TNNI3_HUMAN
ID TNNI3_HUMAN Reviewed; 210 AA.
AC P19429;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Troponin I, cardiac muscle;
DE AltName: Full=Cardiac troponin I;
GN Name=TNNI3; Synonyms=TNNC1;
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].
RC TISSUE=Heart muscle;
RX PubMed=2226790; DOI=10.1016/0014-5793(90)81234-f;
RA Vallins W.J., Brand N.J., Dabhade N., Butler-Browne G., Yacoub M.H.,
RA Barton P.J.R.;
RT "Molecular cloning of human cardiac troponin I using polymerase chain
RT reaction.";
RL FEBS Lett. 270:57-61(1990).
RN [2]
RP SEQUENCE REVISION TO 85, AND NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8406024; DOI=10.1016/0378-1119(93)90308-p;
RA Armour K.L., Harris W.J., Tempest P.R.;
RT "Cloning and expression in Escherichia coli of the cDNA encoding human
RT cardiac troponin I.";
RL Gene 131:287-292(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1934363; DOI=10.1161/01.res.69.5.1409;
RA Hunkeler N.M., Kullman J., Murphy A.M.;
RT "Troponin I isoform expression in human heart.";
RL Circ. Res. 69:1409-1414(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8661099; DOI=10.1006/geno.1996.0317;
RA Bhavsar P.K., Brand N.J., Yacoub M.H., Barton P.J.R.;
RT "Isolation and characterization of the human cardiac troponin I gene
RT (TNNI3).";
RL Genomics 35:11-23(1996).
RN [5]
RP PROTEIN SEQUENCE OF 11-36, ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT
RP SER-23 AND SER-24.
RX PubMed=2226863; DOI=10.1016/0014-5793(90)81046-q;
RA Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.;
RT "A common motif of two adjacent phosphoserines in bovine, rabbit and human
RT cardiac troponin I.";
RL FEBS Lett. 273:41-45(1990).
RN [6]
RP PHOSPHORYLATION AT SER-23 AND SER-24.
RX PubMed=9346285; DOI=10.1111/j.1432-1033.1997.00329.x;
RA Keane N.E., Quirk P.G., Gao Y., Patchell V.B., Perry S.V., Levine B.A.;
RT "The ordered phosphorylation of cardiac troponin I by the cAMP-dependent
RT protein kinase -- structural consequences and functional implications.";
RL Eur. J. Biochem. 248:329-337(1997).
RN [7]
RP PHOSPHORYLATION AT SER-150 BY PAK3.
RX PubMed=12242269; DOI=10.1161/01.res.0000035246.27856.53;
RA Buscemi N., Foster D.B., Neverova I., Van Eyk J.E.;
RT "p21-activated kinase increases the calcium sensitivity of rat triton-
RT skinned cardiac muscle fiber bundles via a mechanism potentially involving
RT novel phosphorylation of troponin I.";
RL Circ. Res. 91:509-516(2002).
RN [8]
RP PHOSPHORYLATION AT SER-23 AND SER-24.
RX PubMed=15514163; DOI=10.1161/01.res.0000149299.34793.3c;
RA Haworth R.S., Cuello F., Herron T.J., Franzen G., Kentish J.C., Gautel M.,
RA Avkiran M.;
RT "Protein kinase D is a novel mediator of cardiac troponin I phosphorylation
RT and regulates myofilament function.";
RL Circ. Res. 95:1091-1099(2004).
RN [9]
RP INTERACTION WITH TRIM63.
RX PubMed=15601779; DOI=10.1073/pnas.0404341102;
RA Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C.;
RT "Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that
RT degrades cardiac troponin I.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004).
RN [10]
RP INTERACTION WITH STK4/MST1, AND PHOSPHORYLATION AT THR-31; THR-51; THR-129
RP AND THR-143.
RX PubMed=18986304; DOI=10.1042/bj20081340;
RA You B., Yan G., Zhang Z., Yan L., Li J., Ge Q., Jin J.P., Sun J.;
RT "Phosphorylation of cardiac troponin I by mammalian sterile 20-like kinase
RT 1.";
RL Biochem. J. 418:93-101(2009).
RN [11]
RP PHOSPHORYLATION AT SER-5; SER-6; SER-23; SER-24; TYR-26; SER-42; SER-44;
RP THR-51; SER-77; THR-78; THR-143; SER-166; THR-181 AND SER-199.
RX PubMed=22972900; DOI=10.1161/circulationaha.112.096388;
RA Zhang P., Kirk J.A., Ji W., dos Remedios C.G., Kass D.A., Van Eyk J.E.,
RA Murphy A.M.;
RT "Multiple reaction monitoring to identify site-specific troponin I
RT phosphorylated residues in the failing human heart.";
RL Circulation 126:1828-1837(2012).
RN [12]
RP STRUCTURE BY NMR OF 148-164.
RX PubMed=10387074; DOI=10.1021/bi9901679;
RA Li M.X., Spyracopoulos L., Sykes B.D.;
RT "Binding of cardiac troponin-I147-163 induces a structural opening in human
RT cardiac troponin-C.";
RL Biochemistry 38:8289-8298(1999).
RN [13]
RP STRUCTURE BY NMR OF 149-165 IN COMPLEX WITH CARDIAC TROPONIN C.
RX PubMed=12060657; DOI=10.1074/jbc.m203896200;
RA Wang X., Li M.X., Sykes B.D.;
RT "Structure of the regulatory N-domain of human cardiac troponin C in
RT complex with human cardiac troponin I147-163 and bepridil.";
RL J. Biol. Chem. 277:31124-31133(2002).
RN [14]
RP VARIANTS CMH7 GLY-145 AND GLN-206.
RX PubMed=9241277; DOI=10.1038/ng0897-379;
RA Kimura A., Harada H., Park J.-E., Nishi H., Satoh M., Takahashi M.,
RA Hiroi S., Sasaoka T., Ohbuchi N., Nakamura T., Koyanagi T., Hwang T.-H.,
RA Choo J., Chung K.-S., Hasegawa A., Nagai R., Okazaki O., Nakamura H.,
RA Matsuzaki M., Sakamoto T., Toshima H., Koga Y., Imaizumi T., Sasazuki T.;
RT "Mutations in the cardiac troponin I gene associated with hypertrophic
RT cardiomyopathy.";
RL Nat. Genet. 16:379-382(1997).
RN [15]
RP VARIANT CMH7 ASN-196, AND VARIANT SER-82.
RX PubMed=11815426; DOI=10.1161/hc0402.102990;
RA Niimura H., Patton K.K., McKenna W.J., Soults J., Maron B.J., Seidman J.G.,
RA Seidman C.E.;
RT "Sarcomere protein gene mutations in hypertrophic cardiomyopathy of the
RT elderly.";
RL Circulation 105:446-451(2002).
RN [16]
RP VARIANTS RCM1 GLN-144; TRP-145; THR-171; GLU-178; HIS-190 AND HIS-192.
RX PubMed=12531876; DOI=10.1172/jci200316336;
RA Mogensen J., Kubo T., Duque M., Uribe W., Shaw A., Murphy R., Gimeno J.R.,
RA Elliott P., McKenna W.J.;
RT "Idiopathic restrictive cardiomyopathy is part of the clinical expression
RT of cardiac troponin I mutations.";
RL J. Clin. Invest. 111:209-216(2003).
RN [17]
RP VARIANTS CMH7 GLN-141; VAL-157; PRO-162; LYS-177 DEL; GLN-186 AND ASN-196.
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 [18]
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 [19]
RP VARIANT CMH7 PHE-166.
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 [20]
RP VARIANT CMD2A VAL-2.
RX PubMed=15070570; DOI=10.1016/s0140-6736(04)15468-8;
RA Murphy R.T., Mogensen J., Shaw A., Kubo T., Hughes S., McKenna W.J.;
RT "Novel mutation in cardiac troponin I in recessive idiopathic dilated
RT cardiomyopathy.";
RL Lancet 363:371-372(2004).
RN [21]
RP VARIANTS CMH7 PRO-162; GLN-162 AND HIS-204.
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 [22]
RP VARIANTS CMD1FF GLN-36 AND LYS-185.
RX PubMed=19590045; DOI=10.1161/circresaha.109.196055;
RA Carballo S., Robinson P., Otway R., Fatkin D., Jongbloed J.D., de Jonge N.,
RA Blair E., van Tintelen J.P., Redwood C., Watkins H.;
RT "Identification and functional characterization of cardiac troponin I as a
RT novel disease gene in autosomal dominant dilated cardiomyopathy.";
RL Circ. Res. 105:375-382(2009).
RN [23]
RP VARIANT CMD1FF GLY-116.
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 I is the inhibitory subunit of troponin, the thin
CC filament regulatory complex which confers calcium-sensitivity to
CC striated muscle actomyosin ATPase activity.
CC -!- SUBUNIT: Binds to actin and tropomyosin. Interacts with TRIM63.
CC Interacts with STK4/MST1. {ECO:0000269|PubMed:12060657,
CC ECO:0000269|PubMed:15601779, ECO:0000269|PubMed:18986304}.
CC -!- INTERACTION:
CC P19429; Q5VU43-11: PDE4DIP; NbExp=4; IntAct=EBI-704146, EBI-10769071;
CC P19429; O43933: PEX1; NbExp=3; IntAct=EBI-704146, EBI-988601;
CC P19429; A6NK89: RASSF10; NbExp=3; IntAct=EBI-704146, EBI-6912267;
CC P19429; Q9UKA8-1: RCAN3; NbExp=3; IntAct=EBI-704146, EBI-10762111;
CC P19429; Q9UKA8-4: RCAN3; NbExp=2; IntAct=EBI-704146, EBI-10762136;
CC P19429; P02585: TNNC2; NbExp=3; IntAct=EBI-704146, EBI-10249681;
CC P19429; Q59H18: TNNI3K; NbExp=2; IntAct=EBI-704146, EBI-704142;
CC P19429; Q59H18-2: TNNI3K; NbExp=2; IntAct=EBI-704146, EBI-10762055;
CC P19429; O76024: WFS1; NbExp=3; IntAct=EBI-704146, EBI-720609;
CC -!- PTM: Phosphorylated at Ser-42 and Ser-44 by PRKCE; phosphorylation
CC increases myocardium contractile dysfunction (By similarity).
CC Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation reduces
CC myofilament calcium sensitivity. Phosphorylated preferentially at Thr-
CC 31. Phosphorylation by STK4/MST1 alters its binding affinity to TNNC1
CC (cardiac Tn-C) and TNNT2 (cardiac Tn-T). {ECO:0000250,
CC ECO:0000269|PubMed:12242269, ECO:0000269|PubMed:15514163,
CC ECO:0000269|PubMed:18986304, ECO:0000269|PubMed:2226863,
CC ECO:0000269|PubMed:22972900, ECO:0000269|PubMed:9346285}.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 7 (CMH7) [MIM:613690]: 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:11815426, ECO:0000269|PubMed:12707239,
CC ECO:0000269|PubMed:12974739, ECO:0000269|PubMed:16199542,
CC ECO:0000269|PubMed:9241277}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, familial restrictive 1 (RCM1) [MIM:115210]: 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:12531876}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated 2A (CMD2A) [MIM:611880]: 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:15070570}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cardiomyopathy, dilated 1FF (CMD1FF) [MIM:613286]: 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:19590045,
CC ECO:0000269|PubMed:21846512}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; X54163; CAA38102.1; -; mRNA.
DR EMBL; M64247; AAA16157.1; -; mRNA.
DR EMBL; X90780; CAA62301.1; -; Genomic_DNA.
DR CCDS; CCDS42628.1; -.
DR PIR; A61229; TPHUIC.
DR RefSeq; NP_000354.4; NM_000363.4.
DR PDB; 1J1D; X-ray; 2.61 A; C/F=31-163.
DR PDB; 1J1E; X-ray; 3.30 A; C/F=31-210.
DR PDB; 1LXF; NMR; -; I=148-164.
DR PDB; 1MXL; NMR; -; I=148-164.
DR PDB; 1OZS; NMR; -; B=129-148.
DR PDB; 2KGB; NMR; -; I=145-164.
DR PDB; 2KRD; NMR; -; I=148-164.
DR PDB; 2L1R; NMR; -; B=145-164.
DR PDB; 2MZP; NMR; -; I=145-171.
DR PDB; 2N7L; NMR; -; C=145-174.
DR PDB; 4Y99; X-ray; 2.00 A; C=1-210.
DR PDB; 5VLN; NMR; -; A=139-164.
DR PDB; 5W88; NMR; -; A=133-164.
DR PDB; 5WCL; NMR; -; A=139-164.
DR PDB; 6KN7; EM; 6.60 A; U/b=41-210.
DR PDB; 6KN8; EM; 4.80 A; U/b=41-166.
DR PDB; 6MV3; NMR; -; A=139-164.
DR PDB; 7JGI; NMR; -; A=139-164.
DR PDB; 7SC2; X-ray; 1.81 A; A=139-164.
DR PDB; 7SC3; X-ray; 2.23 A; A=139-164.
DR PDB; 7SUP; NMR; -; A=147-180.
DR PDB; 7SVC; NMR; -; A=147-180.
DR PDB; 7SWG; NMR; -; A=147-180.
DR PDB; 7SWI; NMR; -; A=147-180.
DR PDB; 7SXC; NMR; -; A=147-180.
DR PDB; 7SXD; NMR; -; A=147-180.
DR PDBsum; 1J1D; -.
DR PDBsum; 1J1E; -.
DR PDBsum; 1LXF; -.
DR PDBsum; 1MXL; -.
DR PDBsum; 1OZS; -.
DR PDBsum; 2KGB; -.
DR PDBsum; 2KRD; -.
DR PDBsum; 2L1R; -.
DR PDBsum; 2MZP; -.
DR PDBsum; 2N7L; -.
DR PDBsum; 4Y99; -.
DR PDBsum; 5VLN; -.
DR PDBsum; 5W88; -.
DR PDBsum; 5WCL; -.
DR PDBsum; 6KN7; -.
DR PDBsum; 6KN8; -.
DR PDBsum; 6MV3; -.
DR PDBsum; 7JGI; -.
DR PDBsum; 7SC2; -.
DR PDBsum; 7SC3; -.
DR PDBsum; 7SUP; -.
DR PDBsum; 7SVC; -.
DR PDBsum; 7SWG; -.
DR PDBsum; 7SWI; -.
DR PDBsum; 7SXC; -.
DR PDBsum; 7SXD; -.
DR AlphaFoldDB; P19429; -.
DR BMRB; P19429; -.
DR SMR; P19429; -.
DR BioGRID; 112991; 18.
DR ComplexPortal; CPX-3280; Cardiac Troponin complex.
DR DIP; DIP-34065N; -.
DR IntAct; P19429; 23.
DR MINT; P19429; -.
DR STRING; 9606.ENSP00000341838; -.
DR ChEMBL; CHEMBL2095202; -.
DR DrugBank; DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide.
DR GlyGen; P19429; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P19429; -.
DR PhosphoSitePlus; P19429; -.
DR BioMuta; TNNI3; -.
DR DMDM; 136213; -.
DR MassIVE; P19429; -.
DR PaxDb; P19429; -.
DR PeptideAtlas; P19429; -.
DR PRIDE; P19429; -.
DR ProteomicsDB; 53658; -.
DR ABCD; P19429; 5 sequenced antibodies.
DR Antibodypedia; 4354; 2575 antibodies from 52 providers.
DR CPTC; P19429; 1 antibody.
DR DNASU; 7137; -.
DR Ensembl; ENST00000344887.10; ENSP00000341838.5; ENSG00000129991.13.
DR GeneID; 7137; -.
DR KEGG; hsa:7137; -.
DR MANE-Select; ENST00000344887.10; ENSP00000341838.5; NM_000363.5; NP_000354.4.
DR CTD; 7137; -.
DR DisGeNET; 7137; -.
DR GeneCards; TNNI3; -.
DR GeneReviews; TNNI3; -.
DR HGNC; HGNC:11947; TNNI3.
DR HPA; ENSG00000129991; Tissue enriched (heart).
DR MalaCards; TNNI3; -.
DR MIM; 115210; phenotype.
DR MIM; 191044; gene.
DR MIM; 611880; phenotype.
DR MIM; 613286; phenotype.
DR MIM; 613690; phenotype.
DR neXtProt; NX_P19429; -.
DR OpenTargets; ENSG00000129991; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 75249; Familial isolated restrictive cardiomyopathy.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA36636; -.
DR VEuPathDB; HostDB:ENSG00000129991; -.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR InParanoid; P19429; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; P19429; -.
DR TreeFam; TF313374; -.
DR PathwayCommons; P19429; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR SignaLink; P19429; -.
DR SIGNOR; P19429; -.
DR BioGRID-ORCS; 7137; 18 hits in 1078 CRISPR screens.
DR ChiTaRS; TNNI3; human.
DR EvolutionaryTrace; P19429; -.
DR GeneWiki; TNNI3; -.
DR GenomeRNAi; 7137; -.
DR Pharos; P19429; Tbio.
DR PRO; PR:P19429; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P19429; protein.
DR Bgee; ENSG00000129991; Expressed in apex of heart and 99 other tissues.
DR ExpressionAtlas; P19429; baseline and differential.
DR Genevisible; P19429; HS.
DR GO; GO:0097512; C:cardiac myofibril; IMP:CAFA.
DR GO; GO:1990584; C:cardiac Troponin complex; IMP:CAFA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030017; C:sarcomere; TAS:BHF-UCL.
DR GO; GO:0005861; C:troponin complex; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IPI:CAFA.
DR GO; GO:0019855; F:calcium channel inhibitor activity; IPI:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030172; F:troponin C binding; IPI:UniProtKB.
DR GO; GO:0031014; F:troponin T binding; IPI:UniProtKB.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0060047; P:heart contraction; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:CAFA.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0001980; P:regulation of systemic arterial blood pressure by ischemic conditions; ISS:UniProtKB.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:HGNC-UCL.
DR DisProt; DP00166; -.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR021666; Troponin-I_N.
DR InterPro; IPR038077; Troponin_sf.
DR Pfam; PF00992; Troponin; 1.
DR Pfam; PF11636; Troponin-I_N; 1.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cardiomyopathy;
KW Direct protein sequencing; Disease variant; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2226863"
FT CHAIN 2..210
FT /note="Troponin I, cardiac muscle"
FT /id="PRO_0000186151"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..79
FT /note="Involved in binding TNC"
FT REGION 129..149
FT /note="Involved in binding TNC and actin"
FT SITE 80
FT /note="Involved in TNI-TNT interactions"
FT SITE 97
FT /note="Involved in TNI-TNT interactions"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2226863"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT MOD_RES 23
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:15514163,
FT ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:22972900,
FT ECO:0000269|PubMed:9346285"
FT MOD_RES 24
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:15514163,
FT ECO:0000269|PubMed:2226863, ECO:0000269|PubMed:22972900,
FT ECO:0000269|PubMed:9346285"
FT MOD_RES 26
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT MOD_RES 31
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:18986304"
FT MOD_RES 42
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 44
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 51
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:18986304,
FT ECO:0000269|PubMed:22972900"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT MOD_RES 78
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT MOD_RES 129
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:18986304"
FT MOD_RES 143
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:18986304,
FT ECO:0000269|PubMed:22972900"
FT MOD_RES 150
FT /note="Phosphoserine; by PAK3"
FT /evidence="ECO:0000269|PubMed:12242269"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22972900"
FT VARIANT 2
FT /note="A -> V (in CMD2A; dbSNP:rs397516359)"
FT /evidence="ECO:0000269|PubMed:15070570"
FT /id="VAR_043989"
FT VARIANT 36
FT /note="K -> Q (in CMD1FF; dbSNP:rs267607130)"
FT /evidence="ECO:0000269|PubMed:19590045"
FT /id="VAR_063548"
FT VARIANT 79
FT /note="R -> C (in dbSNP:rs3729712)"
FT /id="VAR_029453"
FT VARIANT 82
FT /note="P -> S (risk factor for CMH7; dbSNP:rs77615401)"
FT /evidence="ECO:0000269|PubMed:11815426"
FT /id="VAR_016078"
FT VARIANT 116
FT /note="A -> G (in CMD1FF; dbSNP:rs777177571)"
FT /evidence="ECO:0000269|PubMed:21846512"
FT /id="VAR_067264"
FT VARIANT 141
FT /note="R -> Q (in CMH7; dbSNP:rs397516347)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019872"
FT VARIANT 144
FT /note="L -> Q (in RCM1; dbSNP:rs121917760)"
FT /evidence="ECO:0000269|PubMed:12531876"
FT /id="VAR_016079"
FT VARIANT 145
FT /note="R -> G (in CMH7; dbSNP:rs104894724)"
FT /evidence="ECO:0000269|PubMed:9241277"
FT /id="VAR_007603"
FT VARIANT 145
FT /note="R -> W (in RCM1; dbSNP:rs104894724)"
FT /evidence="ECO:0000269|PubMed:12531876"
FT /id="VAR_016080"
FT VARIANT 157
FT /note="A -> V (in CMH7; dbSNP:rs397516353)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019873"
FT VARIANT 162
FT /note="R -> P (in CMH7; dbSNP:rs397516354)"
FT /evidence="ECO:0000269|PubMed:12707239,
FT ECO:0000269|PubMed:16199542"
FT /id="VAR_019874"
FT VARIANT 162
FT /note="R -> Q (in CMH7; dbSNP:rs397516354)"
FT /evidence="ECO:0000269|PubMed:16199542"
FT /id="VAR_042745"
FT VARIANT 166
FT /note="S -> F (in CMH7; dbSNP:rs727504242)"
FT /evidence="ECO:0000269|PubMed:12974739"
FT /id="VAR_029454"
FT VARIANT 171
FT /note="A -> T (in RCM1; dbSNP:rs121917761)"
FT /evidence="ECO:0000269|PubMed:12531876"
FT /id="VAR_016081"
FT VARIANT 177
FT /note="Missing (in CMH7)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019875"
FT VARIANT 178
FT /note="K -> E (in RCM1; dbSNP:rs104894730)"
FT /evidence="ECO:0000269|PubMed:12531876"
FT /id="VAR_016082"
FT VARIANT 185
FT /note="N -> K (in CMD1FF; dbSNP:rs267607129)"
FT /evidence="ECO:0000269|PubMed:19590045"
FT /id="VAR_063549"
FT VARIANT 186
FT /note="R -> Q (in CMH7; dbSNP:rs397516357)"
FT /evidence="ECO:0000269|PubMed:12707239"
FT /id="VAR_019876"
FT VARIANT 190
FT /note="D -> H (in CMH7 and RCM1)"
FT /evidence="ECO:0000269|PubMed:12531876"
FT /id="VAR_016083"
FT VARIANT 192
FT /note="R -> H (in RCM1; dbSNP:rs104894729)"
FT /evidence="ECO:0000269|PubMed:12531876"
FT /id="VAR_016084"
FT VARIANT 196
FT /note="D -> N (in CMH7; dbSNP:rs104894727)"
FT /evidence="ECO:0000269|PubMed:11815426,
FT ECO:0000269|PubMed:12707239"
FT /id="VAR_016085"
FT VARIANT 204
FT /note="R -> H (in CMH7; dbSNP:rs727504275)"
FT /evidence="ECO:0000269|PubMed:16199542"
FT /id="VAR_042746"
FT VARIANT 206
FT /note="K -> Q (in CMH7; dbSNP:rs104894725)"
FT /evidence="ECO:0000269|PubMed:9241277"
FT /id="VAR_007604"
FT HELIX 43..79
FT /evidence="ECO:0007829|PDB:4Y99"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1J1E"
FT HELIX 90..136
FT /evidence="ECO:0007829|PDB:4Y99"
FT HELIX 140..159
FT /evidence="ECO:0007829|PDB:7SC2"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4Y99"
FT HELIX 163..188
FT /evidence="ECO:0007829|PDB:1J1E"
SQ SEQUENCE 210 AA; 24008 MW; 20A804F8C24AE1B0 CRC64;
MADGSSDAAR EPRPAPAPIR RRSSNYRAYA TEPHAKKKSK ISASRKLQLK TLLLQIAKQE
LEREAEERRG EKGRALSTRC QPLELAGLGF AELQDLCRQL HARVDKVDEE RYDIEAKVTK
NITEIADLTQ KIFDLRGKFK RPTLRRVRIS ADAMMQALLG ARAKESLDLR AHLKQVKKED
TEKENREVGD WRKNIDALSG MEGRKKKFES
