TPM3_HUMAN
ID TPM3_HUMAN Reviewed; 285 AA.
AC P06753; D3DV71; P12324; Q2QD06; Q5VU58; Q5VU63; Q5VU66; Q5VU71; Q5VU72;
AC Q8TCG3; Q969Q2; Q9NQH8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Tropomyosin alpha-3 chain;
DE AltName: Full=Gamma-tropomyosin;
DE AltName: Full=Tropomyosin-3;
DE AltName: Full=Tropomyosin-5;
DE Short=hTM5;
GN Name=TPM3;
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).
RX PubMed=3018581; DOI=10.1038/322648a0;
RA Reinach F.C., McLeod A.R.;
RT "Tissue-specific expression of the human tropomyosin gene involved in the
RT generation of the trk oncogene.";
RL Nature 322:648-650(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3024106; DOI=10.1093/nar/14.21.8413;
RA McLeod A.R., Houlker C., Talbot K.;
RT "The mRNA and RNA-copy pseudogenes encoding TM30nm, a human cytoskeletal
RT tropomyosin.";
RL Nucleic Acids Res. 14:8413-8426(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RX PubMed=3418707; DOI=10.1016/0022-2836(88)90633-x;
RA Clayton L., Reinach F.C., Chumbley G.M., MacLeod A.R.;
RT "Organization of the hTMnm gene. Implications for the evolution of muscle
RT and non-muscle tropomyosins.";
RL J. Mol. Biol. 201:507-515(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RC TISSUE=Colon cancer;
RA Lin J.J.-C., Lin J.L.-C., Geng X., Das K.M.;
RT "Identification and characterization of a novel tropomyosin isoform from a
RT colon cancer cell line T84.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone, Kidney, Skeletal muscle, and Uterus;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-248 (ISOFORM 2), AND IDENTIFICATION
RP OF RCTPM3.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [9]
RP PROTEIN SEQUENCE OF 93-126; 135-150; 154-168 AND 215-245, PARTIAL PROTEIN
RP SEQUENCE (ISOFORMS 2/3), CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 2/3),
RP ACETYLATION AT ALA-2 (ISOFORMS 2/3), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (DEC-2005) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 93-119, PARTIAL PROTEIN SEQUENCE (ISOFORMS 2/3),
RP CLEAVAGE OF INITIATOR METHIONINE (ISOFORMS 2/3), ACETYLATION AT ALA-2
RP (ISOFORMS 2/3), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.;
RL Submitted (JUL-2007) to UniProtKB.
RN [11]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHROMOSOMAL
RP TRANSLOCATION WITH NTRK1.
RX PubMed=2869410; DOI=10.1038/319743a0;
RA Martin-Zanca D., Hughes S.H., Barbacid M.;
RT "A human oncogene formed by the fusion of truncated tropomyosin and protein
RT tyrosine kinase sequences.";
RL Nature 319:743-748(1986).
RN [12]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Keratinocyte;
RX PubMed=1286667; DOI=10.1002/elps.11501301199;
RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
RA Vandekerckhove J.;
RT "Microsequences of 145 proteins recorded in the two-dimensional gel protein
RT database of normal human epidermal keratinocytes.";
RL Electrophoresis 13:960-969(1992).
RN [13]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC TISSUE=Skeletal muscle;
RX PubMed=12574106; DOI=10.1161/01.hyp.0000050646.79785.7c;
RA Dunn S.A., Mohteshamzadeh M., Daly A.K., Thomas T.H.;
RT "Altered tropomyosin expression in essential hypertension.";
RL Hypertension 41:347-354(2003).
RN [14]
RP INTERACTION WITH TMOD1.
RX PubMed=8002995; DOI=10.1006/bbrc.1994.1747;
RA Sung L.A., Lin J.J.-C.;
RT "Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin
RT isoform encoded by the gamma-tropomyosin gene.";
RL Biochem. Biophys. Res. Commun. 201:627-634(1994).
RN [15]
RP IDENTIFICATION OF RCTPM3 BY MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RA Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M., Harbi S.O.,
RA Stansalas J., Mohamed A.O.;
RT "Abnormal proteins in primary breast cancer tissues from 25 Sudanese
RT patients.";
RL Eur. J. Inflamm. 6:115-121(2008).
RN [16]
RP IDENTIFICATION BY 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 (ISOFORMS 2; 3 AND 6),
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215 (ISOFORMS 2 AND 5),
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125 (ISOFORM 7), 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP 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 [20]
RP IDENTIFICATION BY 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 [21]
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 [22]
RP VARIANT NEM1 ARG-9.
RX PubMed=7704029; DOI=10.1038/ng0195-75;
RA Laing N.G., Wilton S.D., Akkari P.A., Dorosz S., Boundy K., Kneebone C.,
RA Blumbergs P., White S., Watkins H., Love D.R., Haan E.;
RT "A mutation in the alpha tropomyosin gene TPM3 associated with autosomal
RT dominant nemaline myopathy.";
RL Nat. Genet. 9:75-79(1995).
RN [23]
RP ERRATUM OF PUBMED:7704029.
RX PubMed=7663526; DOI=10.1038/ng0695-249;
RA Laing N.G., Wilton S.D., Akkari P.A., Dorosz S., Boundy K., Kneebone C.,
RA Blumbergs P., White S., Watkins H., Love D.R., Haan E.;
RL Nat. Genet. 10:249-249(1995).
RN [24]
RP CHARACTERIZATION OF VARIANT NEM1 ARG-9.
RX PubMed=10587521; DOI=10.1172/jci7842;
RA Michele D.E., Albayya F.P., Metzger J.M.;
RT "A nemaline myopathy mutation in alpha-tropomyosin causes defective
RT regulation of striated muscle force production.";
RL J. Clin. Invest. 104:1575-1581(1999).
RN [25]
RP VARIANT NEM1 HIS-168.
RX PubMed=17376686; DOI=10.1016/j.nmd.2007.01.017;
RA Penisson-Besnier I., Monnier N., Toutain A., Dubas F., Laing N.;
RT "A second pedigree with autosomal dominant nemaline myopathy caused by TPM3
RT mutation: a clinical and pathological study.";
RL Neuromuscul. Disord. 17:330-337(2007).
RN [26]
RP VARIANTS CFTD MET-100; CYS-168; GLY-168; GLU-169 AND GLY-245, AND VARIANT
RP CAPM1 HIS-168.
RX PubMed=18300303; DOI=10.1002/ana.21308;
RA Clarke N.F., Kolski H., Dye D.E., Lim E., Smith R.L., Patel R., Fahey M.C.,
RA Bellance R., Romero N.B., Johnson E.S., Labarre-Vila A., Monnier N.,
RA Laing N.G., North K.N.;
RT "Mutations in TPM3 are a common cause of congenital fiber type
RT disproportion.";
RL Ann. Neurol. 63:329-337(2008).
RN [27]
RP VARIANT CAPM1 CYS-168.
RX PubMed=19487656; DOI=10.1212/wnl.0b013e3181a82659;
RA Ohlsson M., Fidzianska A., Tajsharghi H., Oldfors A.;
RT "TPM3 mutation in one of the original cases of cap disease.";
RL Neurology 72:1961-1963(2009).
RN [28]
RP VARIANT CAPM1 HIS-168.
RX PubMed=19553118; DOI=10.1016/j.nmd.2009.06.365;
RA De Paula A.M., Franques J., Fernandez C., Monnier N., Lunardi J.,
RA Pellissier J.F., Figarella-Branger D., Pouget J.;
RT "A TPM3 mutation causing cap myopathy.";
RL Neuromuscul. Disord. 19:685-688(2009).
RN [29]
RP VARIANTS CFTD VAL-4; PRO-91; HIS-168 AND LYS-241.
RX PubMed=19953533; DOI=10.1002/humu.21157;
RA Lawlor M.W., Dechene E.T., Roumm E., Geggel A.S., Moghadaszadeh B.,
RA Beggs A.H.;
RT "Mutations of tropomyosin 3 (TPM3) are common and associated with type 1
RT myofiber hypotrophy in congenital fiber type disproportion.";
RL Hum. Mutat. 31:176-183(2010).
RN [30]
RP VARIANTS CFTD HIS-168 AND ALA-174.
RX PubMed=20951040; DOI=10.1016/j.nmd.2010.07.274;
RA Munot P., Lashley D., Jungbluth H., Feng L., Pitt M., Robb S.A., Palace J.,
RA Jayawant S., Kennet R., Beeson D., Cullup T., Abbs S., Laing N., Sewry C.,
RA Muntoni F.;
RT "Congenital fibre type disproportion associated with mutations in the
RT tropomyosin 3 (TPM3) gene mimicking congenital myasthenia.";
RL Neuromuscul. Disord. 20:796-800(2010).
RN [31]
RP VARIANTS NEM1 PHE-88 AND CYS-168, VARIANTS CAPM1 PHE-88; ALA-151; CYS-168
RP AND ILE-245, VARIANTS CFTD VAL-100; CYS-168 AND HIS-168, AND VARIANTS
RP CYS-91 AND LYS-253.
RX PubMed=24692096; DOI=10.1002/humu.22554;
RA Marttila M., Lehtokari V.L., Marston S., Nyman T.A., Barnerias C.,
RA Beggs A.H., Bertini E., Ceyhan-Birsoy O., Cintas P., Gerard M.,
RA Gilbert-Dussardier B., Hogue J.S., Longman C., Eymard B., Frydman M.,
RA Kang P.B., Klinge L., Kolski H., Lochmueller H., Magy L., Manel V.,
RA Mayer M., Mercuri E., North K.N., Peudenier-Robert S., Pihko H.,
RA Probst F.J., Reisin R., Stewart W., Taratuto A.L., de Visser M.,
RA Wilichowski E., Winer J., Nowak K., Laing N.G., Winder T.L., Monnier N.,
RA Clarke N.F., Pelin K., Groenholm M., Wallgren-Pettersson C.;
RT "Mutation update and genotype-phenotype correlations of novel and
RT previously described mutations in TPM2 and TPM3 causing congenital
RT myopathies.";
RL Hum. Mutat. 35:779-790(2014).
RN [32]
RP VARIANT CAPM1 ILE-149.
RX PubMed=24239060; DOI=10.1016/j.nmd.2013.10.002;
RA Schreckenbach T., Schroeder J.M., Voit T., Abicht A., Neuen-Jacob E.,
RA Roos A., Bulst S., Kuhl C., Schulz J.B., Weis J., Claeys K.G.;
RT "Novel TPM3 mutation in a family with cap myopathy and review of the
RT literature.";
RL Neuromuscul. Disord. 24:117-124(2014).
CC -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC Plays a central role, in association with the troponin complex, in the
CC calcium dependent regulation of vertebrate striated muscle contraction.
CC Smooth muscle contraction is regulated by interaction with caldesmon.
CC In non-muscle cells is implicated in stabilizing cytoskeleton actin
CC filaments. {ECO:0000250|UniProtKB:P09493}.
CC -!- SUBUNIT: Homodimer. Heterodimer of an alpha (TPM1, TPM3 or TPM4) and a
CC beta (TPM2) chain (By similarity). Interacts with TMOD1
CC (PubMed:8002995). {ECO:0000250|UniProtKB:P04692,
CC ECO:0000269|PubMed:8002995}.
CC -!- INTERACTION:
CC P06753; P54253: ATXN1; NbExp=4; IntAct=EBI-355607, EBI-930964;
CC P06753; Q8TAB5: C1orf216; NbExp=4; IntAct=EBI-355607, EBI-747505;
CC P06753; Q969G5: CAVIN3; NbExp=3; IntAct=EBI-355607, EBI-3893101;
CC P06753; Q8TD31-3: CCHCR1; NbExp=13; IntAct=EBI-355607, EBI-10175300;
CC P06753; Q8IZT9: FAM9C; NbExp=8; IntAct=EBI-355607, EBI-2870039;
CC P06753; P02671-2: FGA; NbExp=3; IntAct=EBI-355607, EBI-9640259;
CC P06753; Q03933: HSF2; NbExp=10; IntAct=EBI-355607, EBI-2556750;
CC P06753; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-355607, EBI-12056251;
CC P06753; O14879: IFIT3; NbExp=5; IntAct=EBI-355607, EBI-745127;
CC P06753; Q9BQD3: KXD1; NbExp=11; IntAct=EBI-355607, EBI-739657;
CC P06753; O95447: LCA5L; NbExp=4; IntAct=EBI-355607, EBI-8473670;
CC P06753; Q96LR2: LURAP1; NbExp=4; IntAct=EBI-355607, EBI-741355;
CC P06753; Q9Y6D9: MAD1L1; NbExp=10; IntAct=EBI-355607, EBI-742610;
CC P06753; Q7Z3B4: NUP54; NbExp=6; IntAct=EBI-355607, EBI-741048;
CC P06753; O43482: OIP5; NbExp=12; IntAct=EBI-355607, EBI-536879;
CC P06753; Q6NSJ2-2: PHLDB3; NbExp=3; IntAct=EBI-355607, EBI-11018958;
CC P06753; P62195: PSMC5; NbExp=3; IntAct=EBI-355607, EBI-357745;
CC P06753; O95295: SNAPIN; NbExp=3; IntAct=EBI-355607, EBI-296723;
CC P06753; Q8N0S2: SYCE1; NbExp=7; IntAct=EBI-355607, EBI-6872807;
CC P06753; Q9NYJ8: TAB2; NbExp=3; IntAct=EBI-355607, EBI-358708;
CC P06753; A0A024R4Q5: TFPT; NbExp=6; IntAct=EBI-355607, EBI-11527449;
CC P06753; P0C1Z6: TFPT; NbExp=7; IntAct=EBI-355607, EBI-1245626;
CC P06753; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-355607, EBI-10178002;
CC P06753; Q9NVV9: THAP1; NbExp=6; IntAct=EBI-355607, EBI-741515;
CC P06753; Q9BT49: THAP7; NbExp=3; IntAct=EBI-355607, EBI-741350;
CC P06753; P19237: TNNI1; NbExp=3; IntAct=EBI-355607, EBI-746692;
CC P06753; P13805-3: TNNT1; NbExp=3; IntAct=EBI-355607, EBI-12151635;
CC P06753; P67936: TPM4; NbExp=3; IntAct=EBI-355607, EBI-1642100;
CC P06753; Q9UJT2: TSKS; NbExp=3; IntAct=EBI-355607, EBI-852101;
CC P06753; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-355607, EBI-2799833;
CC P06753-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-10977875, EBI-11954292;
CC P06753-2; P54253: ATXN1; NbExp=3; IntAct=EBI-10977875, EBI-930964;
CC P06753-2; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-10977875, EBI-11282723;
CC P06753-2; Q92876: KLK6; NbExp=3; IntAct=EBI-10977875, EBI-2432309;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Skeletal muscle;
CC IsoId=P06753-1; Sequence=Displayed;
CC Name=2; Synonyms=Cytoskeletal, TM30nm;
CC IsoId=P06753-2; Sequence=VSP_006604, VSP_006605, VSP_006606;
CC Name=3;
CC IsoId=P06753-3; Sequence=VSP_006604, VSP_006605, VSP_006607;
CC Name=4;
CC IsoId=P06753-4; Sequence=VSP_047302, VSP_047303, VSP_047304,
CC VSP_047305, VSP_047306;
CC Name=5;
CC IsoId=P06753-5; Sequence=VSP_047302, VSP_047303, VSP_047304,
CC VSP_006606;
CC Name=6;
CC IsoId=P06753-6; Sequence=VSP_006604, VSP_006605;
CC Name=7;
CC IsoId=P06753-7; Sequence=VSP_054792, VSP_006606;
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2
CC polypeptide chains. The sequence exhibits a prominent seven-residues
CC periodicity.
CC -!- DISEASE: Nemaline myopathy 1 (NEM1) [MIM:609284]: A form of nemaline
CC myopathy with autosomal dominant or recessive inheritance. Nemaline
CC myopathies are disorders characterized by muscle weakness of varying
CC onset and severity, and abnormal thread-like or rod-shaped structures
CC in muscle fibers on histologic examination. Autosomal dominant NEM1 is
CC characterized by a moderate phenotype with onset between birth and
CC early second decade of life. Weakness is diffuse and symmetric with
CC slow progression often with need for a wheelchair in adulthood. The
CC autosomal recessive form has onset at birth with moderate to severe
CC hypotonia and diffuse weakness. In the most severe cases, death can
CC occur before 2 years. Less severe cases have delayed major motor
CC milestones, and these patients may walk, but often need a wheelchair
CC before 10 years. {ECO:0000269|PubMed:10587521,
CC ECO:0000269|PubMed:17376686, ECO:0000269|PubMed:24692096,
CC ECO:0000269|PubMed:7704029}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving TPM3 is found in
CC papillary thyroid carcinomas (PTCs). A rearrangement with NTRK1
CC generates the TRK fusion transcript by fusing the amino end of isoform
CC 2 of TPM3 to the 3'-end of NTRK1. {ECO:0000269|PubMed:2869410}.
CC -!- DISEASE: Myopathy, congenital, with fiber-type disproportion (CFTD)
CC [MIM:255310]: A genetically heterogeneous disorder in which there is
CC relative hypotrophy of type 1 muscle fibers compared to type 2 fibers
CC on skeletal muscle biopsy. However, these findings are not specific and
CC can be found in many different myopathic and neuropathic conditions.
CC {ECO:0000269|PubMed:18300303, ECO:0000269|PubMed:19953533,
CC ECO:0000269|PubMed:20951040, ECO:0000269|PubMed:24692096}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cap myopathy 1 (CAPM1) [MIM:609284]: A rare congenital
CC skeletal muscle disorder characterized by the presence of cap-like
CC structures which are well demarcated and peripherally located under the
CC sarcolemma and show abnormal accumulation of sarcomeric proteins.
CC Clinical features are early onset of hypotonia and slowly progressive
CC muscle weakness. Respiratory problems are common.
CC {ECO:0000269|PubMed:18300303, ECO:0000269|PubMed:19487656,
CC ECO:0000269|PubMed:19553118, ECO:0000269|PubMed:24239060,
CC ECO:0000269|PubMed:24692096}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Peptides 2-27, 41-55, 132-153, 163-169,
CC 216-225 and 237-248 have been identified and sequenced by MS.
CC PubMed:16201836 (ABC40673) sequence corresponds to a TPM3 retrocopy
CC (rcTPM3) on chromosome 16 that is generated by retroposition of
CC reversed transcribed mRNA back to the genome. rcTPM3 functionality is
CC uncertain. It has been detected by MS in primary breast cancer tissues.
CC {ECO:0000269|Ref.10, ECO:0000269|Ref.9, ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Peptides 2-27, 41-55, 132-153 and 163-169
CC have been identified and sequenced by MS. {ECO:0000269|Ref.10,
CC ECO:0000269|Ref.9, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TPM3ID225.html";
CC ---------------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
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DR EMBL; X04201; CAA27798.1; -; mRNA.
DR EMBL; AY004867; AAF87083.1; -; mRNA.
DR EMBL; X04588; CAB37185.1; -; mRNA.
DR EMBL; AL590431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53229.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53230.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53231.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53235.1; -; Genomic_DNA.
DR EMBL; BC000771; AAH00771.1; -; mRNA.
DR EMBL; BC008407; AAH08407.1; -; mRNA.
DR EMBL; BC008425; AAH08425.1; -; mRNA.
DR EMBL; BC015403; AAH15403.1; -; mRNA.
DR EMBL; BC072428; AAH72428.1; -; mRNA.
DR EMBL; DQ120714; ABC40673.1; -; Genomic_DNA.
DR EMBL; X03541; CAA27243.1; ALT_TERM; mRNA.
DR EMBL; AF474157; AAL84570.1; -; mRNA.
DR CCDS; CCDS1060.1; -. [P06753-2]
DR CCDS; CCDS41400.1; -. [P06753-5]
DR CCDS; CCDS41401.1; -. [P06753-4]
DR CCDS; CCDS41402.1; -. [P06753-3]
DR CCDS; CCDS41403.1; -. [P06753-1]
DR CCDS; CCDS60274.1; -. [P06753-7]
DR CCDS; CCDS60275.1; -. [P06753-6]
DR PIR; A25530; A25530.
DR PIR; S06210; A24199.
DR RefSeq; NP_001036816.1; NM_001043351.1. [P06753-5]
DR RefSeq; NP_001036817.1; NM_001043352.1. [P06753-3]
DR RefSeq; NP_001036818.1; NM_001043353.1. [P06753-4]
DR RefSeq; NP_001265118.1; NM_001278189.1. [P06753-6]
DR RefSeq; NP_001265120.1; NM_001278191.1. [P06753-7]
DR RefSeq; NP_689476.2; NM_152263.3. [P06753-1]
DR RefSeq; NP_705935.1; NM_153649.3. [P06753-2]
DR PDB; 6OTN; X-ray; 2.40 A; A/B/C/D=44-117.
DR PDBsum; 6OTN; -.
DR AlphaFoldDB; P06753; -.
DR SMR; P06753; -.
DR BioGRID; 113023; 294.
DR IntAct; P06753; 118.
DR MINT; P06753; -.
DR STRING; 9606.ENSP00000357516; -.
DR ChEMBL; CHEMBL3804747; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; P06753; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P06753; -.
DR MetOSite; P06753; -.
DR PhosphoSitePlus; P06753; -.
DR SwissPalm; P06753; -.
DR BioMuta; TPM3; -.
DR DMDM; 519668659; -.
DR DOSAC-COBS-2DPAGE; P06753; -.
DR SWISS-2DPAGE; P06753; -.
DR EPD; P06753; -.
DR jPOST; P06753; -.
DR MassIVE; P06753; -.
DR MaxQB; P06753; -.
DR PaxDb; P06753; -.
DR PeptideAtlas; P06753; -.
DR PRIDE; P06753; -.
DR ProteomicsDB; 51930; -. [P06753-1]
DR ProteomicsDB; 51931; -. [P06753-2]
DR ProteomicsDB; 51932; -. [P06753-3]
DR ProteomicsDB; 65387; -.
DR ProteomicsDB; 65390; -.
DR ProteomicsDB; 65392; -.
DR ProteomicsDB; 65394; -.
DR Antibodypedia; 1682; 240 antibodies from 33 providers.
DR DNASU; 7170; -.
DR Ensembl; ENST00000302206.9; ENSP00000307712.5; ENSG00000143549.21. [P06753-7]
DR Ensembl; ENST00000323144.12; ENSP00000357518.4; ENSG00000143549.21. [P06753-4]
DR Ensembl; ENST00000328159.9; ENSP00000357520.1; ENSG00000143549.21. [P06753-6]
DR Ensembl; ENST00000330188.13; ENSP00000339035.7; ENSG00000143549.21. [P06753-5]
DR Ensembl; ENST00000341485.10; ENSP00000341653.6; ENSG00000143549.21. [P06753-4]
DR Ensembl; ENST00000368531.6; ENSP00000357517.2; ENSG00000143549.21. [P06753-3]
DR Ensembl; ENST00000368533.8; ENSP00000357521.3; ENSG00000143549.21. [P06753-2]
DR Ensembl; ENST00000651641.1; ENSP00000498577.1; ENSG00000143549.21. [P06753-1]
DR GeneID; 7170; -.
DR KEGG; hsa:7170; -.
DR MANE-Select; ENST00000651641.1; ENSP00000498577.1; NM_152263.4; NP_689476.2.
DR UCSC; uc001fdy.2; human. [P06753-1]
DR CTD; 7170; -.
DR DisGeNET; 7170; -.
DR GeneCards; TPM3; -.
DR HGNC; HGNC:12012; TPM3.
DR HPA; ENSG00000143549; Group enriched (skeletal muscle, tongue).
DR MalaCards; TPM3; -.
DR MIM; 164970; gene.
DR MIM; 191030; gene.
DR MIM; 255310; phenotype.
DR MIM; 609284; phenotype.
DR neXtProt; NX_P06753; -.
DR OpenTargets; ENSG00000143549; -.
DR Orphanet; 171881; Cap myopathy.
DR Orphanet; 171439; Childhood-onset nemaline myopathy.
DR Orphanet; 2020; Congenital fiber-type disproportion myopathy.
DR Orphanet; 476406; Congenital generalized hypercontractile muscle stiffness syndrome.
DR Orphanet; 178342; Inflammatory myofibroblastic tumor.
DR Orphanet; 171433; Intermediate nemaline myopathy.
DR PharmGKB; PA36692; -.
DR VEuPathDB; HostDB:ENSG00000143549; -.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_3_0_1; -.
DR InParanoid; P06753; -.
DR OMA; XKCSELE; -.
DR OrthoDB; 1576041at2759; -.
DR PhylomeDB; P06753; -.
DR TreeFam; TF351519; -.
DR PathwayCommons; P06753; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; P06753; -.
DR SIGNOR; P06753; -.
DR BioGRID-ORCS; 7170; 15 hits in 1074 CRISPR screens.
DR ChiTaRS; TPM3; human.
DR GeneWiki; Tropomyosin_3; -.
DR GenomeRNAi; 7170; -.
DR Pharos; P06753; Tbio.
DR PRO; PR:P06753; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P06753; protein.
DR Bgee; ENSG00000143549; Expressed in hindlimb stylopod muscle and 152 other tissues.
DR ExpressionAtlas; P06753; baseline and differential.
DR Genevisible; P06753; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Chromosomal rearrangement; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Muscle protein;
KW Nemaline myopathy; Phosphoprotein; Proto-oncogene; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P58776"
FT CHAIN 2..285
FT /note="Tropomyosin alpha-3 chain"
FT /id="PRO_0000205632"
FT REGION 16..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..285
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P58776"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58774"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 262
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P58775"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21107"
FT MOD_RES 283
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07951"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21107"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_054792"
FT VAR_SEQ 1..81
FT /note="MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLK
FT GTEDELDKYSEALKDAQEKLELAEKKAAD -> MAGITTIEAVKRKIQVLQQQADDAEE
FT RAERLQREVEGERRAREQ (in isoform 2, isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3024106"
FT /id="VSP_006604"
FT VAR_SEQ 1..2
FT /note="MM -> MAGITTI (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047302"
FT VAR_SEQ 5..21
FT /note="IKKKMQMLKLDKENALD -> VKRKIQVLQQQADDAEE (in isoform 4
FT and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047303"
FT VAR_SEQ 25..81
FT /note="QAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAE
FT KKAAD -> RLQREVEGERRAREQ (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047304"
FT VAR_SEQ 190..212
FT /note="KCSELEEELKNVTNNLKSLEAQA -> RCREMDEQIRLMDQNLKCLSAAE
FT (in isoform 2, isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3024106"
FT /id="VSP_006605"
FT VAR_SEQ 259..285
FT /note="DELYAQKLKYKAISEELDHALNDMTSI -> ERLYSQLERNRLLSNELKLTL
FT HDLCD (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006607"
FT VAR_SEQ 259..260
FT /note="DE -> ER (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047305"
FT VAR_SEQ 260..285
FT /note="ELYAQKLKYKAISEELDHALNDMTSI -> KLKCTKEEHLCTQRMLDQTLLD
FT LNEM (in isoform 2, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:3024106"
FT /id="VSP_006606"
FT VAR_SEQ 263..285
FT /note="AQKLKYKAISEELDHALNDMTSI -> SQLERNRLLSNELKLTLHDLCD
FT (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047306"
FT VARIANT 4
FT /note="A -> V (in CFTD; dbSNP:rs199474711)"
FT /evidence="ECO:0000269|PubMed:19953533"
FT /id="VAR_071499"
FT VARIANT 9
FT /note="M -> R (in NEM1; decrease in the sensitivity of
FT contraction to activating calcium; dbSNP:rs80358247)"
FT /evidence="ECO:0000269|PubMed:10587521,
FT ECO:0000269|PubMed:7704029"
FT /id="VAR_013460"
FT VARIANT 88
FT /note="S -> F (in NEM1 and CAPM1)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071500"
FT VARIANT 91
FT /note="R -> C (probable disease-associated variant found in
FT patients with undefined congenital myopathy;
FT dbSNP:rs1571418855)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071501"
FT VARIANT 91
FT /note="R -> P (in CFTD; dbSNP:rs199474713)"
FT /evidence="ECO:0000269|PubMed:19953533"
FT /id="VAR_071502"
FT VARIANT 100
FT /note="L -> M (in CFTD; dbSNP:rs121964853)"
FT /evidence="ECO:0000269|PubMed:18300303"
FT /id="VAR_070066"
FT VARIANT 100
FT /note="L -> V (in CFTD; dbSNP:rs121964853)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071503"
FT VARIANT 149
FT /note="L -> I (in CAPM1)"
FT /evidence="ECO:0000269|PubMed:24239060"
FT /id="VAR_071504"
FT VARIANT 151
FT /note="E -> A (in CAPM1)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071505"
FT VARIANT 168
FT /note="R -> C (in CFTD, CAPM1 and NEM1; also found in
FT patients with undefined congenital myopathy;
FT dbSNP:rs121964854)"
FT /evidence="ECO:0000269|PubMed:18300303,
FT ECO:0000269|PubMed:19487656, ECO:0000269|PubMed:24692096"
FT /id="VAR_070067"
FT VARIANT 168
FT /note="R -> G (in CFTD; dbSNP:rs121964854)"
FT /evidence="ECO:0000269|PubMed:18300303"
FT /id="VAR_070068"
FT VARIANT 168
FT /note="R -> H (in NEM1, CAPM1 and CFTD; also found in
FT patients with undefined congenital myopathy;
FT dbSNP:rs121964852)"
FT /evidence="ECO:0000269|PubMed:17376686,
FT ECO:0000269|PubMed:18300303, ECO:0000269|PubMed:19553118,
FT ECO:0000269|PubMed:19953533, ECO:0000269|PubMed:20951040,
FT ECO:0000269|PubMed:24692096"
FT /id="VAR_070069"
FT VARIANT 169
FT /note="K -> E (in CFTD; dbSNP:rs199474715)"
FT /evidence="ECO:0000269|PubMed:18300303"
FT /id="VAR_070070"
FT VARIANT 174
FT /note="E -> A (in CFTD; dbSNP:rs199474716)"
FT /evidence="ECO:0000269|PubMed:20951040"
FT /id="VAR_071506"
FT VARIANT 241
FT /note="E -> K (in CFTD; dbSNP:rs199474717)"
FT /evidence="ECO:0000269|PubMed:19953533"
FT /id="VAR_071507"
FT VARIANT 245
FT /note="R -> G (in CFTD; dbSNP:rs199474718)"
FT /evidence="ECO:0000269|PubMed:18300303"
FT /id="VAR_070071"
FT VARIANT 245
FT /note="R -> I (in CAPM1; dbSNP:rs797046047)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071508"
FT VARIANT 253
FT /note="T -> K (probable disease-associated variant found in
FT patients with undefined congenital myopathy;
FT dbSNP:rs1553248515)"
FT /evidence="ECO:0000269|PubMed:24692096"
FT /id="VAR_071509"
FT CONFLICT 150
FT /note="K -> E (in Ref. 13; CAA27243)"
FT /evidence="ECO:0000305"
FT HELIX 44..110
FT /evidence="ECO:0007829|PDB:6OTN"
FT INIT_MET P06753-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P06753-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES P06753-2:177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES P06753-2:215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CONFLICT P06753-2:33
FT /note="R -> Q (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:43
FT /note="E -> K (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:66
FT /note="A -> P (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:85
FT /note="D -> G (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:110
FT /note="I -> L (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:135
FT /note="I -> T (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:150
FT /note="A -> T (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:192
FT /note="L -> F (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:196
FT /note="L -> P (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT CONFLICT P06753-2:202
FT /note="R -> C (in Ref. 8; ABC40673)"
FT /evidence="ECO:0000305"
FT INIT_MET P06753-3:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT MOD_RES P06753-3:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000305"
FT MOD_RES P06753-3:177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES P06753-5:215
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES P06753-6:177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES P06753-7:125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
SQ SEQUENCE 285 AA; 32950 MW; 99EAD24C45460A14 CRC64;
MMEAIKKKMQ MLKLDKENAL DRAEQAEAEQ KQAEERSKQL EDELAAMQKK LKGTEDELDK
YSEALKDAQE KLELAEKKAA DAEAEVASLN RRIQLVEEEL DRAQERLATA LQKLEEAEKA
ADESERGMKV IENRALKDEE KMELQEIQLK EAKHIAEEAD RKYEEVARKL VIIEGDLERT
EERAELAESK CSELEEELKN VTNNLKSLEA QAEKYSQKED KYEEEIKILT DKLKEAETRA
EFAERSVAKL EKTIDDLEDE LYAQKLKYKA ISEELDHALN DMTSI
