ID TPM1_HUMAN Reviewed; 284 AA. AC P09493; B7Z5T7; D9YZV2; D9YZV3; D9YZV8; P09494; P10469; Q6DV89; Q6DV90; AC Q7Z6L8; Q86W64; Q96IK2; Q9UCI1; Q9UCI2; Q9UCY9; Q9Y427; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 2. DT 27-MAR-2024, entry version 236. DE RecName: Full=Tropomyosin alpha-1 chain; DE AltName: Full=Alpha-tropomyosin; DE AltName: Full=Tropomyosin-1; GN Name=TPM1; Synonyms=C15orf13, TMSA; 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 PROTEIN SEQUENCE (ISOFORM 1), AND ACETYLATION AT MET-1. RX PubMed=3548719; DOI=10.1016/0006-291x(87)91486-0; RA Mische S.M., Manjula B.N., Fischetti V.A.; RT "Relation of streptococcal M protein with human and rabbit tropomyosin: the RT complete amino acid sequence of human cardiac alpha tropomyosin, a highly RT conserved contractile protein."; RL Biochem. Biophys. Res. Commun. 142:813-818(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Fibroblast; RX PubMed=3336357; DOI=10.1128/mcb.8.1.160-168.1988; RA Lin C.-S., Leavitt J.; RT "Cloning and characterization of a cDNA encoding transformation-sensitive RT tropomyosin isoform 3 from tumorigenic human fibroblasts."; RL Mol. Cell. Biol. 8:160-168(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). RX PubMed=3336363; DOI=10.1128/mcb.8.1.433-440.1988; RA McLeod A.R., Gooding C.; RT "Human hTM alpha gene: expression in muscle and nonmuscle tissue."; RL Mol. Cell. Biol. 8:433-440(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), AND TISSUE SPECIFICITY. RC TISSUE=Heart; RX PubMed=15249230; DOI=10.1016/j.bbrc.2004.06.084; RA Denz C.R., Narshi A., Zajdel R.W., Dube D.K.; RT "Expression of a novel cardiac-specific tropomyosin isoform in humans."; RL Biochem. Biophys. Res. Commun. 320:1291-1297(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Tongue; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [9] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5). RC TISSUE=Brain, Hippocampus, and Placenta; 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 [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 58-284 (ISOFORM 2). RC TISSUE=Liver; RX PubMed=3138425; DOI=10.1007/bf02100079; RA Colote S., Widada J.S., Ferraz C., Bonhomme F., Marti J., Liautard J.-P.; RT "Evolution of tropomyosin functional domains: differential splicing and RT genomic constraints."; RL J. Mol. Evol. 27:228-235(1988). RN [12] RP PROTEIN SEQUENCE OF 134-149 AND 153-167. RC TISSUE=Colon; RX PubMed=8450225; RA Das K.M., Dasgupta A., Mandal A., Geng X.; RT "Autoimmunity to cytoskeletal protein tropomyosin. A clue to the RT pathogenetic mechanism for ulcerative colitis."; RL J. Immunol. 150:2487-2493(1993). RN [13] RP MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=11840567; RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h; RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., RA Zvelebil M.J.; RT "Cluster analysis of an extensive human breast cancer cell line protein RT expression map database."; RL Proteomics 2:212-223(2002). RN [14] RP PHOSPHORYLATION AT SER-283, AND MUTAGENESIS OF SER-283. RX PubMed=17895359; DOI=10.1242/jcs.003251; RA Houle F., Poirier A., Dumaresq J., Huot J.; RT "DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the RT ERK pathway, which regulates the formation of stress fibers in response to RT oxidative stress."; RL J. Cell Sci. 120:3666-3677(2007). RN [15] RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY. RA Ahamed M.E.; RL Submitted (APR-2007) to UniProtKB. 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-213 (ISOFORMS 10; 3; 4 AND 8), RP AND 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 FUNCTION, CHARACTERIZATION OF VARIANTS CMH3 ASN-175 AND GLY-180, AND RP SUBUNIT. RX PubMed=23170982; DOI=10.1021/bi301323n; RA Janco M., Kalyva A., Scellini B., Piroddi N., Tesi C., Poggesi C., RA Geeves M.A.; RT "alpha-Tropomyosin with a D175N or E180G mutation in only one chain differs RT from tropomyosin with mutations in both chains."; RL Biochemistry 51:9880-9890(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-31 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-51 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 INTERACTION WITH LMOD2. RX PubMed=26873245; DOI=10.1016/j.bbapap.2016.02.009; RA Colpan M., Tolkatchev D., Grover S., Helms G.L., Cort J.R., Moroz N., RA Kostyukova A.S.; RT "Localization of the binding interface between leiomodin-2 and alpha- RT tropomyosin."; RL Biochim. Biophys. Acta 1864:523-530(2016). RN [22] RP VARIANTS CMH3 ASN-175 AND GLY-180. RX PubMed=8205619; DOI=10.1016/0092-8674(94)90054-x; RA Thierfelder L., Watkins H., Macrae C., Lamas R., McKenna W.J., RA Vosberg H.-P., Seidman J.G., Seidman C.E.; RT "Alpha-tropomyosin and cardiac troponin T mutations cause familial RT hypertrophic cardiomyopathy: a disease of the sarcomere."; RL Cell 77:701-712(1994). RN [23] RP VARIANTS CMH3 VAL-63 AND ASN-175. RX PubMed=8523464; DOI=10.1016/0022-2828(95)90026-8; RA Nakajima-Taniguchi C., Matsui H., Nagata S., Kishimoto T., RA Yamauchi-Takihara K.; RT "Novel missense mutation in alpha-tropomyosin gene found in Japanese RT patients with hypertrophic cardiomyopathy."; RL J. Mol. Cell. Cardiol. 27:2053-2058(1995). RN [24] RP VARIANT CMH3 ASN-175. RX PubMed=7898523; DOI=10.1056/nejm199504203321603; RA Watkins H., McKenna W.J., Thierfelder L., Suk H.J., Anan R., O'Donoghue A., RA Spirito P., Matsumori A., Moravec C.S., Seidman J.G., Seidman C.E.; RT "Mutations in the genes for cardiac troponin T and alpha-tropomyosin in RT hypertrophic cardiomyopathy."; RL N. Engl. J. Med. 332:1058-1064(1995). RN [25] RP VARIANT CMH3 ASN-175. RX PubMed=9822100; DOI=10.1016/s0735-1097(98)00448-3; RA Jaeaeskelaeinen P., Soranta M., Miettinen R., Saarinen L., Pihlajamaeki J., RA Silvennoinen K., Tikanoja T., Laakso M., Kuusisto J.; RT "The cardiac beta-myosin heavy chain gene is not the predominant gene for RT hypertrophic cardiomyopathy in the Finnish population."; RL J. Am. Coll. Cardiol. 32:1709-1716(1998). RN [26] RP VARIANTS CMD1Y LYS-40 AND LYS-54. RX PubMed=11273725; DOI=10.1006/jmcc.2000.1339; RA Olson T.M., Kishimoto N.Y., Whitby F.G., Michels V.V.; RT "Mutations that alter the surface charge of alpha-tropomyosin are RT associated with dilated cardiomyopathy."; RL J. Mol. Cell. Cardiol. 33:723-732(2001). RN [27] RP VARIANT CMH3 VAL-180. RX PubMed=12974739; DOI=10.1034/j.1399-0004.2003.00151.x; RA Erdmann J., Daehmlow S., Wischke S., Senyuva M., Werner U., Raible J., RA Tanis N., Dyachenko S., Hummel M., Hetzer R., Regitz-Zagrosek V.; RT "Mutation spectrum in a large cohort of unrelated consecutive patients with RT hypertrophic cardiomyopathy."; RL Clin. Genet. 64:339-349(2003). RN [28] RP VARIANTS LVNC9 LYS-192 AND GLU-248. RX PubMed=21551322; DOI=10.1161/circgenetics.110.959270; RA Probst S., Oechslin E., Schuler P., Greutmann M., Boye P., Knirsch W., RA Berger F., Thierfelder L., Jenni R., Klaassen S.; RT "Sarcomere gene mutations in isolated left ventricular noncompaction RT cardiomyopathy do not predict clinical phenotype."; RL Circ. Cardiovasc. Genet. 4:367-374(2011). CC -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells CC (PubMed:23170982). Plays a central role, in association with the CC troponin complex, in the calcium dependent regulation of vertebrate CC striated muscle contraction (PubMed:23170982). Smooth muscle CC contraction is regulated by interaction with caldesmon. In non-muscle CC cells is implicated in stabilizing cytoskeleton actin filaments. CC -!- SUBUNIT: Homodimer (PubMed:23170982). Heterodimer of an alpha (TPM1, CC TPM3 or TPM4) and a beta (TPM2) chain (By similarity). Interacts with CC HRG (via the HRR domain); the interaction contributes to the CC antiangiogenic properties of the histidine/proline-rich region (HRR) of CC HRG (By similarity). Interacts (via N-terminus) with LMOD2 (via N- CC terminus) and TMOD1 (via N-terminus) (PubMed:26873245). {ECO:0000250, CC ECO:0000250|UniProtKB:P04268, ECO:0000250|UniProtKB:P04692, CC ECO:0000269|PubMed:23170982, ECO:0000269|PubMed:26873245}. CC -!- INTERACTION: CC P09493; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-351158, EBI-747505; CC P09493; Q8TC20: CAGE1; NbExp=3; IntAct=EBI-351158, EBI-10196469; CC P09493; Q08379: GOLGA2; NbExp=3; IntAct=EBI-351158, EBI-618309; CC P09493; Q9BQD3: KXD1; NbExp=4; IntAct=EBI-351158, EBI-739657; CC P09493; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-351158, EBI-742610; CC P09493; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-351158, EBI-6872807; CC P09493; P13805: TNNT1; NbExp=4; IntAct=EBI-351158, EBI-726527; CC P09493-5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10196387, EBI-618309; CC P09493-5; V9HW56: HEL-S-108; NbExp=3; IntAct=EBI-10196387, EBI-10330141; CC P09493-5; Q9BQD3: KXD1; NbExp=3; IntAct=EBI-10196387, EBI-739657; CC P09493-5; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-10196387, EBI-6872807; CC P09493-5; P0C1Z6-2: TFPT; NbExp=3; IntAct=EBI-10196387, EBI-10178002; CC P09493-10; Q9UL45: BLOC1S6; NbExp=5; IntAct=EBI-12123928, EBI-465781; CC P09493-10; Q8TC20-4: CAGE1; NbExp=4; IntAct=EBI-12123928, EBI-11522698; CC P09493-10; Q2M329: CCDC96; NbExp=3; IntAct=EBI-12123928, EBI-12382974; CC P09493-10; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-12123928, EBI-10175300; CC P09493-10; Q8IZT9: FAM9C; NbExp=3; IntAct=EBI-12123928, EBI-2870039; CC P09493-10; P02671-2: FGA; NbExp=3; IntAct=EBI-12123928, EBI-9640259; CC P09493-10; Q08379: GOLGA2; NbExp=3; IntAct=EBI-12123928, EBI-618309; CC P09493-10; O14879: IFIT3; NbExp=4; IntAct=EBI-12123928, EBI-745127; CC P09493-10; Q9BQD3: KXD1; NbExp=7; IntAct=EBI-12123928, EBI-739657; CC P09493-10; Q9Y6D9: MAD1L1; NbExp=6; IntAct=EBI-12123928, EBI-742610; CC P09493-10; P62195: PSMC5; NbExp=3; IntAct=EBI-12123928, EBI-357745; CC P09493-10; Q8N0S2: SYCE1; NbExp=4; IntAct=EBI-12123928, EBI-6872807; CC P09493-10; P0C1Z6: TFPT; NbExp=3; IntAct=EBI-12123928, EBI-1245626; CC P09493-10; P13805-3: TNNT1; NbExp=4; IntAct=EBI-12123928, EBI-12151635; CC P09493-10; O95619: YEATS4; NbExp=3; IntAct=EBI-12123928, EBI-399269; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress CC fibers. {ECO:0000250|UniProtKB:P04692}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=Skeletal muscle, TPM1alpha; CC IsoId=P09493-1; Sequence=Displayed; CC Name=2; Synonyms=Smooth muscle; CC IsoId=P09493-2; Sequence=VSP_006576, VSP_006578, VSP_006579; CC Name=3; Synonyms=Fibroblast, TM3; CC IsoId=P09493-3; Sequence=VSP_006577, VSP_006579; CC Name=4; CC IsoId=P09493-4; Sequence=VSP_006577; CC Name=5; CC IsoId=P09493-5; Sequence=VSP_017498, VSP_017499; CC Name=6; Synonyms=10, TPM1kappa; CC IsoId=P09493-6; Sequence=VSP_036064; CC Name=7; CC IsoId=P09493-7; Sequence=VSP_036064, VSP_006579; CC Name=8; CC IsoId=P09493-8; Sequence=VSP_047297, VSP_047298, VSP_047299, CC VSP_047300, VSP_006579; CC Name=9; CC IsoId=P09493-9; Sequence=VSP_006579; CC Name=10; CC IsoId=P09493-10; Sequence=VSP_047299, VSP_047300, VSP_047301; CC -!- TISSUE SPECIFICITY: Detected in primary breast cancer tissues but CC undetectable in normal breast tissues in Sudanese patients. Isoform 1 CC is expressed in adult and fetal skeletal muscle and cardiac tissues, CC with higher expression levels in the cardiac tissues. Isoform 10 is CC expressed in adult and fetal cardiac tissues, but not in skeletal CC muscle. {ECO:0000269|PubMed:15249230, ECO:0000269|Ref.15}. 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 -!- PTM: Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress CC and this phosphorylation enhances stress fiber formation in endothelial CC cells. {ECO:0000269|PubMed:17895359}. CC -!- MASS SPECTROMETRY: [Isoform 3]: Mass=32875.93; Method=MALDI; Note=The CC measured range is 1-284.; Evidence={ECO:0000269|PubMed:11840567}; CC -!- DISEASE: Cardiomyopathy, familial hypertrophic, 3 (CMH3) [MIM:115196]: CC A hereditary heart disorder characterized by ventricular hypertrophy, CC which is usually asymmetric and often involves the interventricular CC septum. The symptoms include dyspnea, syncope, collapse, palpitations, CC and chest pain. They can be readily provoked by exercise. The disorder CC has inter- and intrafamilial variability ranging from benign to CC malignant forms with high risk of cardiac failure and sudden cardiac CC death. {ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:23170982, CC ECO:0000269|PubMed:7898523, ECO:0000269|PubMed:8205619, CC ECO:0000269|PubMed:8523464, ECO:0000269|PubMed:9822100}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Cardiomyopathy, dilated, 1Y (CMD1Y) [MIM:611878]: A disorder CC characterized by ventricular dilation and impaired systolic function, CC resulting in congestive heart failure and arrhythmia. Patients are at CC risk of premature death. {ECO:0000269|PubMed:11273725}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Left ventricular non-compaction 9 (LVNC9) [MIM:611878]: A form CC of left ventricular non-compaction, a cardiomyopathy due to myocardial CC morphogenesis arrest and characterized by a hypertrophic left CC ventricle, a severely thickened 2-layered myocardium, numerous CC prominent trabeculations, deep intertrabecular recesses, and poor CC systolic function. Clinical manifestations are variable. Some affected CC individuals experience no symptoms at all, others develop heart CC failure. In some cases, left ventricular non-compaction is associated CC with other congenital heart anomalies. LVNC9 is an autosomal dominant CC condition. {ECO:0000269|PubMed:21551322}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the tropomyosin family. {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; M19267; AAA36771.1; -; mRNA. DR EMBL; M19713; AAA61225.1; -; mRNA. DR EMBL; M19714; AAA61226.1; -; mRNA. DR EMBL; M19715; AAA61227.1; -; mRNA. DR EMBL; AY640414; AAT68294.1; -; mRNA. DR EMBL; AY640415; AAT68295.1; -; mRNA. DR EMBL; AK299387; BAH13023.1; -; mRNA. DR EMBL; AL050179; CAB43309.2; -; mRNA. DR EMBL; GU324929; ADL14500.1; -; Genomic_DNA. DR EMBL; GU324930; ADL14501.1; -; Genomic_DNA. DR EMBL; GU324933; ADL14504.1; -; Genomic_DNA. DR EMBL; GU324935; ADL14506.1; -; Genomic_DNA. DR EMBL; AC079328; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471082; EAW77619.1; -; Genomic_DNA. DR EMBL; CH471082; EAW77622.1; -; Genomic_DNA. DR EMBL; CH471082; EAW77623.1; -; Genomic_DNA. DR EMBL; CH471082; EAW77627.1; -; Genomic_DNA. DR EMBL; CH471082; EAW77628.1; -; Genomic_DNA. DR EMBL; BC007433; AAH07433.1; -; mRNA. DR EMBL; BC050473; AAH50473.1; -; mRNA. DR EMBL; BC053545; AAH53545.1; -; mRNA. DR EMBL; X12369; CAA30930.1; -; mRNA. DR CCDS; CCDS10181.1; -. [P09493-10] DR CCDS; CCDS32262.1; -. [P09493-7] DR CCDS; CCDS32263.1; -. [P09493-3] DR CCDS; CCDS32264.1; -. [P09493-5] DR CCDS; CCDS45273.1; -. [P09493-1] DR CCDS; CCDS58368.1; -. [P09493-8] DR CCDS; CCDS58369.1; -. [P09493-9] DR CCDS; CCDS86459.1; -. [P09493-6] DR PIR; A27674; A27674. DR PIR; A27678; A25825. DR PIR; S05585; S05585. DR RefSeq; NP_000357.3; NM_000366.5. [P09493-10] DR RefSeq; NP_001018004.1; NM_001018004.1. [P09493-9] DR RefSeq; NP_001018005.1; NM_001018005.1. [P09493-1] DR RefSeq; NP_001018006.1; NM_001018006.1. [P09493-3] DR RefSeq; NP_001018007.1; NM_001018007.1. [P09493-7] DR RefSeq; NP_001018008.1; NM_001018008.1. [P09493-5] DR RefSeq; NP_001018020.1; NM_001018020.1. [P09493-8] DR RefSeq; NP_001288173.1; NM_001301244.1. [P09493-6] DR RefSeq; NP_001317273.1; NM_001330344.1. DR RefSeq; NP_001317275.1; NM_001330346.1. DR RefSeq; NP_001317280.1; NM_001330351.1. DR PDB; 3MUD; X-ray; 2.20 A; C/D=1-29. DR PDB; 5KHT; X-ray; 1.50 A; A/B/C/D=1-28. DR PDB; 6UT2; NMR; -; B/C=1-14. DR PDB; 6X5Z; EM; 4.24 A; O/P=1-284. DR PDB; 7UTI; EM; 4.80 A; W/b/e/f/g/h/i/j=1-284. DR PDB; 7UTL; EM; 6.60 A; W/Z/a/b/g/h/i/j=1-284. DR PDB; 8EFH; EM; 3.30 A; O/P=1-284. DR PDB; 8EFI; EM; 3.40 A; O/P=1-284. DR PDB; 8ENC; EM; 3.60 A; O/P=1-284. DR PDBsum; 3MUD; -. DR PDBsum; 5KHT; -. DR PDBsum; 6UT2; -. DR PDBsum; 6X5Z; -. DR PDBsum; 7UTI; -. DR PDBsum; 7UTL; -. DR PDBsum; 8EFH; -. DR PDBsum; 8EFI; -. DR PDBsum; 8ENC; -. DR AlphaFoldDB; P09493; -. DR BMRB; P09493; -. DR EMDB; EMD-0728; -. DR EMDB; EMD-0729; -. DR EMDB; EMD-22067; -. DR EMDB; EMD-28082; -. DR EMDB; EMD-28083; -. DR EMDB; EMD-28270; -. DR SMR; P09493; -. DR BioGRID; 113021; 273. DR IntAct; P09493; 105. DR MINT; P09493; -. DR STRING; 9606.ENSP00000351022; -. DR ChEMBL; CHEMBL4295705; -. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyGen; P09493; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P09493; -. DR MetOSite; P09493; -. DR PhosphoSitePlus; P09493; -. DR SwissPalm; P09493; -. DR BioMuta; TPM1; -. DR DMDM; 136092; -. DR CPTAC; CPTAC-1462; -. DR CPTAC; CPTAC-1463; -. DR CPTAC; CPTAC-1464; -. DR EPD; P09493; -. DR jPOST; P09493; -. DR MassIVE; P09493; -. DR MaxQB; P09493; -. DR PaxDb; 9606-ENSP00000351022; -. DR PeptideAtlas; P09493; -. DR ProteomicsDB; 15181; -. DR ProteomicsDB; 15182; -. DR ProteomicsDB; 15183; -. DR ProteomicsDB; 52229; -. [P09493-1] DR ProteomicsDB; 52230; -. [P09493-2] DR ProteomicsDB; 52231; -. [P09493-3] DR ProteomicsDB; 52232; -. [P09493-4] DR ProteomicsDB; 52233; -. [P09493-5] DR ProteomicsDB; 52234; -. [P09493-6] DR ProteomicsDB; 52235; -. [P09493-7] DR Pumba; P09493; -. DR Antibodypedia; 635; 362 antibodies from 39 providers. DR DNASU; 7168; -. DR Ensembl; ENST00000267996.11; ENSP00000267996.7; ENSG00000140416.25. [P09493-7] DR Ensembl; ENST00000288398.10; ENSP00000288398.6; ENSG00000140416.25. [P09493-10] DR Ensembl; ENST00000334895.10; ENSP00000334624.4; ENSG00000140416.25. [P09493-5] DR Ensembl; ENST00000358278.7; ENSP00000351022.3; ENSG00000140416.25. [P09493-3] DR Ensembl; ENST00000403994.9; ENSP00000385107.4; ENSG00000140416.25. [P09493-1] DR Ensembl; ENST00000559397.6; ENSP00000452879.1; ENSG00000140416.25. [P09493-8] DR Ensembl; ENST00000559556.5; ENSP00000453941.1; ENSG00000140416.25. [P09493-9] DR Ensembl; ENST00000561266.6; ENSP00000453955.2; ENSG00000140416.25. [P09493-6] DR GeneID; 7168; -. DR KEGG; hsa:7168; -. DR MANE-Select; ENST00000403994.9; ENSP00000385107.4; NM_001018005.2; NP_001018005.1. DR UCSC; uc002alg.4; human. [P09493-1] DR AGR; HGNC:12010; -. DR CTD; 7168; -. DR DisGeNET; 7168; -. DR GeneCards; TPM1; -. DR GeneReviews; TPM1; -. DR HGNC; HGNC:12010; TPM1. DR HPA; ENSG00000140416; Tissue enhanced (heart muscle, skeletal muscle, tongue). DR MalaCards; TPM1; -. DR MIM; 115196; phenotype. DR MIM; 191010; gene. DR MIM; 611878; phenotype. DR neXtProt; NX_P09493; -. DR OpenTargets; ENSG00000140416; -. DR Orphanet; 154; Familial isolated dilated cardiomyopathy. DR Orphanet; 54260; Left ventricular noncompaction. DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy. DR PharmGKB; PA36690; -. DR VEuPathDB; HostDB:ENSG00000140416; -. DR GeneTree; ENSGT01030000234542; -. DR HOGENOM; CLU_055027_0_0_1; -. DR InParanoid; P09493; -. DR OrthoDB; 5398117at2759; -. DR PhylomeDB; P09493; -. DR TreeFam; TF351519; -. DR PathwayCommons; P09493; -. DR Reactome; R-HSA-390522; Striated Muscle Contraction. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR SignaLink; P09493; -. DR SIGNOR; P09493; -. DR BioGRID-ORCS; 7168; 14 hits in 1165 CRISPR screens. DR ChiTaRS; TPM1; human. DR GeneWiki; TPM1; -. DR GenomeRNAi; 7168; -. DR Pharos; P09493; Tbio. DR PRO; PR:P09493; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P09493; Protein. DR Bgee; ENSG00000140416; Expressed in left ventricle myocardium and 216 other cell types or tissues. DR ExpressionAtlas; P09493; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0005884; C:actin filament; IBA:GO_Central. DR GO; GO:0032059; C:bleb; IMP:BHF-UCL. DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:ProtInc. DR GO; GO:0032587; C:ruffle membrane; IDA:BHF-UCL. DR GO; GO:0030017; C:sarcomere; TAS:BHF-UCL. DR GO; GO:0001725; C:stress fiber; IDA:BHF-UCL. DR GO; GO:0003779; F:actin binding; TAS:BHF-UCL. DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB. DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:BHF-UCL. DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL. DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:BHF-UCL. DR GO; GO:0007010; P:cytoskeleton organization; TAS:BHF-UCL. DR GO; GO:0030049; P:muscle filament sliding; ISS:BHF-UCL. DR GO; GO:0030336; P:negative regulation of cell migration; ISS:BHF-UCL. DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; IMP:BHF-UCL. DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:BHF-UCL. DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:BHF-UCL. DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:BHF-UCL. DR GO; GO:0003065; P:positive regulation of heart rate by epinephrine; ISS:BHF-UCL. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:BHF-UCL. DR GO; GO:0008360; P:regulation of cell shape; IMP:BHF-UCL. DR GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc. DR GO; GO:0006937; P:regulation of muscle contraction; TAS:ProtInc. DR GO; GO:0031529; P:ruffle organization; ISS:BHF-UCL. DR GO; GO:0045214; P:sarcomere organization; IMP:BHF-UCL. DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL. DR GO; GO:0042060; P:wound healing; ISS:BHF-UCL. DR Gene3D; 1.20.5.170; -; 2. DR Gene3D; 1.20.5.340; -; 1. DR InterPro; IPR000533; Tropomyosin. DR PANTHER; PTHR19269; TROPOMYOSIN; 1. DR PANTHER; PTHR19269:SF80; TROPOMYOSIN ALPHA-1 CHAIN; 1. DR Pfam; PF00261; Tropomyosin; 1. DR PRINTS; PR00194; TROPOMYOSIN. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PROSITE; PS00326; TROPOMYOSIN; 1. DR UCD-2DPAGE; P09493; -. DR Genevisible; P09493; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; KW Cardiomyopathy; Coiled coil; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Disease variant; Muscle protein; Phosphoprotein; KW Reference proteome. FT CHAIN 1..284 FT /note="Tropomyosin alpha-1 chain" FT /id="PRO_0000205620" FT REGION 1..38 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 116..136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1..284 FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:3548719" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P04692" FT MOD_RES 174 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 186 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58771" FT MOD_RES 206 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58771" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58771" FT MOD_RES 261 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P04692" FT MOD_RES 271 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P58771" FT MOD_RES 283 FT /note="Phosphoserine; by DAPK1" FT /evidence="ECO:0000269|PubMed:17895359" FT VAR_SEQ 1..80 FT /note="MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKG FT TEDELDKYSEALKDAQEKLELAEKKATD -> MCRLRIFLRTASSEHLHERKLRET FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:3138425" FT /id="VSP_006576" FT VAR_SEQ 1..80 FT /note="MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKG FT TEDELDKYSEALKDAQEKLELAEKKATD -> MAGSSSLEAVRRKIRSLQEQADAAEER FT AGTLQRELDHERKLRET (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017498" FT VAR_SEQ 41..80 FT /note="DELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD -> EDIAAKEK FT LLRVSEDERDRVLEELHKAEDSLLAAEEAAAK (in isoform 6 and isoform FT 7)" FT /evidence="ECO:0000303|PubMed:15249230, FT ECO:0000303|PubMed:17974005" FT /id="VSP_036064" FT VAR_SEQ 41..53 FT /note="DELVSLQKKLKGT -> EDIAAKEKLLRVS (in isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_047297" FT VAR_SEQ 57..80 FT /note="LDKYSEALKDAQEKLELAEKKATD -> RDRVLEELHKAEDSLLAAEEAAAK FT (in isoform 8)" FT /evidence="ECO:0000305" FT /id="VSP_047298" FT VAR_SEQ 189..212 FT /note="KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMDSDLESINAAED FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:3138425" FT /id="VSP_006578" FT VAR_SEQ 189..212 FT /note="KCAELEEELKTVTNNLKSLEAQAE -> QVRQLEEQLRIMDQTLKALMAAED FT (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:3336357, ECO:0000303|PubMed:3336363" FT /id="VSP_006577" FT VAR_SEQ 189..192 FT /note="KCAE -> QVRQ (in isoform 8 and isoform 10)" FT /evidence="ECO:0000305" FT /id="VSP_047299" FT VAR_SEQ 196..212 FT /note="ELKTVTNNLKSLEAQAE -> QLRIMDQTLKALMAAED (in isoform 8 FT and isoform 10)" FT /evidence="ECO:0000305" FT /id="VSP_047300" FT VAR_SEQ 258..284 FT /note="DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEENLSMHQMLDQTL FT LELNNM (in isoform 2, isoform 3, isoform 7, isoform 8 and FT isoform 9)" FT /evidence="ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:3138425, ECO:0000303|PubMed:3336357, FT ECO:0000303|PubMed:3336363" FT /id="VSP_006579" FT VAR_SEQ 259..284 FT /note="ELYAQKLKYKAISEELDHALNDMTSI -> QLYQQLEQNRRLTNELKLALNE FT D (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_017499" FT VAR_SEQ 284 FT /note="I -> M (in isoform 10)" FT /evidence="ECO:0000305" FT /id="VSP_047301" FT VARIANT 40 FT /note="E -> K (in CMD1Y; dbSNP:rs104894501)" FT /evidence="ECO:0000269|PubMed:11273725" FT /id="VAR_043986" FT VARIANT 54 FT /note="E -> K (in CMD1Y; dbSNP:rs104894505)" FT /evidence="ECO:0000269|PubMed:11273725" FT /id="VAR_043987" FT VARIANT 63 FT /note="A -> V (in CMH3; dbSNP:rs199476306)" FT /evidence="ECO:0000269|PubMed:8523464" FT /id="VAR_013135" FT VARIANT 175 FT /note="D -> N (in CMH3; no change in homodimerization; no FT change in homodimer thermal stability; decreased actin FT binding; recessive effect in the homodimer; increased FT calcium-dependent regulation of myosin binding to actin FT filaments; dominant effect in the homodimer; FT dbSNP:rs104894503)" FT /evidence="ECO:0000269|PubMed:23170982, FT ECO:0000269|PubMed:7898523, ECO:0000269|PubMed:8205619, FT ECO:0000269|PubMed:8523464, ECO:0000269|PubMed:9822100" FT /id="VAR_007601" FT VARIANT 180 FT /note="E -> G (in CMH3; no change in homodimerization; FT decreased in hom odimer thermal stability; decreased in FT actin binding; increased calcium-dependent regulation of FT myosin binding to actin filaments; dominant effect in the FT homodimer; dbSNP:rs104894502)" FT /evidence="ECO:0000269|PubMed:23170982, FT ECO:0000269|PubMed:8205619" FT /id="VAR_007602" FT VARIANT 180 FT /note="E -> V (in CMH3; dbSNP:rs104894502)" FT /evidence="ECO:0000269|PubMed:12974739" FT /id="VAR_029452" FT VARIANT 192 FT /note="E -> K (in LVNC9; dbSNP:rs199476315)" FT /evidence="ECO:0000269|PubMed:21551322" FT /id="VAR_070121" FT VARIANT 248 FT /note="K -> E (in LVNC9; dbSNP:rs199476319)" FT /evidence="ECO:0000269|PubMed:21551322" FT /id="VAR_070122" FT MUTAGEN 15 FT /note="K->N: Impairs interaction with LMOD2 and TMOD1." FT /evidence="ECO:0000269|PubMed:26873245" FT MUTAGEN 283 FT /note="S->A: Loss of phosphorylation and decreased FT formation of actin stress fibers." FT /evidence="ECO:0000269|PubMed:17895359" FT MUTAGEN 283 FT /note="S->E: Increased formation of actin stress fibers." FT /evidence="ECO:0000269|PubMed:17895359" FT CONFLICT 109 FT /note="A -> V (in Ref. 11; CAA30930)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="N -> D (in Ref. 4; AAT68294/AAT68295)" FT /evidence="ECO:0000305" FT HELIX 1..28 FT /evidence="ECO:0007829|PDB:5KHT" FT HELIX 46..209 FT /evidence="ECO:0007829|PDB:8EFH" FT MOD_RES P09493-2:31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES P09493-3:213 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES P09493-4:213 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES P09493-5:51 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES P09493-8:213 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES P09493-10:213 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" SQ SEQUENCE 284 AA; 32709 MW; F57139E2B0972F4D CRC64; MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDR YEEEIKVLSD KLKEAETRAE FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI //