ID   TPIS_MOUSE              Reviewed;         249 AA.
AC   P17751; Q3TJH2; Q3UC04; Q3UKG9; Q64513; Q9CVF9; Q9CWE7;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 5.
DT   24-JAN-2024, entry version 199.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1 {ECO:0000255|PROSITE-ProRule:PRU10127};
DE   AltName: Full=Methylglyoxal synthase {ECO:0000250|UniProtKB:P00939};
DE            EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939};
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=Tpi1; Synonyms=Tpi;
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 [GENOMIC DNA].
RX   PubMed=9445485;
RA   Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J.,
RA   Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.;
RT   "Comparative sequence analysis of a gene-rich cluster at human chromosome
RT   12p13 and its syntenic region in mouse chromosome 6.";
RL   Genome Res. 8:29-40(1998).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Placenta, and Stomach;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2377473; DOI=10.1093/nar/18.14.4261;
RA   Cheng J., Mielnicki L.M., Pruitt S.C., Maquat L.E.;
RT   "Nucleotide sequence of murine triosephosphate isomerase cDNA.";
RL   Nucleic Acids Res. 18:4261-4261(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [6]
RP   PROTEIN SEQUENCE OF 6-14; 71-103; 60-131; 193-206; 161-188; 195-206 AND
RP   220-248, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-249, AND MUTAGENESIS OF LEU-163 AND
RP   LEU-193.
RX   PubMed=7739600; DOI=10.1016/0027-5107(95)00004-3;
RA   Zingg B.C., Pretsch W., Mohrenweiser H.W.;
RT   "Molecular analysis of four ENU induced triosephosphate isomerase null
RT   mutants in Mus musculus.";
RL   Mutat. Res. 328:163-173(1995).
RN   [8]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-68 AND TYR-209, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA   Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA   Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT   disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; THR-173 AND SER-212, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156 AND LYS-194, SUCCINYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-149; LYS-156 AND LYS-194, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [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).
CC   -!- FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic
CC       enzyme that catalyzes the interconversion between dihydroxyacetone
CC       phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis
CC       and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.
CC   -!- FUNCTION: It is also responsible for the non-negligible production of
CC       methylglyoxal a reactive cytotoxic side-product that modifies and can
CC       alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate;
CC         Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57642; EC=4.2.3.3;
CC         Evidence={ECO:0000250|UniProtKB:P00939};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate;
CC         Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC         EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-
CC       ProRule:PRU10127}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=P17751-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P17751-2; Sequence=VSP_060724;
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AC002397; AAC36016.1; -; Genomic_DNA.
DR   EMBL; AC142254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK008373; BAB25634.1; -; mRNA.
DR   EMBL; AK010808; BAB27194.1; -; mRNA.
DR   EMBL; AK146013; BAE26832.1; -; mRNA.
DR   EMBL; AK149768; BAE29073.1; -; mRNA.
DR   EMBL; AK150735; BAE29810.1; -; mRNA.
DR   EMBL; AK159741; BAE35334.1; -; mRNA.
DR   EMBL; AK167437; BAE39523.1; -; mRNA.
DR   EMBL; AK168446; BAE40350.1; -; mRNA.
DR   EMBL; AK168756; BAE40594.1; -; mRNA.
DR   EMBL; X53333; CAA37420.1; -; mRNA.
DR   EMBL; BC046761; AAH46761.1; -; mRNA.
DR   EMBL; L31777; AAB48543.1; -; Genomic_DNA.
DR   CCDS; CCDS20530.2; -. [P17751-1]
DR   PIR; S10490; ISMST.
DR   RefSeq; NP_033441.2; NM_009415.2. [P17751-1]
DR   AlphaFoldDB; P17751; -.
DR   SMR; P17751; -.
DR   BioGRID; 204290; 55.
DR   IntAct; P17751; 11.
DR   MINT; P17751; -.
DR   STRING; 10090.ENSMUSP00000130858; -.
DR   GlyGen; P17751; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P17751; -.
DR   PhosphoSitePlus; P17751; -.
DR   SwissPalm; P17751; -.
DR   REPRODUCTION-2DPAGE; IPI00467833; -.
DR   REPRODUCTION-2DPAGE; P17751; -.
DR   CPTAC; non-CPTAC-3752; -.
DR   EPD; P17751; -.
DR   jPOST; P17751; -.
DR   MaxQB; P17751; -.
DR   PaxDb; 10090-ENSMUSP00000130858; -.
DR   PeptideAtlas; P17751; -.
DR   ProteomicsDB; 259059; -. [P17751-1]
DR   Pumba; P17751; -.
DR   Antibodypedia; 22744; 525 antibodies from 37 providers.
DR   DNASU; 21991; -.
DR   Ensembl; ENSMUST00000172132.10; ENSMUSP00000130858.4; ENSMUSG00000023456.17. [P17751-1]
DR   Ensembl; ENSMUST00000239432.2; ENSMUSP00000159368.2; ENSMUSG00000023456.17. [P17751-2]
DR   GeneID; 21991; -.
DR   KEGG; mmu:21991; -.
DR   UCSC; uc012esp.1; mouse. [P17751-1]
DR   AGR; MGI:98797; -.
DR   CTD; 7167; -.
DR   MGI; MGI:98797; Tpi1.
DR   VEuPathDB; HostDB:ENSMUSG00000023456; -.
DR   eggNOG; KOG1643; Eukaryota.
DR   GeneTree; ENSGT00390000013354; -.
DR   HOGENOM; CLU_024251_2_0_1; -.
DR   InParanoid; P17751; -.
DR   OMA; GSVNPHN; -.
DR   OrthoDB; 167479at2759; -.
DR   PhylomeDB; P17751; -.
DR   TreeFam; TF300829; -.
DR   Reactome; R-MMU-70171; Glycolysis.
DR   Reactome; R-MMU-70263; Gluconeogenesis.
DR   SABIO-RK; P17751; -.
DR   UniPathway; UPA00109; UER00189.
DR   UniPathway; UPA00138; -.
DR   BioGRID-ORCS; 21991; 28 hits in 78 CRISPR screens.
DR   ChiTaRS; Tpi1; mouse.
DR   PRO; PR:P17751; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P17751; Protein.
DR   Bgee; ENSMUSG00000023456; Expressed in epithelium of small intestine and 280 other cell types or tissues.
DR   ExpressionAtlas; P17751; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0016853; F:isomerase activity; IDA:MGI.
DR   GO; GO:0008929; F:methylglyoxal synthase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0061621; P:canonical glycolysis; IGI:MGI.
DR   GO; GO:0006094; P:gluconeogenesis; IDA:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
DR   GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR   GO; GO:0019242; P:methylglyoxal biosynthetic process; ISS:UniProtKB.
DR   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00147_B; TIM_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
DR   InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR   NCBIfam; TIGR00419; tim; 1.
DR   PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR21139:SF2; TRIOSEPHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
DR   COMPLUYEAST-2DPAGE; P17751; -.
DR   SWISS-2DPAGE; P17751; -.
DR   UCD-2DPAGE; P17751; -.
DR   Genevisible; P17751; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Cytoplasm; Direct protein sequencing;
KW   Gluconeogenesis; Glycolysis; Isomerase; Isopeptide bond; Lyase;
KW   Methylation; Nitration; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   CHAIN           2..249
FT                   /note="Triosephosphate isomerase"
FT                   /id="PRO_0000090116"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         12
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   BINDING         14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         68
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16800626"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48500"
FT   MOD_RES         149
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         156
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         156
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         173
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         194
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         194
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         194
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         209
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0007744|PubMed:16800626"
FT   MOD_RES         212
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         214
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   MOD_RES         238
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   CROSSLNK        142
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:P60174"
FT   VAR_SEQ         1
FT                   /note="M -> MEGKAEQQGAGLTMAEGGEKEEFCFTAIYISGQWREPCVCTDLQRLE
FT                   PGTM (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060724"
FT   MUTAGEN         163
FT                   /note="L->Q: 50% reduced activity."
FT                   /evidence="ECO:0000269|PubMed:7739600"
FT   MUTAGEN         193
FT                   /note="L->Q: 50% reduced activity."
FT                   /evidence="ECO:0000269|PubMed:7739600"
FT   CONFLICT        74
FT                   /note="A -> P (in Ref. 4; CAA37420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        107
FT                   /note="D -> G (in Ref. 3; BAE39523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="K -> R (in Ref. 3; BAB27194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="S -> P (in Ref. 3; BAE26832)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="A -> G (in Ref. 3; BAB27194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="A -> Q (in Ref. 3; BAB27194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223..225
FT                   /note="SQP -> TPA (in Ref. 4; CAA37420)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="V -> M (in Ref. 3; BAB25634)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  26713 MW;  4C69846D0C8AF33A CRC64;
     MAPTRKFFVG GNWKMNGRKK CLGELICTLN AANVPAGTEV VCAPPTAYID FARQKLDPKI
     AVAAQNCYKV TNGAFTGEIS PGMIKDLGAT WVVLGHSERR HVFGESDELI GQKVSHALAE
     GLGVIACIGE KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ
     QAQEVHEKLR GWLKSNVNDG VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE
     FVDIINAKQ
//