TNNT2_HUMAN
ID TNNT2_HUMAN Reviewed; 298 AA.
AC P45379; A2TDB9; A8K3K6; O60214; Q99596; Q99597; Q9BUF6; Q9UM96;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Troponin T, cardiac muscle;
DE Short=TnTc;
DE AltName: Full=Cardiac muscle troponin T;
DE Short=cTnT;
GN Name=TNNT2;
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 6).
RC TISSUE=Heart;
RX PubMed=8344420; DOI=10.1016/0014-5793(93)80981-y;
RA Mesnard L., Samson F., Espinasse I., Durand J., Neveux J.-Y.,
RA Mercadier J.-J.;
RT "Molecular cloning and developmental expression of human cardiac troponin
RT T.";
RL FEBS Lett. 328:139-144(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 12).
RC TISSUE=Heart muscle;
RX PubMed=8088824; DOI=10.1006/geno.1994.1271;
RA Townsend P.J., Farza H., Macgeoch C., Spurr N.K., Wade R., Gahlman R.,
RA Yacoub M.H., Barton P.J.R.;
RT "Human cardiac troponin T: identification of fetal isoforms and assignment
RT of the TNNT2 locus to chromosome 1q.";
RL Genomics 21:311-316(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Fetal heart;
RX PubMed=8576938; DOI=10.1016/s0022-2828(95)91587-7;
RA Townsend P.J., Barton P.J.R., Yacoub M.H., Farza H.;
RT "Molecular cloning of human cardiac troponin T isoforms: expression in
RT developing and failing heart.";
RL J. Mol. Cell. Cardiol. 27:2223-2236(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 7 AND 8).
RC TISSUE=Heart;
RX PubMed=7534662; DOI=10.1161/01.res.76.4.681;
RA Anderson P.A., Greig A., Mark T.M., Malouf N.N., Oakeley A.E.,
RA Ungerleider R.M., Allen P.D., Kay B.K.;
RT "Molecular basis of human cardiac troponin T isoforms expressed in the
RT developing, adult, and failing heart.";
RL Circ. Res. 76:681-686(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 10).
RC TISSUE=Fetal heart;
RX PubMed=7895342; DOI=10.1161/01.res.76.4.687;
RA Mesnard L., Logeart D., Taviaux S., Diriong S., Mercadier J.-J., Samson F.;
RT "Human cardiac troponin T: cloning and expression of new isoforms in the
RT normal and failing heart.";
RL Circ. Res. 76:687-692(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 6), AND VARIANT CMH2 ILE-120.
RC TISSUE=Heart muscle;
RX PubMed=9482583;
RX DOI=10.1002/(sici)1098-1004(1998)11:2<179::aid-humu12>3.0.co;2-w;
RA Gerull B., Osterziel K.-J., Witt C., Dietz R., Thierfelder L.;
RT "A rapid protocol for cardiac troponin T gene mutation detection in
RT familial hypertrophic cardiomyopathy.";
RL Hum. Mutat. 11:179-182(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 6).
RA D'Cruz L.G., Oberoi J., Mughal F., Steffensen U., Steffensen M., Kubo T.,
RA Mogensen J., McKoy G., O'Donnoghue A., Pondel M., McKenna W.J.,
RA Carter N.D., Baboonian C.;
RT "Genomic organization of the human cardiac troponin T gene (TNNT2) and
RT characterization of the candidate promoter region.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Heart;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11).
RC TISSUE=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 [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-229 AND 231-288, ALTERNATIVE
RP SPLICING, AND VARIANT ARG-263.
RC TISSUE=Blood;
RX PubMed=9689598; DOI=10.1006/jmcc.1998.0698;
RA Farza H., Townsend P.J., Carrier L., Barton P.J., Mesnard L., Bahrend E.,
RA Forissier J.F., Fiszman M., Yacoub M.H., Schwartz K.;
RT "Genomic organisation, alternative splicing and polymorphisms of the human
RT cardiac troponin T gene.";
RL J. Mol. Cell. Cardiol. 30:1247-1253(1998).
RN [13]
RP PROTEIN SEQUENCE OF 70-76 AND 177-182.
RC TISSUE=Heart;
RX PubMed=7498159; DOI=10.1002/elps.11501601192;
RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
RA Ershova E.S., Egorov T.A., Musalyamov A.K.;
RT "The major protein expression profile and two-dimensional protein database
RT of human heart.";
RL Electrophoresis 16:1160-1169(1995).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 193-298.
RX PubMed=12840750; DOI=10.1038/nature01780;
RA Takeda S., Yamashita A., Maeda K., Maeda Y.;
RT "Structure of the core domain of human cardiac troponin in the Ca(2+)-
RT saturated form.";
RL Nature 424:35-41(2003).
RN [15]
RP VARIANTS CMH2 ASN-89 AND GLN-102.
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 [16]
RP VARIANTS CMH2 ILE-120; LYS-173; ASP-254 AND CYS-288.
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 [17]
RP VARIANT CMH2 LEU-102.
RX PubMed=8989109; DOI=10.1161/01.cir.94.12.3069;
RA Forissier J.F., Carrier L., Farza H., Bonne G., Bercovici J., Richard P.,
RA Hainque B., Townsend P.J., Yacoub M.H., Faure S., Dubourg O., Millaire A.,
RA Hagege A.A., Desnos M., Komajda M., Schwartz K.;
RT "Codon 102 of the cardiac troponin T gene is a putative hot spot for
RT mutations in familial hypertrophic cardiomyopathy.";
RL Circulation 94:3069-3073(1996).
RN [18]
RP VARIANT CMH2 TRP-102.
RX PubMed=9060892; DOI=10.1016/s0735-1097(96)00530-x;
RA Moolman J.C., Corfield V.A., Posen B., Ngumbela K., Seidman C., Brink P.A.,
RA Watkins H.;
RT "Sudden death due to troponin T mutations.";
RL J. Am. Coll. Cardiol. 29:549-555(1997).
RN [19]
RP VARIANT CMH2 PRO-288.
RA Erdmann J., Wischke S., Kallisch H., Riedel K., Heidenreich M., Fleck E.,
RA Regitz-Zagrosek V.;
RT "A novel missense Arg 278 Pro mutation in the troponin T gene (TNNT2).";
RL Hum. Mutat. 12:364-364(1998).
RN [20]
RP VARIANT CMH2 LEU-104.
RX PubMed=10525521; DOI=10.1136/hrt.82.5.621;
RA Varnava A., Baboonian C., Davison F., de Cruz L., Elliott P.M.,
RA Davies M.J., McKenna W.J.;
RT "A new mutation of the cardiac troponin T gene causing familial
RT hypertrophic cardiomyopathy without left ventricular hypertrophy.";
RL Heart 82:621-624(1999).
RN [21]
RP VARIANT CMH2 VAL-114.
RX PubMed=9140840; DOI=10.1006/jmcc.1996.0322;
RA Nakajima-Taniguchi C., Matsui H., Fujio Y., Nagata S., Kishimoto T.,
RA Yamauchi-Takihara K.;
RT "Novel missense mutation in cardiac troponin T gene found in Japanese
RT patient with hypertrophic cardiomyopathy.";
RL J. Mol. Cell. Cardiol. 29:839-843(1997).
RN [22]
RP VARIANT CMH2 PHE-189.
RX PubMed=11034944; DOI=10.1161/01.cir.102.16.1950;
RA Ho C.Y., Lever H.M., DeSanctis R., Farver C.F., Seidman J.G., Seidman C.E.;
RT "Homozygous mutation in cardiac troponin T: implications for hypertrophic
RT cardiomyopathy.";
RL Circulation 102:1950-1955(2000).
RN [23]
RP VARIANT CMD1D LYS-210 DEL.
RX PubMed=11106718; DOI=10.1056/nejm200012073432304;
RA Kamisago M., Sharma S.D., DePalma S.R., Solomon S., Sharma P.,
RA McDonough B., Smoot L., Mullen M.P., Woolf P.K., Wigle E.D., Seidman J.G.,
RA Seidman C.E.;
RT "Mutations in sarcomere protein genes as a cause of dilated
RT cardiomyopathy.";
RL N. Engl. J. Med. 343:1688-1696(2000).
RN [24]
RP VARIANT CMD1D TRP-151.
RX PubMed=11684629; DOI=10.1161/hc4301.098285;
RA Li D., Czernuszewicz G.Z., Gonzalez O., Tapscott T., Karibe A.,
RA Durand J.B., Brugada R., Hill R., Gregoritch J.M., Anderson J.L.,
RA Quinones M., Bachinski L.L., Roberts R.;
RT "Novel cardiac troponin T mutation as a cause of familial dilated
RT cardiomyopathy.";
RL Circulation 104:2188-2193(2001).
RN [25]
RP VARIANTS CMH2 LEU-80; VAL-120; ILE-281 AND CYS-296.
RX PubMed=12707239; DOI=10.1161/01.cir.0000066323.15244.54;
RA Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C.,
RA Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A.,
RA Desnos M., Schwartz K., Hainque B., Komajda M.;
RT "Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of
RT mutations, and implications for a molecular diagnosis strategy.";
RL Circulation 107:2227-2232(2003).
RN [26]
RP ERRATUM OF PUBMED:12707239.
RA Richard P., Charron P., Carrier L., Ledeuil C., Cheav T., Pichereau C.,
RA Benaiche A., Isnard R., Dubourg O., Burban M., Gueffet J.-P., Millaire A.,
RA Desnos M., Schwartz K., Hainque B., Komajda M.;
RL Circulation 109:3258-3258(2004).
RN [27]
RP VARIANT CMH2 PRO-288.
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 CMD1D TRP-141; LEU-215 AND LYS-220 DEL.
RX PubMed=15542288; DOI=10.1016/j.jacc.2004.08.027;
RA Mogensen J., Murphy R.T., Shaw T., Bahl A., Redwood C., Watkins H.,
RA Burke M., Elliott P.M., McKenna W.J.;
RT "Severe disease expression of cardiac troponin C and T mutations in
RT patients with idiopathic dilated cardiomyopathy.";
RL J. Am. Coll. Cardiol. 44:2033-2040(2004).
RN [29]
RP VARIANT CMH2 CYS-140.
RX PubMed=15563892; DOI=10.1016/j.cccn.2004.09.016;
RA Song L., Zou Y., Wang J., Wang Z., Zhen Y., Lou K., Zhang Q., Wang X.,
RA Wang H., Li J., Hui R.;
RT "Mutations profile in Chinese patients with hypertrophic cardiomyopathy.";
RL Clin. Chim. Acta 351:209-216(2005).
RN [30]
RP VARIANT CMD1D TRP-151.
RX PubMed=15769782; DOI=10.1093/eurheartj/ehi193;
RA Villard E., Duboscq-Bidot L., Charron P., Benaiche A., Conraads V.,
RA Sylvius N., Komajda M.;
RT "Mutation screening in dilated cardiomyopathy: prominent role of the beta
RT myosin heavy chain gene.";
RL Eur. Heart J. 26:794-803(2005).
RN [31]
RP VARIANT CMH2 CYS-288.
RX PubMed=16199542; DOI=10.1136/jmg.2005.033886;
RA Ingles J., Doolan A., Chiu C., Seidman J., Seidman C., Semsarian C.;
RT "Compound and double mutations in patients with hypertrophic
RT cardiomyopathy: implications for genetic testing and counselling.";
RL J. Med. Genet. 42:E59-E59(2005).
RN [32]
RP INVOLVEMENT IN RCM3.
RX PubMed=16651346; DOI=10.1542/peds.2005-2301;
RA Peddy S.B., Vricella L.A., Crosson J.E., Oswald G.L., Cohn R.D.,
RA Cameron D.E., Valle D., Loeys B.L.;
RT "Infantile restrictive cardiomyopathy resulting from a mutation in the
RT cardiac troponin T gene.";
RL Pediatrics 117:1830-1833(2006).
RN [33]
RP VARIANTS CMH2 VAL-38 AND CYS-288, AND VARIANTS CMD1D TRP-141 AND LYS-220
RP DEL.
RX PubMed=21846512; DOI=10.1016/j.ejmg.2011.07.005;
RA Millat G., Bouvagnet P., Chevalier P., Sebbag L., Dulac A., Dauphin C.,
RA Jouk P.S., Delrue M.A., Thambo J.B., Le Metayer P., Seronde M.F.,
RA Faivre L., Eicher J.C., Rousson R.;
RT "Clinical and mutational spectrum in a cohort of 105 unrelated patients
RT with dilated cardiomyopathy.";
RL Eur. J. Med. Genet. 54:E570-E575(2011).
CC -!- FUNCTION: Troponin T is the tropomyosin-binding subunit of troponin,
CC the thin filament regulatory complex which confers calcium-sensitivity
CC to striated muscle actomyosin ATPase activity.
CC -!- INTERACTION:
CC P45379; Q15014: MORF4L2; NbExp=3; IntAct=EBI-8485957, EBI-399257;
CC P45379-11; O60341: KDM1A; NbExp=3; IntAct=EBI-17559309, EBI-710124;
CC P45379-11; Q9UH92-3: MLX; NbExp=3; IntAct=EBI-17559309, EBI-8852072;
CC P45379-11; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-17559309, EBI-10288852;
CC P45379-11; Q15172: PPP2R5A; NbExp=3; IntAct=EBI-17559309, EBI-641666;
CC P45379-11; P19237: TNNI1; NbExp=3; IntAct=EBI-17559309, EBI-746692;
CC P45379-11; P13805-3: TNNT1; NbExp=3; IntAct=EBI-17559309, EBI-12151635;
CC P45379-11; P45379-11: TNNT2; NbExp=3; IntAct=EBI-17559309, EBI-17559309;
CC P45379-11; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-17559309, EBI-11525489;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Comment=Additional isoforms seem to exist. Experimental confirmation
CC may be lacking for some isoforms.;
CC Name=1; Synonyms=TNT1;
CC IsoId=P45379-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P45379-2; Sequence=VSP_006644;
CC Name=3;
CC IsoId=P45379-3; Sequence=VSP_006645;
CC Name=4;
CC IsoId=P45379-4; Sequence=VSP_006644, VSP_006645;
CC Name=5;
CC IsoId=P45379-5; Sequence=VSP_006647;
CC Name=6; Synonyms=TNT3;
CC IsoId=P45379-6; Sequence=VSP_006643;
CC Name=7; Synonyms=TNT4;
CC IsoId=P45379-7; Sequence=VSP_006642;
CC Name=8; Synonyms=TNT2;
CC IsoId=P45379-8; Sequence=VSP_006641;
CC Name=9;
CC IsoId=P45379-9; Sequence=VSP_006646;
CC Name=10;
CC IsoId=P45379-10; Sequence=VSP_006648;
CC Name=11;
CC IsoId=P45379-11; Sequence=VSP_006643, VSP_006648;
CC Name=12;
CC IsoId=P45379-12; Sequence=VSP_006645, VSP_006646, VSP_006648;
CC -!- TISSUE SPECIFICITY: Heart. The fetal heart shows a greater expression
CC in the atrium than in the ventricle, while the adult heart shows a
CC greater expression in the ventricle than in the atrium. Isoform 6
CC predominates in normal adult heart. Isoforms 1, 7 and 8 are expressed
CC in fetal heart. Isoform 7 is also expressed in failing adult heart.
CC -!- PTM: Phosphorylation at Thr-213 by PRKCA induces significant reduction
CC in myofilament calcium sensitivity and actomyosin ATPase activity.
CC {ECO:0000250}.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 2 (CMH2) [MIM:115195]: A
CC 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:10525521, ECO:0000269|PubMed:11034944,
CC ECO:0000269|PubMed:12707239, ECO:0000269|PubMed:12974739,
CC ECO:0000269|PubMed:15563892, ECO:0000269|PubMed:16199542,
CC ECO:0000269|PubMed:21846512, ECO:0000269|PubMed:7898523,
CC ECO:0000269|PubMed:8205619, ECO:0000269|PubMed:8989109,
CC ECO:0000269|PubMed:9060892, ECO:0000269|PubMed:9140840,
CC ECO:0000269|PubMed:9482583, ECO:0000269|Ref.19}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated 1D (CMD1D) [MIM:601494]: 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:11106718,
CC ECO:0000269|PubMed:11684629, ECO:0000269|PubMed:15542288,
CC ECO:0000269|PubMed:15769782, ECO:0000269|PubMed:21846512}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cardiomyopathy, familial restrictive 3 (RCM3) [MIM:612422]: A
CC heart disorder characterized by impaired filling of the ventricles with
CC reduced diastolic volume, in the presence of normal or near normal wall
CC thickness and systolic function. {ECO:0000269|PubMed:16651346}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR EMBL; S64668; AAB27731.1; ALT_SEQ; mRNA.
DR EMBL; X74819; CAA52818.1; -; mRNA.
DR EMBL; L40162; AAA67422.1; -; mRNA.
DR EMBL; X79855; CAA56235.1; -; mRNA.
DR EMBL; X79856; CAA56236.1; -; mRNA.
DR EMBL; X79857; CAA56237.1; -; mRNA.
DR EMBL; X79858; CAA56238.1; -; mRNA.
DR EMBL; AF004422; AAC39590.1; -; Genomic_DNA.
DR EMBL; AF004409; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004410; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004411; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004412; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004413; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004414; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004415; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004416; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004417; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004418; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004419; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004420; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AF004421; AAC39590.1; JOINED; Genomic_DNA.
DR EMBL; AY044273; AAK92231.1; -; Genomic_DNA.
DR EMBL; AK290621; BAF83310.1; -; mRNA.
DR EMBL; EF179183; ABN05286.1; -; Genomic_DNA.
DR EMBL; AC119427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002653; AAH02653.1; -; mRNA.
DR EMBL; Y09626; CAA70839.1; -; Genomic_DNA.
DR EMBL; Y09627; CAA70840.1; -; Genomic_DNA.
DR EMBL; Y09628; CAA70841.1; -; Genomic_DNA.
DR EMBL; S71126; AAB30956.1; -; mRNA.
DR EMBL; S71127; AAB30957.1; -; Genomic_DNA.
DR EMBL; S71128; AAB30957.1; JOINED; Genomic_DNA.
DR CCDS; CCDS30968.1; -. [P45379-11]
DR CCDS; CCDS30969.1; -. [P45379-6]
DR CCDS; CCDS60390.1; -. [P45379-12]
DR CCDS; CCDS73003.1; -. [P45379-1]
DR PIR; A54671; TPHUTC.
DR RefSeq; NP_000355.2; NM_000364.3. [P45379-10]
DR RefSeq; NP_001001430.1; NM_001001430.2. [P45379-6]
DR RefSeq; NP_001001431.1; NM_001001431.2. [P45379-11]
DR RefSeq; NP_001001432.1; NM_001001432.2.
DR RefSeq; NP_001263274.1; NM_001276345.1. [P45379-1]
DR RefSeq; NP_001263275.1; NM_001276346.1. [P45379-12]
DR RefSeq; NP_001263276.1; NM_001276347.1. [P45379-6]
DR RefSeq; XP_006711571.1; XM_006711508.3. [P45379-6]
DR RefSeq; XP_011508240.1; XM_011509938.2. [P45379-1]
DR RefSeq; XP_011508241.1; XM_011509939.1. [P45379-3]
DR RefSeq; XP_011508242.1; XM_011509940.2. [P45379-5]
DR RefSeq; XP_011508244.1; XM_011509942.2. [P45379-7]
DR RefSeq; XP_011508245.1; XM_011509943.2. [P45379-7]
DR RefSeq; XP_016857706.1; XM_017002217.1. [P45379-11]
DR PDB; 1J1D; X-ray; 2.61 A; B/E=193-298.
DR PDB; 1J1E; X-ray; 3.30 A; B/E=193-298.
DR PDB; 4Y99; X-ray; 2.00 A; B=193-298.
DR PDB; 6KN7; EM; 6.60 A; T/a=97-282.
DR PDB; 6KN8; EM; 4.80 A; T/a=109-282.
DR PDBsum; 1J1D; -.
DR PDBsum; 1J1E; -.
DR PDBsum; 4Y99; -.
DR PDBsum; 6KN7; -.
DR PDBsum; 6KN8; -.
DR AlphaFoldDB; P45379; -.
DR SMR; P45379; -.
DR BioGRID; 112993; 15.
DR ComplexPortal; CPX-3280; Cardiac Troponin complex.
DR IntAct; P45379; 9.
DR MINT; P45379; -.
DR STRING; 9606.ENSP00000236918; -.
DR ChEMBL; CHEMBL2095202; -.
DR GlyGen; P45379; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P45379; -.
DR PhosphoSitePlus; P45379; -.
DR BioMuta; TNNT2; -.
DR DMDM; 21264536; -.
DR UCD-2DPAGE; P45379; -.
DR EPD; P45379; -.
DR MassIVE; P45379; -.
DR PaxDb; P45379; -.
DR PeptideAtlas; P45379; -.
DR PRIDE; P45379; -.
DR ProteomicsDB; 55665; -. [P45379-1]
DR ProteomicsDB; 55666; -. [P45379-10]
DR ProteomicsDB; 55667; -. [P45379-11]
DR ProteomicsDB; 55668; -. [P45379-2]
DR ProteomicsDB; 55669; -. [P45379-3]
DR ProteomicsDB; 55670; -. [P45379-4]
DR ProteomicsDB; 55671; -. [P45379-5]
DR ProteomicsDB; 55672; -. [P45379-6]
DR ProteomicsDB; 55673; -. [P45379-7]
DR ProteomicsDB; 55674; -. [P45379-8]
DR ProteomicsDB; 55675; -. [P45379-9]
DR Antibodypedia; 4204; 1227 antibodies from 45 providers.
DR CPTC; P45379; 1 antibody.
DR DNASU; 7139; -.
DR Ensembl; ENST00000236918.11; ENSP00000236918.8; ENSG00000118194.21. [P45379-1]
DR Ensembl; ENST00000360372.8; ENSP00000353535.5; ENSG00000118194.21. [P45379-12]
DR Ensembl; ENST00000367318.10; ENSP00000356287.5; ENSG00000118194.21. [P45379-6]
DR Ensembl; ENST00000367320.6; ENSP00000356289.2; ENSG00000118194.21. [P45379-12]
DR Ensembl; ENST00000412633.3; ENSP00000408731.2; ENSG00000118194.21. [P45379-11]
DR Ensembl; ENST00000422165.6; ENSP00000395163.2; ENSG00000118194.21. [P45379-10]
DR Ensembl; ENST00000509001.5; ENSP00000422031.1; ENSG00000118194.21. [P45379-6]
DR Ensembl; ENST00000656932.1; ENSP00000499593.1; ENSG00000118194.21. [P45379-1]
DR Ensembl; ENST00000660295.1; ENSP00000499418.1; ENSG00000118194.21. [P45379-6]
DR GeneID; 7139; -.
DR KEGG; hsa:7139; -.
DR MANE-Select; ENST00000656932.1; ENSP00000499593.1; NM_001276345.2; NP_001263274.1.
DR UCSC; uc001gwg.5; human. [P45379-1]
DR CTD; 7139; -.
DR DisGeNET; 7139; -.
DR GeneCards; TNNT2; -.
DR GeneReviews; TNNT2; -.
DR HGNC; HGNC:11949; TNNT2.
DR HPA; ENSG00000118194; Tissue enriched (heart).
DR MalaCards; TNNT2; -.
DR MIM; 115195; phenotype.
DR MIM; 191045; gene.
DR MIM; 601494; phenotype.
DR MIM; 612422; phenotype.
DR neXtProt; NX_P45379; -.
DR OpenTargets; ENSG00000118194; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 75249; Familial isolated restrictive cardiomyopathy.
DR Orphanet; 54260; Left ventricular noncompaction.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA36638; -.
DR VEuPathDB; HostDB:ENSG00000118194; -.
DR eggNOG; KOG3634; Eukaryota.
DR GeneTree; ENSGT00940000154709; -.
DR InParanoid; P45379; -.
DR OMA; RIXEERA; -.
DR OrthoDB; 1480247at2759; -.
DR PhylomeDB; P45379; -.
DR TreeFam; TF313321; -.
DR PathwayCommons; P45379; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P45379; -.
DR SIGNOR; P45379; -.
DR BioGRID-ORCS; 7139; 292 hits in 1066 CRISPR screens.
DR ChiTaRS; TNNT2; human.
DR EvolutionaryTrace; P45379; -.
DR GeneWiki; TNNT2; -.
DR GenomeRNAi; 7139; -.
DR Pharos; P45379; Tbio.
DR PRO; PR:P45379; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P45379; protein.
DR Bgee; ENSG00000118194; Expressed in apex of heart and 94 other tissues.
DR ExpressionAtlas; P45379; baseline and differential.
DR Genevisible; P45379; HS.
DR GO; GO:0097512; C:cardiac myofibril; IDA:CAFA.
DR GO; GO:1990584; C:cardiac Troponin complex; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030017; C:sarcomere; TAS:BHF-UCL.
DR GO; GO:0005865; C:striated muscle thin filament; IDA:UniProtKB.
DR GO; GO:0005861; C:troponin complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0005523; F:tropomyosin binding; IDA:UniProtKB.
DR GO; GO:0030172; F:troponin C binding; IPI:UniProtKB.
DR GO; GO:0031013; F:troponin I binding; IPI:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IEA:Ensembl.
DR GO; GO:0060048; P:cardiac muscle contraction; IDA:CAFA.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030049; P:muscle filament sliding; IDA:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:UniProtKB.
DR GO; GO:0032972; P:regulation of muscle filament sliding speed; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR DisProt; DP02705; -.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR027707; TNNT.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR PANTHER; PTHR11521; PTHR11521; 1.
DR Pfam; PF00992; Troponin; 2.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy;
KW Direct protein sequencing; Disease variant; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09741"
FT CHAIN 2..298
FT /note="Troponin T, cardiac muscle"
FT /id="PRO_0000186173"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P09741"
FT MOD_RES 2
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 204
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 208
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P50752"
FT MOD_RES 213
FT /note="Phosphothreonine; by PKC/PRKCA and RAF1"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 294
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT VAR_SEQ 18..32
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:7534662"
FT /id="VSP_006642"
FT VAR_SEQ 18..22
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:7534662"
FT /id="VSP_006641"
FT VAR_SEQ 23..32
FT /note="Missing (in isoform 6 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7534662,
FT ECO:0000303|PubMed:7895342, ECO:0000303|PubMed:8088824,
FT ECO:0000303|PubMed:8344420"
FT /id="VSP_006643"
FT VAR_SEQ 23
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:7895342"
FT /id="VSP_006644"
FT VAR_SEQ 54
FT /note="Missing (in isoform 3, isoform 4 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:7895342,
FT ECO:0000303|PubMed:8088824"
FT /id="VSP_006645"
FT VAR_SEQ 99..137
FT /note="Missing (in isoform 9 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:8088824"
FT /id="VSP_006646"
FT VAR_SEQ 201..203
FT /note="Missing (in isoform 10, isoform 11 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7895342, ECO:0000303|PubMed:8088824"
FT /id="VSP_006648"
FT VAR_SEQ 201
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:7895342"
FT /id="VSP_006647"
FT VARIANT 38
FT /note="A -> V (in CMH2; dbSNP:rs200754249)"
FT /evidence="ECO:0000269|PubMed:21846512"
FT /id="VAR_067259"
FT VARIANT 80
FT /note="F -> L (in CMH2; dbSNP:rs886039053)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019877"
FT VARIANT 89
FT /note="I -> N (in CMH2; dbSNP:rs121964855)"
FT /evidence="ECO:0000269|PubMed:8205619"
FT /id="VAR_007605"
FT VARIANT 102
FT /note="R -> L (in CMH2; dbSNP:rs121964856)"
FT /evidence="ECO:0000269|PubMed:8989109"
FT /id="VAR_016195"
FT VARIANT 102
FT /note="R -> Q (in CMH2; dbSNP:rs121964856)"
FT /evidence="ECO:0000269|PubMed:8205619"
FT /id="VAR_007606"
FT VARIANT 102
FT /note="R -> W (in CMH2; dbSNP:rs397516456)"
FT /evidence="ECO:0000269|PubMed:9060892"
FT /id="VAR_016196"
FT VARIANT 104
FT /note="R -> L (in CMH2; dbSNP:rs397516457)"
FT /evidence="ECO:0000269|PubMed:10525521"
FT /id="VAR_009194"
FT VARIANT 114
FT /note="A -> V (in CMH2; dbSNP:rs727504245)"
FT /evidence="ECO:0000269|PubMed:9140840"
FT /id="VAR_016197"
FT VARIANT 120
FT /note="F -> I (in CMH2; dbSNP:rs121964858)"
FT /evidence="ECO:0000269|PubMed:7898523,
FT ECO:0000269|PubMed:9482583"
FT /id="VAR_007607"
FT VARIANT 120
FT /note="F -> V (in CMH2; dbSNP:rs121964858)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019878"
FT VARIANT 139
FT /note="R -> K (in dbSNP:rs2996496)"
FT /id="VAR_013021"
FT VARIANT 140
FT /note="R -> C (in CMH2; dbSNP:rs397516463)"
FT /evidence="ECO:0000269|PubMed:15563892"
FT /id="VAR_042747"
FT VARIANT 140
FT /note="R -> K (in dbSNP:rs2996496)"
FT /id="VAR_029450"
FT VARIANT 141
FT /note="R -> W (in CMD1D; dbSNP:rs74315380)"
FT /evidence="ECO:0000269|PubMed:15542288,
FT ECO:0000269|PubMed:21846512"
FT /id="VAR_043983"
FT VARIANT 151
FT /note="R -> W (in CMD1D; dbSNP:rs74315379)"
FT /evidence="ECO:0000269|PubMed:11684629,
FT ECO:0000269|PubMed:15769782"
FT /id="VAR_016198"
FT VARIANT 170
FT /note="Missing (in CMH2)"
FT /id="VAR_007608"
FT VARIANT 173
FT /note="E -> K (in CMH2)"
FT /evidence="ECO:0000269|PubMed:7898523"
FT /id="VAR_007609"
FT VARIANT 189
FT /note="S -> F (in CMH2; dbSNP:rs727504246)"
FT /evidence="ECO:0000269|PubMed:11034944"
FT /id="VAR_016199"
FT VARIANT 210
FT /note="Missing (in CMD1D)"
FT /evidence="ECO:0000269|PubMed:11106718"
FT /id="VAR_022931"
FT VARIANT 215
FT /note="R -> L (in CMD1D; dbSNP:rs121964860)"
FT /evidence="ECO:0000269|PubMed:15542288"
FT /id="VAR_043984"
FT VARIANT 220
FT /note="Missing (in CMD1D)"
FT /evidence="ECO:0000269|PubMed:15542288,
FT ECO:0000269|PubMed:21846512"
FT /id="VAR_043985"
FT VARIANT 221
FT /note="I -> T (in dbSNP:rs45520032)"
FT /id="VAR_042748"
FT VARIANT 231
FT /note="I -> T (in dbSNP:rs45520032)"
FT /id="VAR_057310"
FT VARIANT 249
FT /note="S -> T (in dbSNP:rs2996495)"
FT /id="VAR_013022"
FT VARIANT 254
FT /note="E -> D (in CMH2; dbSNP:rs45466197)"
FT /evidence="ECO:0000269|PubMed:7898523"
FT /id="VAR_007610"
FT VARIANT 263
FT /note="K -> R (in dbSNP:rs3730238)"
FT /evidence="ECO:0000269|PubMed:9689598"
FT /id="VAR_007611"
FT VARIANT 279
FT /note="N -> Y (in dbSNP:rs4523540)"
FT /id="VAR_029451"
FT VARIANT 281
FT /note="N -> I (in CMH2; dbSNP:rs863225119)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019879"
FT VARIANT 288
FT /note="R -> C (in CMH2; dbSNP:rs121964857)"
FT /evidence="ECO:0000269|PubMed:16199542,
FT ECO:0000269|PubMed:21846512, ECO:0000269|PubMed:7898523"
FT /id="VAR_007612"
FT VARIANT 288
FT /note="R -> P (in CMH2; dbSNP:rs397516484)"
FT /evidence="ECO:0000269|PubMed:12974739, ECO:0000269|Ref.19"
FT /id="VAR_007613"
FT VARIANT 296
FT /note="R -> C (in CMH2; dbSNP:rs367785431)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019880"
FT CONFLICT 242
FT /note="K -> E (in Ref. 12; CAA70840)"
FT /evidence="ECO:0000305"
FT HELIX 210..225
FT /evidence="ECO:0007829|PDB:4Y99"
FT HELIX 236..280
FT /evidence="ECO:0007829|PDB:4Y99"
SQ SEQUENCE 298 AA; 35924 MW; 69974F2200CD5BEF CRC64;
MSDIEEVVEE YEEEEQEEAA VEEEEDWRED EDEQEEAAEE DAEAEAETEE TRAEEDEEEE
EAKEAEDGPM EESKPKPRSF MPNLVPPKIP DGERVDFDDI HRKRMEKDLN ELQALIEAHF
ENRKKEEEEL VSLKDRIERR RAERAEQQRI RNEREKERQN RLAEERARRE EEENRRKAED
EARKKKALSN MMHFGGYIQK QAQTERKSGK RQTEREKKKK ILAERRKVLA IDHLNEDQLR
EKAKELWQSI YNLEAEKFDL QEKFKQQKYE INVLRNRIND NQKVSKTRGK AKVTGRWK
