G6PI_HUMAN
ID G6PI_HUMAN Reviewed; 558 AA.
AC P06744; B4DG39; Q9BRD3; Q9BSK5; Q9UHE6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Glucose-6-phosphate isomerase {ECO:0000303|PubMed:2387591};
DE Short=GPI {ECO:0000303|PubMed:2387591};
DE EC=5.3.1.9 {ECO:0000269|PubMed:28803808};
DE AltName: Full=Autocrine motility factor {ECO:0000303|PubMed:11004567};
DE Short=AMF {ECO:0000303|PubMed:11004567};
DE AltName: Full=Neuroleukin {ECO:0000303|PubMed:3352745};
DE Short=NLK {ECO:0000303|PubMed:3352745};
DE AltName: Full=Phosphoglucose isomerase {ECO:0000303|PubMed:12163179};
DE Short=PGI {ECO:0000303|PubMed:12163179};
DE AltName: Full=Phosphohexose isomerase {ECO:0000303|PubMed:11004567};
DE Short=PHI {ECO:0000303|PubMed:11004567};
DE AltName: Full=Sperm antigen 36 {ECO:0000303|PubMed:10727272};
DE Short=SA-36 {ECO:0000303|PubMed:10727272};
GN Name=GPI {ECO:0000303|PubMed:2387591, ECO:0000312|HGNC:HGNC:4458};
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).
RA Gurney M.E.;
RL Submitted (MAR-1987) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=10727272; DOI=10.1095/biolreprod62.4.1016;
RA Yakirevich E., Naot Y.;
RT "Cloning of a glucose phosphate isomerase/neuroleukin-like sperm antigen
RT involved in sperm agglutination.";
RL Biol. Reprod. 62:1016-1023(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-208.
RG NIEHS SNPs program;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Amygdala;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RX PubMed=2387591; DOI=10.1016/0888-7543(90)90212-d;
RA Walker J.I.H., Faik P., Morgan M.J.;
RT "Characterization of the 5' end of the gene for human glucose phosphate
RT isomerase (GPI).";
RL Genomics 7:638-643(1990).
RN [8]
RP PROTEIN SEQUENCE OF 2-12; 58-73; 97-104; 181-226; 424-438 AND 455-461,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [9]
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 [10]
RP FUNCTION, AND PHOSPHORYLATION AT SER-185.
RX PubMed=11004567; DOI=10.1016/s0167-4838(00)00075-3;
RA Haga A., Niinaka Y., Raz A.;
RT "Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation
RT factor is a multifunctional phosphoprotein.";
RL Biochim. Biophys. Acta 1480:235-244(2000).
RN [11]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11437381; DOI=10.1006/bbrc.2001.5135;
RA Funasaka T., Haga A., Raz A., Nagase H.;
RT "Tumor autocrine motility factor is an angiogenic factor that stimulates
RT endothelial cell motility.";
RL Biochem. Biophys. Res. Commun. 285:118-128(2001).
RN [12]
RP SPECIES SPECIFICITY OF THE CYTOKINE FUNCTION.
RX PubMed=12163179; DOI=10.1016/s0014-5793(02)03072-7;
RA Amraei M., Nabi I.R.;
RT "Species specificity of the cytokine function of phosphoglucose
RT isomerase.";
RL FEBS Lett. 525:151-155(2002).
RN [13]
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 [14]
RP PHOSPHORYLATION AT SER-185, AND MUTAGENESIS OF SER-185.
RX PubMed=15637053; DOI=10.1074/jbc.m409457200;
RA Yanagawa T., Funasaka T., Tsutsumi S., Raz T., Tanaka N., Raz A.;
RT "Differential regulation of phosphoglucose isomerase/autocrine motility
RT factor activities by protein kinase CK2 phosphorylation.";
RL J. Biol. Chem. 280:10419-10426(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12 AND LYS-142, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP MALONYLATION AT LYS-454.
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; THR-109 AND SER-455, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP HYDROXYBUTYRYLATION AT LYS-34.
RX PubMed=29775581; DOI=10.1016/j.molcel.2018.04.011;
RA Huang H., Tang S., Ji M., Tang Z., Shimada M., Liu X., Qi S.,
RA Locasale J.W., Roeder R.G., Zhao Y., Li X.;
RT "p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis.";
RL Mol. Cell 70:663-678(2018).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=11371164; DOI=10.1006/jmbi.2001.4680;
RA Read J., Pearce J., Li X., Muirhead H., Chirgwin J., Davies C.;
RT "The crystal structure of human phosphoglucose isomerase at 1.6 A
RT resolution: implications for catalytic mechanism, cytokine activity and
RT haemolytic anaemia.";
RL J. Mol. Biol. 309:447-463(2001).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) ALONE AND IN COMPLEX WITH INHIBITOR.
RX PubMed=12054796; DOI=10.1016/s0022-2836(02)00186-9;
RA Tanaka N., Haga A., Uemura H., Akiyama H., Funasaka T., Nagase H., Raz A.,
RA Nakamura K.T.;
RT "Inhibition mechanism of cytokine activity of human autocrine motility
RT factor examined by crystal structure analyses and site-directed mutagenesis
RT studies.";
RL J. Mol. Biol. 318:985-997(2002).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP ACTIVE SITE.
RX PubMed=12777791; DOI=10.1107/s0907444903007352;
RA Davies C., Muirhead H., Chirgwin J.;
RT "The structure of human phosphoglucose isomerase complexed with a
RT transition-state analogue.";
RL Acta Crystallogr. D 59:1111-1113(2003).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=12573240; DOI=10.1016/s1570-9639(02)00464-8;
RA Cordeiro A.T., Godoi P.H., Silva C.H., Garratt R.C., Oliva G.,
RA Thiemann O.H.;
RT "Crystal structure of human phosphoglucose isomerase and analysis of the
RT initial catalytic steps.";
RL Biochim. Biophys. Acta 1645:117-122(2003).
RN [29]
RP VARIANTS HA-GPID SER-159; HIS-347 AND THR-525.
RX PubMed=8499925; DOI=10.1093/hmg/2.3.327;
RA Walker J.I.H., Layton D.M., Bellingham A.J., Morgan M.J., Faik P.;
RT "DNA sequence abnormalities in human glucose 6-phosphate isomerase
RT deficiency.";
RL Hum. Mol. Genet. 2:327-329(1993).
RN [30]
RP VARIANTS HA-GPID TRP-83; MET-224; HIS-273; LEU-278; CYS-347; PHE-487 AND
RP LYS-495.
RX PubMed=7989588; DOI=10.1172/jci117597;
RA Xu W., Beutler E.;
RT "The characterization of gene mutations for human glucose phosphate
RT isomerase deficiency associated with chronic hemolytic anemia.";
RL J. Clin. Invest. 94:2326-2329(1994).
RN [31]
RP VARIANTS HA-GPID MET-101; ILE-195; ARG-343 AND THR-525.
RX PubMed=8822952;
RA Baronciani L., Zanella A., Bianchi P., Zappa M., Alfinito F., Iolascon A.,
RA Tannoia N., Beutler E., Sirchia G.;
RT "Study of the molecular defects in glucose phosphate isomerase-deficient
RT patients affected by chronic hemolytic anemia.";
RL Blood 88:2306-2310(1996).
RN [32]
RP VARIANTS HA-GPID ILE-5; MET-224; ARG-343; ARG-375 AND ASN-539.
RX PubMed=8822954;
RA Kanno H., Fujii H., Hirono A., Ishida Y., Ohga S., Fukumoto Y.,
RA Matsuzawa K., Ogawa S., Miwa S.;
RT "Molecular analysis of glucose phosphate isomerase deficiency associated
RT with hereditary hemolytic anemia.";
RL Blood 88:2321-2325(1996).
RN [33]
RP VARIANTS HA-GPID GLY-75; PRO-300; CYS-347 AND HIS-472.
RX PubMed=9446754; DOI=10.1006/bcmd.1997.0157;
RA Beutler E., West C., Britton H.A., Harris J., Forman L.;
RT "Glucosephosphate isomerase (GPI) deficiency mutations associated with
RT hereditary nonspherocytic hemolytic anemia (HNSHA).";
RL Blood Cells Mol. Dis. 23:402-409(1997).
RN [34]
RP VARIANTS HA-GPID PRO-20; PRO-339; ARG-389 AND VAL-517.
RX PubMed=9856489; DOI=10.1007/s004390050849;
RA Kugler W., Breme K., Laspe P., Muirhead H., Davies C., Winkler H.,
RA Schroter W., Lakomek M.;
RT "Molecular basis of neurological dysfunction coupled with haemolytic
RT anaemia in human glucose-6-phosphate isomerase (GPI) deficiency.";
RL Hum. Genet. 103:450-454(1998).
RN [35]
RP VARIANTS HA-GPID PRO-160 AND CYS-472, FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=28803808; DOI=10.1016/j.bcmd.2017.04.003;
RA Mojzikova R., Koralkova P., Holub D., Saxova Z., Pospisilova D.,
RA Prochazkova D., Dzubak P., Horvathova M., Divoky V.;
RT "Two novel mutations (p.(Ser160Pro) and p.(Arg472Cys)) causing glucose-6-
RT phosphate isomerase deficiency are associated with erythroid dysplasia and
RT inappropriately suppressed hepcidin.";
RL Blood Cells Mol. Dis. 69:23-29(2018).
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:28803808). Besides
CC it's role as a glycolytic enzyme, also acts as a secreted cytokine:
CC acts as an angiogenic factor (AMF) that stimulates endothelial cell
CC motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin,
CC for spinal and sensory neurons (PubMed:3352745, PubMed:11004567). It is
CC secreted by lectin-stimulated T-cells and induces immunoglobulin
CC secretion (PubMed:3352745, PubMed:11004567).
CC {ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:11437381,
CC ECO:0000269|PubMed:28803808, ECO:0000269|PubMed:3352745}.
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:28803808};
CC -!- ACTIVITY REGULATION: Strongly inhibited by erythrose 4-phosphate.
CC {ECO:0000269|PubMed:12054796}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000269|PubMed:28803808}.
CC -!- SUBUNIT: Homodimer; in the catalytically active form (PubMed:11371164,
CC PubMed:12054796, PubMed:12777791). Monomer in the secreted form
CC (PubMed:11371164, PubMed:12054796, PubMed:12777791).
CC {ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12054796,
CC ECO:0000269|PubMed:12777791}.
CC -!- INTERACTION:
CC P06744; Q96BW9: TAMM41; NbExp=3; IntAct=EBI-2558394, EBI-13943422;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11437381}. Secreted
CC {ECO:0000269|PubMed:11437381}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P06744-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06744-2; Sequence=VSP_043475, VSP_043476;
CC -!- PTM: Phosphorylation at Ser-185 by CK2 has been shown to decrease
CC enzymatic activity and may contribute to secretion by a non-classical
CC secretory pathway. {ECO:0000269|PubMed:11004567,
CC ECO:0000269|PubMed:15637053}.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
CC -!- DISEASE: Hemolytic anemia, non-spherocytic, due to glucose phosphate
CC isomerase deficiency (HA-GPID) [MIM:613470]: A form of anemia in which
CC there is no abnormal hemoglobin or spherocytosis. It is caused by
CC glucose phosphate isomerase deficiency. {ECO:0000269|PubMed:28803808,
CC ECO:0000269|PubMed:7989588, ECO:0000269|PubMed:8499925,
CC ECO:0000269|PubMed:8822952, ECO:0000269|PubMed:8822954,
CC ECO:0000269|PubMed:9446754, ECO:0000269|PubMed:9856489}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Phosphoglucose isomerase entry;
CC URL="https://en.wikipedia.org/wiki/Phosphoglucose_isomerase";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gpi/";
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DR EMBL; K03515; AAA36368.1; -; mRNA.
DR EMBL; AF187554; AAF22645.1; -; mRNA.
DR EMBL; AY324386; AAP72966.1; -; Genomic_DNA.
DR EMBL; AK294396; BAG57650.1; -; mRNA.
DR EMBL; AC010504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004982; AAH04982.1; -; mRNA.
DR EMBL; AH002710; AAA52593.1; -; Genomic_DNA.
DR CCDS; CCDS12437.1; -. [P06744-1]
DR CCDS; CCDS54246.1; -. [P06744-2]
DR PIR; A35333; A35333.
DR RefSeq; NP_000166.2; NM_000175.4. [P06744-1]
DR RefSeq; NP_001171651.1; NM_001184722.1. [P06744-2]
DR RefSeq; NP_001316838.1; NM_001329909.1. [P06744-1]
DR RefSeq; NP_001316839.1; NM_001329910.1. [P06744-1]
DR RefSeq; NP_001316840.1; NM_001329911.1.
DR PDB; 1IAT; X-ray; 1.62 A; A=2-558.
DR PDB; 1IRI; X-ray; 2.40 A; A/B/C/D=1-558.
DR PDB; 1JIQ; X-ray; 1.90 A; A/B/C/D=1-558.
DR PDB; 1JLH; X-ray; 2.10 A; A/B/C/D=1-558.
DR PDB; 1NUH; X-ray; 2.51 A; A=1-558.
DR PDB; 6XUH; X-ray; 2.38 A; A/B/C/D=2-557.
DR PDB; 6XUI; X-ray; 1.95 A; A/B/C/D=2-557.
DR PDBsum; 1IAT; -.
DR PDBsum; 1IRI; -.
DR PDBsum; 1JIQ; -.
DR PDBsum; 1JLH; -.
DR PDBsum; 1NUH; -.
DR PDBsum; 6XUH; -.
DR PDBsum; 6XUI; -.
DR AlphaFoldDB; P06744; -.
DR SMR; P06744; -.
DR BioGRID; 109082; 151.
DR IntAct; P06744; 24.
DR MINT; P06744; -.
DR STRING; 9606.ENSP00000405573; -.
DR ChEMBL; CHEMBL4295702; -.
DR DrugBank; DB02093; 5-phospho-D-arabinohydroxamic acid.
DR DrugBank; DB03042; 5-Phosphoarabinonic Acid.
DR DrugBank; DB02076; 6-phospho-D-gluconic acid.
DR DrugBank; DB02007; alpha-D-glucose 6-phosphate.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB03937; D-erythrose 4-phosphate.
DR DrugBank; DB02548; D-glucitol 6-phosphate.
DR DrugBank; DB04493; Fructose-6-phosphate.
DR DrugBank; DB03581; Glucose-6-Phosphate.
DR MoonDB; P06744; Curated.
DR GlyConnect; 1268; 1 N-Linked glycan (1 site).
DR GlyGen; P06744; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P06744; -.
DR MetOSite; P06744; -.
DR PhosphoSitePlus; P06744; -.
DR SwissPalm; P06744; -.
DR BioMuta; GPI; -.
DR DMDM; 17380385; -.
DR EPD; P06744; -.
DR jPOST; P06744; -.
DR MassIVE; P06744; -.
DR MaxQB; P06744; -.
DR PeptideAtlas; P06744; -.
DR PRIDE; P06744; -.
DR ProteomicsDB; 51924; -. [P06744-1]
DR ProteomicsDB; 51925; -. [P06744-2]
DR TopDownProteomics; P06744-1; -. [P06744-1]
DR TopDownProteomics; P06744-2; -. [P06744-2]
DR Antibodypedia; 15715; 721 antibodies from 42 providers.
DR CPTC; P06744; 3 antibodies.
DR DNASU; 2821; -.
DR Ensembl; ENST00000356487.11; ENSP00000348877.3; ENSG00000105220.17. [P06744-1]
DR Ensembl; ENST00000588991.7; ENSP00000465858.3; ENSG00000105220.17. [P06744-2]
DR GeneID; 2821; -.
DR KEGG; hsa:2821; -.
DR MANE-Select; ENST00000356487.11; ENSP00000348877.3; NM_000175.5; NP_000166.2.
DR UCSC; uc002nvg.3; human. [P06744-1]
DR CTD; 2821; -.
DR DisGeNET; 2821; -.
DR GeneCards; GPI; -.
DR HGNC; HGNC:4458; GPI.
DR HPA; ENSG00000105220; Low tissue specificity.
DR MalaCards; GPI; -.
DR MIM; 172400; gene.
DR MIM; 613470; phenotype.
DR neXtProt; NX_P06744; -.
DR OpenTargets; ENSG00000105220; -.
DR Orphanet; 712; Hemolytic anemia due to glucophosphate isomerase deficiency.
DR PharmGKB; PA28841; -.
DR VEuPathDB; HostDB:ENSG00000105220; -.
DR eggNOG; KOG2446; Eukaryota.
DR GeneTree; ENSGT00390000000707; -.
DR HOGENOM; CLU_017947_3_0_1; -.
DR InParanoid; P06744; -.
DR OMA; IGVWYIN; -.
DR OrthoDB; 446616at2759; -.
DR PhylomeDB; P06744; -.
DR TreeFam; TF300436; -.
DR BioCyc; MetaCyc:HS02693-MON; -.
DR BRENDA; 5.3.1.9; 2681.
DR PathwayCommons; P06744; -.
DR Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; P06744; -.
DR SignaLink; P06744; -.
DR SIGNOR; P06744; -.
DR UniPathway; UPA00109; UER00181.
DR BioGRID-ORCS; 2821; 242 hits in 1095 CRISPR screens.
DR ChiTaRS; GPI; human.
DR EvolutionaryTrace; P06744; -.
DR GeneWiki; Glucose-6-phosphate_isomerase; -.
DR GenomeRNAi; 2821; -.
DR Pharos; P06744; Tbio.
DR PRO; PR:P06744; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P06744; protein.
DR Bgee; ENSG00000105220; Expressed in apex of heart and 199 other tissues.
DR ExpressionAtlas; P06744; baseline and differential.
DR Genevisible; P06744; HS.
DR GO; GO:0060170; C:ciliary membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
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:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR GO; GO:0034101; P:erythrocyte homeostasis; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0007599; P:hemostasis; TAS:ProtInc.
DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:CAFA.
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; IEA:Ensembl.
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; Alternative splicing; Cytokine; Cytoplasm;
KW Direct protein sequencing; Disease variant; Gluconeogenesis; Glycolysis;
KW Growth factor; Hereditary hemolytic anemia; Hydroxylation; Isomerase;
KW Phosphoprotein; Reference proteome; Secreted; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT CHAIN 2..558
FT /note="Glucose-6-phosphate isomerase"
FT /id="PRO_0000180537"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:11371164,
FT ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791"
FT ACT_SITE 389
FT /evidence="ECO:0000269|PubMed:11371164,
FT ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791"
FT ACT_SITE 519
FT /evidence="ECO:0000269|PubMed:11371164,
FT ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791"
FT BINDING 159..160
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 210..215
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 354
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 358
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 389
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT BINDING 519
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 34
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 185
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:11004567,
FT ECO:0000269|PubMed:15637053"
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:0000250|UniProtKB:P06745"
FT MOD_RES 454
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 454
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P06745"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MVALCSLQHLGSSDPRALPTLPTATSGQRPAKRRRKSPAM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043475"
FT VAR_SEQ 135..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043476"
FT VARIANT 5
FT /note="T -> I (in HA-GPID; GPI Matsumoto;
FT dbSNP:rs267606852)"
FT /evidence="ECO:0000269|PubMed:8822954"
FT /id="VAR_002516"
FT VARIANT 20
FT /note="H -> P (in HA-GPID; severe form with neurological
FT deficits; GPI Homburg; dbSNP:rs137853586)"
FT /evidence="ECO:0000269|PubMed:9856489"
FT /id="VAR_002517"
FT VARIANT 75
FT /note="R -> G (in HA-GPID; GPI Elyria; dbSNP:rs1246980119)"
FT /evidence="ECO:0000269|PubMed:9446754"
FT /id="VAR_002518"
FT VARIANT 83
FT /note="R -> W (in HA-GPID; dbSNP:rs983725326)"
FT /evidence="ECO:0000269|PubMed:7989588"
FT /id="VAR_002519"
FT VARIANT 101
FT /note="V -> M (in HA-GPID; GPI Sarcina; dbSNP:rs757341382)"
FT /evidence="ECO:0000269|PubMed:8822952"
FT /id="VAR_002521"
FT VARIANT 159
FT /note="G -> S (in HA-GPID; dbSNP:rs137853582)"
FT /evidence="ECO:0000269|PubMed:8499925"
FT /id="VAR_002520"
FT VARIANT 160
FT /note="S -> P (in HA-GPID; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28803808"
FT /id="VAR_082092"
FT VARIANT 195
FT /note="T -> I (in HA-GPID; GPI Bari and Mola;
FT dbSNP:rs1426869331)"
FT /evidence="ECO:0000269|PubMed:8822952"
FT /id="VAR_002522"
FT VARIANT 208
FT /note="I -> T (in dbSNP:rs8191371)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018816"
FT VARIANT 224
FT /note="T -> M (in HA-GPID; GPI Iwate; dbSNP:rs61754634)"
FT /evidence="ECO:0000269|PubMed:7989588,
FT ECO:0000269|PubMed:8822954"
FT /id="VAR_002523"
FT VARIANT 273
FT /note="R -> H (in HA-GPID; dbSNP:rs1250029517)"
FT /evidence="ECO:0000269|PubMed:7989588"
FT /id="VAR_002524"
FT VARIANT 278
FT /note="S -> L (in HA-GPID; dbSNP:rs34306618)"
FT /evidence="ECO:0000269|PubMed:7989588"
FT /id="VAR_002525"
FT VARIANT 300
FT /note="A -> P (in HA-GPID; dbSNP:rs1435398228)"
FT /evidence="ECO:0000269|PubMed:9446754"
FT /id="VAR_002526"
FT VARIANT 308
FT /note="R -> H (in dbSNP:rs2230294)"
FT /id="VAR_033943"
FT VARIANT 339
FT /note="L -> P (in HA-GPID; severe form with neurological
FT deficits; GPI Homburg; dbSNP:rs137853587)"
FT /evidence="ECO:0000269|PubMed:9856489"
FT /id="VAR_002527"
FT VARIANT 343
FT /note="Q -> R (in HA-GPID; GPI Narita and Morcone;
FT dbSNP:rs267606851)"
FT /evidence="ECO:0000269|PubMed:8822952,
FT ECO:0000269|PubMed:8822954"
FT /id="VAR_002528"
FT VARIANT 347
FT /note="R -> C (in HA-GPID; GPI Mount Scopus;
FT dbSNP:rs758132799)"
FT /evidence="ECO:0000269|PubMed:7989588,
FT ECO:0000269|PubMed:9446754"
FT /id="VAR_002529"
FT VARIANT 347
FT /note="R -> H (in HA-GPID; dbSNP:rs137853583)"
FT /evidence="ECO:0000269|PubMed:8499925"
FT /id="VAR_002530"
FT VARIANT 375
FT /note="T -> R (in HA-GPID; GPI Kinki; dbSNP:rs267606853)"
FT /evidence="ECO:0000269|PubMed:8822954"
FT /id="VAR_002531"
FT VARIANT 389
FT /note="H -> R (in HA-GPID; severe form; GPI Calden;
FT dbSNP:rs139382538)"
FT /evidence="ECO:0000269|PubMed:9856489"
FT /id="VAR_002532"
FT VARIANT 472
FT /note="R -> C (in HA-GPID; Strongly reduced glucose-6-
FT phosphate isomerase activity; dbSNP:rs1364382189)"
FT /evidence="ECO:0000269|PubMed:28803808"
FT /id="VAR_082093"
FT VARIANT 472
FT /note="R -> H (in HA-GPID; dbSNP:rs148811525)"
FT /evidence="ECO:0000269|PubMed:9446754"
FT /id="VAR_002533"
FT VARIANT 487
FT /note="L -> F (in HA-GPID; dbSNP:rs374583873)"
FT /evidence="ECO:0000269|PubMed:7989588"
FT /id="VAR_002534"
FT VARIANT 495
FT /note="E -> K (in HA-GPID; dbSNP:rs900848255)"
FT /evidence="ECO:0000269|PubMed:7989588"
FT /id="VAR_002535"
FT VARIANT 517
FT /note="L -> V (in HA-GPID; severe form; GPI Calden)"
FT /evidence="ECO:0000269|PubMed:9856489"
FT /id="VAR_002536"
FT VARIANT 525
FT /note="I -> T (in HA-GPID; dbSNP:rs137853584)"
FT /evidence="ECO:0000269|PubMed:8499925,
FT ECO:0000269|PubMed:8822952"
FT /id="VAR_002537"
FT VARIANT 539
FT /note="D -> N (in HA-GPID; GPI Fukuoka and Kinki;
FT dbSNP:rs137853585)"
FT /evidence="ECO:0000269|PubMed:8822954"
FT /id="VAR_002538"
FT MUTAGEN 185
FT /note="S->A: Retained full enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15637053"
FT MUTAGEN 185
FT /note="S->E: Decreased enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15637053"
FT CONFLICT 158
FT /note="G -> V (in Ref. 1; AAA36368)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="L -> V (in Ref. 2; AAF22645)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="L -> V (in Ref. 2; AAF22645)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 62..74
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:1IAT"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 119..137
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 216..233
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 250..256
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1IAT"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 290..309
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 335..341
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:6XUH"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1JLH"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 420..438
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 442..451
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 456..462
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 474..481
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 484..505
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 516..528
FT /evidence="ECO:0007829|PDB:1IAT"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:1IAT"
FT HELIX 540..552
FT /evidence="ECO:0007829|PDB:1IAT"
SQ SEQUENCE 558 AA; 63147 MW; 7C8E95277BDC79A6 CRC64;
MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV
TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP
EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR
VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA
KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA
HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN
GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL
HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT
KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA
STNGLINFIK QQREARVQ
