TPIS_MOUSE
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 03-AUG-2022, entry version 191.
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, 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 [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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 50.
DR IntAct; P17751; 11.
DR MINT; P17751; -.
DR STRING; 10090.ENSMUSP00000130858; -.
DR iPTMnet; P17751; -.
DR PhosphoSitePlus; P17751; -.
DR SwissPalm; P17751; -.
DR COMPLUYEAST-2DPAGE; P17751; -.
DR REPRODUCTION-2DPAGE; IPI00467833; -.
DR REPRODUCTION-2DPAGE; P17751; -.
DR SWISS-2DPAGE; P17751; -.
DR UCD-2DPAGE; P17751; -.
DR CPTAC; non-CPTAC-3752; -.
DR EPD; P17751; -.
DR jPOST; P17751; -.
DR MaxQB; P17751; -.
DR PaxDb; P17751; -.
DR PeptideAtlas; P17751; -.
DR PRIDE; P17751; -.
DR ProteomicsDB; 259059; -. [P17751-1]
DR Antibodypedia; 22744; 479 antibodies from 37 providers.
DR DNASU; 21991; -.
DR Ensembl; ENSMUST00000172132; ENSMUSP00000130858; ENSMUSG00000023456. [P17751-1]
DR Ensembl; ENSMUST00000239432; ENSMUSP00000159368; ENSMUSG00000023456. [P17751-2]
DR GeneID; 21991; -.
DR KEGG; mmu:21991; -.
DR UCSC; uc012esp.1; mouse. [P17751-1]
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; HTEVICA; -.
DR OrthoDB; 1272577at2759; -.
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 74 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 277 other tissues.
DR ExpressionAtlas; P17751; baseline and differential.
DR Genevisible; P17751; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO: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:0005975; P:carbohydrate metabolic process; ISO: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; -; 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 PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
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
