TNNC1_HUMAN
ID TNNC1_HUMAN Reviewed; 161 AA.
AC P63316; O14800; P02590; P04463;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Troponin C, slow skeletal and cardiac muscles;
DE Short=TN-C;
GN Name=TNNC1; Synonyms=TNNC;
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, AND ACETYLATION AT MET-1.
RC TISSUE=Heart muscle;
RX PubMed=3951483; DOI=10.1002/mus.880090112;
RA Roher A., Lieska N., Spitz W.;
RT "The amino acid sequence of human cardiac troponin-C.";
RL Muscle Nerve 9:73-77(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Slow skeletal muscle;
RX PubMed=3166492; DOI=10.1016/0022-2836(88)90145-3;
RA Gahlmann R., Wade R., Gunning R., Kedes L.;
RT "Differential expression of slow and fast skeletal muscle troponin C. Slow
RT skeletal muscle troponin C is expressed in human fibroblasts.";
RL J. Mol. Biol. 201:379-391(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Slow skeletal muscle;
RX PubMed=2250022; DOI=10.1016/s0021-9258(17)45353-1;
RA Schreier T., Kedes L., Gahlmann R.;
RT "Cloning, structural analysis, and expression of the human slow twitch
RT skeletal muscle/cardiac troponin C gene.";
RL J. Biol. Chem. 265:21247-21253(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Margossian S.S., Yang F., Umeda P.K., Sciaky D., Anderson P.A.W.;
RT "H. sapiens mRNA for cardiac ventricular troponin C in idiopathic dilated
RT cardiomyopathy.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP STRUCTURE BY NMR OF 1-89.
RC TISSUE=Heart muscle;
RX PubMed=9315850; DOI=10.1021/bi971223d;
RA Spyracopoulos L., Li M.X., Sia S.K., Gagne S.M., Chandra M., Solaro R.J.,
RA Sykes B.D.;
RT "Calcium-induced structural transition in the regulatory domain of human
RT cardiac troponin C.";
RL Biochemistry 36:12138-12146(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).
RX PubMed=9219516; DOI=10.1111/j.1432-1033.1997.00611.x;
RA Takeda S., Kobayashi T., Taniguchi H., Hayashi H., Maeda Y.;
RT "Structural and functional domains of the troponin complex revealed by
RT limited digestion.";
RL Eur. J. Biochem. 246:611-617(1997).
RN [8]
RP STRUCTURE BY NMR OF 89-161.
RC TISSUE=Heart muscle;
RX PubMed=12732641; DOI=10.1074/jbc.m302497200;
RA Lindhout D.A., Sykes B.D.;
RT "Structure and dynamics of the C-domain of human cardiac troponin C in
RT complex with the inhibitory region of human cardiac troponin I.";
RL J. Biol. Chem. 278:27024-27034(2003).
RN [9]
RP VARIANT CMH13 GLN-29.
RX PubMed=11385718; DOI=10.1002/humu.1143;
RA Hoffmann B., Schmidt-Traub H., Perrot A., Osterziel K.J., Gessner R.;
RT "First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic
RT cardiomyopathy.";
RL Hum. Mutat. 17:524-524(2001).
RN [10]
RP VARIANT CMD1Z ASP-159.
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 [11]
RP CHARACTERIZATION OF VARIANT CMH13 GLN-29.
RX PubMed=16302972; DOI=10.1111/j.1742-4658.2005.05001.x;
RA Schmidtmann A., Lindow C., Villard S., Heuser A., Mugge A., Gessner R.,
RA Granier C., Jaquet K.;
RT "Cardiac troponin C-L29Q, related to hypertrophic cardiomyopathy, hinders
RT the transduction of the protein kinase A dependent phosphorylation signal
RT from cardiac troponin I to C.";
RL FEBS J. 272:6087-6097(2005).
RN [12]
RP VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145, AND CHARACTERIZATION OF
RP VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145.
RX PubMed=18572189; DOI=10.1016/j.yjmcc.2008.05.003;
RA Landstrom A.P., Parvatiyar M.S., Pinto J.R., Marquardt M.L., Bos J.M.,
RA Tester D.J., Ommen S.R., Potter J.D., Ackerman M.J.;
RT "Molecular and functional characterization of novel hypertrophic
RT cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C.";
RL J. Mol. Cell. Cardiol. 45:281-288(2008).
RN [13]
RP CHARACTERIZATION OF VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145.
RX PubMed=19439414; DOI=10.1074/jbc.m109.007021;
RA Pinto J.R., Parvatiyar M.S., Jones M.A., Liang J., Ackerman M.J.,
RA Potter J.D.;
RT "A functional and structural study of troponin C mutations related to
RT hypertrophic cardiomyopathy.";
RL J. Biol. Chem. 284:19090-19100(2009).
CC -!- FUNCTION: Troponin is the central regulatory protein of striated muscle
CC contraction. Tn consists of three components: Tn-I which is the
CC inhibitor of actomyosin ATPase, Tn-T which contains the binding site
CC for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the
CC inhibitory action of Tn on actin filaments.
CC -!- INTERACTION:
CC P63316; P19237: TNNI1; NbExp=5; IntAct=EBI-3906339, EBI-746692;
CC -!- DISEASE: Cardiomyopathy, dilated 1Z (CMD1Z) [MIM:611879]: 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:15542288}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 13 (CMH13) [MIM:613243]:
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:11385718, ECO:0000269|PubMed:16302972,
CC ECO:0000269|PubMed:18572189, ECO:0000269|PubMed:19439414}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: Cardiac muscle Tn-C can bind 3 calcium ions per
CC molecule. Domain I does not bind calcium.
CC -!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
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DR EMBL; X07897; CAA30736.1; -; mRNA.
DR EMBL; M37984; AAA36772.1; -; Genomic_DNA.
DR EMBL; AF020769; AAB91994.1; -; mRNA.
DR EMBL; BC030244; AAH30244.1; -; mRNA.
DR CCDS; CCDS2857.1; -.
DR RefSeq; NP_003271.1; NM_003280.2.
DR PDB; 1AP4; NMR; -; A=1-89.
DR PDB; 1IH0; NMR; -; A=91-161.
DR PDB; 1J1D; X-ray; 2.61 A; A/D=1-161.
DR PDB; 1J1E; X-ray; 3.30 A; A/D=1-161.
DR PDB; 1LXF; NMR; -; C=1-89.
DR PDB; 1MXL; NMR; -; C=1-89.
DR PDB; 1OZS; NMR; -; A=90-161.
DR PDB; 1SPY; NMR; -; A=1-89.
DR PDB; 1WRK; X-ray; 2.15 A; A/B=1-88.
DR PDB; 1WRL; X-ray; 2.60 A; A/B/C/D/E/F=1-88.
DR PDB; 2JT0; NMR; -; A=1-161.
DR PDB; 2JT3; NMR; -; A=1-161.
DR PDB; 2JT8; NMR; -; A=1-161.
DR PDB; 2JTZ; NMR; -; A=1-161.
DR PDB; 2JXL; NMR; -; A=1-89.
DR PDB; 2KDH; NMR; -; A=91-161.
DR PDB; 2KFX; NMR; -; T=1-89.
DR PDB; 2KGB; NMR; -; C=1-89.
DR PDB; 2KRD; NMR; -; C=1-89.
DR PDB; 2L1R; NMR; -; A=1-89.
DR PDB; 2L98; NMR; -; A=91-161.
DR PDB; 2MKP; NMR; -; C=1-89.
DR PDB; 2MLE; NMR; -; C=91-161.
DR PDB; 2MLF; NMR; -; C=91-161.
DR PDB; 2MZP; NMR; -; C=1-89.
DR PDB; 2N79; NMR; -; C=1-89.
DR PDB; 2N7L; NMR; -; C=1-89.
DR PDB; 3RV5; X-ray; 2.20 A; A/B/C/D=1-89.
DR PDB; 3SD6; X-ray; 1.37 A; A=1-89.
DR PDB; 3SWB; X-ray; 1.67 A; A=1-89.
DR PDB; 4GJE; X-ray; 1.60 A; A=1-89.
DR PDB; 4GJF; X-ray; 1.90 A; A=1-89.
DR PDB; 4GJG; X-ray; 2.00 A; A=1-89.
DR PDB; 4Y99; X-ray; 2.00 A; A=1-161.
DR PDB; 5VLN; NMR; -; A=1-92.
DR PDB; 5W88; NMR; -; A=1-90.
DR PDB; 5WCL; NMR; -; A=1-92.
DR PDB; 6KN7; EM; 6.60 A; V/c=2-161.
DR PDB; 6KN8; EM; 4.80 A; V/c=2-161.
DR PDB; 6MV3; NMR; -; A=1-92.
DR PDB; 7JGI; NMR; -; A=1-92.
DR PDB; 7SC2; X-ray; 1.81 A; A=1-92.
DR PDB; 7SC3; X-ray; 2.23 A; A=1-92.
DR PDB; 7SUP; NMR; -; A=2-91.
DR PDB; 7SVC; NMR; -; A=2-91.
DR PDB; 7SWG; NMR; -; A=2-91.
DR PDB; 7SWI; NMR; -; A=2-91.
DR PDB; 7SXC; NMR; -; A=2-91.
DR PDB; 7SXD; NMR; -; A=2-91.
DR PDBsum; 1AP4; -.
DR PDBsum; 1IH0; -.
DR PDBsum; 1J1D; -.
DR PDBsum; 1J1E; -.
DR PDBsum; 1LXF; -.
DR PDBsum; 1MXL; -.
DR PDBsum; 1OZS; -.
DR PDBsum; 1SPY; -.
DR PDBsum; 1WRK; -.
DR PDBsum; 1WRL; -.
DR PDBsum; 2JT0; -.
DR PDBsum; 2JT3; -.
DR PDBsum; 2JT8; -.
DR PDBsum; 2JTZ; -.
DR PDBsum; 2JXL; -.
DR PDBsum; 2KDH; -.
DR PDBsum; 2KFX; -.
DR PDBsum; 2KGB; -.
DR PDBsum; 2KRD; -.
DR PDBsum; 2L1R; -.
DR PDBsum; 2L98; -.
DR PDBsum; 2MKP; -.
DR PDBsum; 2MLE; -.
DR PDBsum; 2MLF; -.
DR PDBsum; 2MZP; -.
DR PDBsum; 2N79; -.
DR PDBsum; 2N7L; -.
DR PDBsum; 3RV5; -.
DR PDBsum; 3SD6; -.
DR PDBsum; 3SWB; -.
DR PDBsum; 4GJE; -.
DR PDBsum; 4GJF; -.
DR PDBsum; 4GJG; -.
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; P63316; -.
DR BMRB; P63316; -.
DR SMR; P63316; -.
DR BioGRID; 112988; 29.
DR ComplexPortal; CPX-3280; Cardiac Troponin complex.
DR IntAct; P63316; 10.
DR STRING; 9606.ENSP00000232975; -.
DR ChEMBL; CHEMBL2095202; -.
DR DrugBank; DB03944; 5-[1-(3,4-Dimethoxy-Benzoyl)-1,2,3,4-Tetrahydro-Quinolin-6-Yl]-6-Methyl-3,6-Dihydro-[1,3,4]Thiadiazin-2-One.
DR DrugBank; DB01375; Aluminium monostearate.
DR DrugBank; DB01244; Bepridil.
DR DrugBank; DB01373; Calcium.
DR DrugBank; DB01023; Felodipine.
DR DrugBank; DB00922; Levosimendan.
DR DrugBank; DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide.
DR DrugBank; DB00831; Trifluoperazine.
DR DrugCentral; P63316; -.
DR iPTMnet; P63316; -.
DR PhosphoSitePlus; P63316; -.
DR BioMuta; TNNC1; -.
DR DMDM; 54042075; -.
DR EPD; P63316; -.
DR jPOST; P63316; -.
DR MassIVE; P63316; -.
DR PaxDb; P63316; -.
DR PeptideAtlas; P63316; -.
DR PRIDE; P63316; -.
DR ProteomicsDB; 57520; -.
DR Antibodypedia; 3730; 453 antibodies from 34 providers.
DR DNASU; 7134; -.
DR Ensembl; ENST00000232975.8; ENSP00000232975.3; ENSG00000114854.8.
DR GeneID; 7134; -.
DR KEGG; hsa:7134; -.
DR MANE-Select; ENST00000232975.8; ENSP00000232975.3; NM_003280.3; NP_003271.1.
DR CTD; 7134; -.
DR DisGeNET; 7134; -.
DR GeneCards; TNNC1; -.
DR GeneReviews; TNNC1; -.
DR HGNC; HGNC:11943; TNNC1.
DR HPA; ENSG00000114854; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; TNNC1; -.
DR MIM; 191040; gene.
DR MIM; 611879; phenotype.
DR MIM; 613243; phenotype.
DR neXtProt; NX_P63316; -.
DR OpenTargets; ENSG00000114854; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA36632; -.
DR VEuPathDB; HostDB:ENSG00000114854; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000153541; -.
DR HOGENOM; CLU_061288_2_5_1; -.
DR InParanoid; P63316; -.
DR OMA; QKSEFRA; -.
DR OrthoDB; 1386217at2759; -.
DR PhylomeDB; P63316; -.
DR TreeFam; TF318191; -.
DR PathwayCommons; P63316; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR SignaLink; P63316; -.
DR BioGRID-ORCS; 7134; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; TNNC1; human.
DR EvolutionaryTrace; P63316; -.
DR GeneWiki; Troponin_C_type_1; -.
DR GenomeRNAi; 7134; -.
DR Pharos; P63316; Tclin.
DR PRO; PR:P63316; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P63316; protein.
DR Bgee; ENSG00000114854; Expressed in gluteal muscle and 136 other tissues.
DR ExpressionAtlas; P63316; baseline and differential.
DR Genevisible; P63316; HS.
DR GO; GO:1990584; C:cardiac Troponin complex; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005861; C:troponin complex; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0031013; F:troponin I binding; IDA:BHF-UCL.
DR GO; GO:0031014; F:troponin T binding; IPI:UniProtKB.
DR GO; GO:0060048; P:cardiac muscle contraction; IDA:CAFA.
DR GO; GO:0002086; P:diaphragm contraction; IEA:Ensembl.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; ISS:BHF-UCL.
DR GO; GO:0006937; P:regulation of muscle contraction; IDA:BHF-UCL.
DR GO; GO:0032972; P:regulation of muscle filament sliding speed; ISS:BHF-UCL.
DR GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cardiomyopathy;
KW Direct protein sequencing; Disease variant; Metal-binding; Muscle protein;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..161
FT /note="Troponin C, slow skeletal and cardiac muscles"
FT /id="PRO_0000073697"
FT DOMAIN 16..51
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 52..87
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 92..127
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 128..161
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3951483"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19123"
FT VARIANT 8
FT /note="A -> V (in CMH13; increases calcium sensitivity of
FT the myofilaments; dbSNP:rs267607125)"
FT /evidence="ECO:0000269|PubMed:18572189,
FT ECO:0000269|PubMed:19439414"
FT /id="VAR_063070"
FT VARIANT 29
FT /note="L -> Q (in CMH13; impairs protein kinase A dependent
FT signaling from cardiac troponin I to troponin C;
FT dbSNP:rs267607123)"
FT /evidence="ECO:0000269|PubMed:11385718,
FT ECO:0000269|PubMed:16302972"
FT /id="VAR_019776"
FT VARIANT 84
FT /note="C -> Y (in CMH13; increases calcium sensitivity of
FT the myofilaments; dbSNP:rs267607126)"
FT /evidence="ECO:0000269|PubMed:18572189,
FT ECO:0000269|PubMed:19439414"
FT /id="VAR_063071"
FT VARIANT 134
FT /note="E -> D (in CMH13; no changes in calcium sensitivity
FT of the myofilaments; dbSNP:rs397516847)"
FT /evidence="ECO:0000269|PubMed:18572189,
FT ECO:0000269|PubMed:19439414"
FT /id="VAR_063072"
FT VARIANT 145
FT /note="D -> E (in CMH13; increases calcium sensitivity of
FT the myofilaments; dbSNP:rs267607124)"
FT /evidence="ECO:0000269|PubMed:18572189,
FT ECO:0000269|PubMed:19439414"
FT /id="VAR_063073"
FT VARIANT 159
FT /note="G -> D (in CMD1Z; dbSNP:rs104893823)"
FT /evidence="ECO:0000269|PubMed:15542288"
FT /id="VAR_043988"
FT CONFLICT 96
FT /note="Missing (in Ref. 4; AAB91994)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="D -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..9
FT /evidence="ECO:0007829|PDB:3SD6"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:3SD6"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3SD6"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3SD6"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:3SD6"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2JT8"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:3SD6"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4Y99"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3SD6"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:3SD6"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:7SC3"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:4Y99"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2MLE"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:4Y99"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:4Y99"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1J1D"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:4Y99"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:4Y99"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:4Y99"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2JT0"
SQ SEQUENCE 161 AA; 18403 MW; 34DCCC46D503A312 CRC64;
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL FRMFDKNADG YIDLDELKIM
LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E
