           526..529
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   STRAND          530..533
FT                   /evidence="ECO:0000244|PDB:2CXN"
FT   HELIX           540..552
FT                   /evidence="ECO:0000244|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
//

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