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Troponin C, slow skeletal and cardiac muscles (TN-C)

 TNNC1_HUMAN             Reviewed;         161 AA.
P63316; O14800; P02590; P04463;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
11-OCT-2004, sequence version 1.
25-OCT-2017, entry version 139.
RecName: Full=Troponin C, slow skeletal and cardiac muscles;
Short=TN-C;
Name=TNNC1; Synonyms=TNNC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
TISSUE=Heart muscle;
PubMed=3951483; DOI=10.1002/mus.880090112;
Roher A., Lieska N., Spitz W.;
"The amino acid sequence of human cardiac troponin-C.";
Muscle Nerve 9:73-77(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Slow skeletal muscle;
PubMed=3166492; DOI=10.1016/0022-2836(88)90145-3;
Gahlmann R., Wade R., Gunning R., Kedes L.;
"Differential expression of slow and fast skeletal muscle troponin C.
Slow skeletal muscle troponin C is expressed in human fibroblasts.";
J. Mol. Biol. 201:379-391(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Slow skeletal muscle;
PubMed=2250022;
Schreier T., Kedes L., Gahlmann R.;
"Cloning, structural analysis, and expression of the human slow twitch
skeletal muscle/cardiac troponin C gene.";
J. Biol. Chem. 265:21247-21253(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Margossian S.S., Yang F., Umeda P.K., Sciaky D., Anderson P.A.W.;
"H. sapiens mRNA for cardiac ventricular troponin C in idiopathic
dilated cardiomyopathy.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
STRUCTURE BY NMR OF 1-89.
TISSUE=Heart muscle;
PubMed=9315850; DOI=10.1021/bi971223d;
Spyracopoulos L., Li M.X., Sia S.K., Gagne S.M., Chandra M.,
Solaro R.J., Sykes B.D.;
"Calcium-induced structural transition in the regulatory domain of
human cardiac troponin C.";
Biochemistry 36:12138-12146(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).
PubMed=9219516; DOI=10.1111/j.1432-1033.1997.00611.x;
Takeda S., Kobayashi T., Taniguchi H., Hayashi H., Maeda Y.;
"Structural and functional domains of the troponin complex revealed by
limited digestion.";
Eur. J. Biochem. 246:611-617(1997).
[8]
STRUCTURE BY NMR OF 89-161.
TISSUE=Heart muscle;
PubMed=12732641; DOI=10.1074/jbc.M302497200;
Lindhout D.A., Sykes B.D.;
"Structure and dynamics of the C-domain of human cardiac troponin C in
complex with the inhibitory region of human cardiac troponin I.";
J. Biol. Chem. 278:27024-27034(2003).
[9]
VARIANT CMH13 GLN-29.
PubMed=11385718; DOI=10.1002/humu.1143;
Hoffmann B., Schmidt-Traub H., Perrot A., Osterziel K.J., Gessner R.;
"First mutation in cardiac troponin C, L29Q, in a patient with
hypertrophic cardiomyopathy.";
Hum. Mutat. 17:524-524(2001).
[10]
VARIANT CMD1Z ARG-159.
PubMed=15542288; DOI=10.1016/j.jacc.2004.08.027;
Mogensen J., Murphy R.T., Shaw T., Bahl A., Redwood C., Watkins H.,
Burke M., Elliott P.M., McKenna W.J.;
"Severe disease expression of cardiac troponin C and T mutations in
patients with idiopathic dilated cardiomyopathy.";
J. Am. Coll. Cardiol. 44:2033-2040(2004).
[11]
CHARACTERIZATION OF VARIANT CMH13 GLN-29.
PubMed=16302972; DOI=10.1111/j.1742-4658.2005.05001.x;
Schmidtmann A., Lindow C., Villard S., Heuser A., Mugge A.,
Gessner R., Granier C., Jaquet K.;
"Cardiac troponin C-L29Q, related to hypertrophic cardiomyopathy,
hinders the transduction of the protein kinase A dependent
phosphorylation signal from cardiac troponin I to C.";
FEBS J. 272:6087-6097(2005).
[12]
VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145, AND
CHARACTERIZATION OF VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145.
PubMed=18572189; DOI=10.1016/j.yjmcc.2008.05.003;
Landstrom A.P., Parvatiyar M.S., Pinto J.R., Marquardt M.L., Bos J.M.,
Tester D.J., Ommen S.R., Potter J.D., Ackerman M.J.;
"Molecular and functional characterization of novel hypertrophic
cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C.";
J. Mol. Cell. Cardiol. 45:281-288(2008).
[13]
CHARACTERIZATION OF VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145.
PubMed=19439414; DOI=10.1074/jbc.M109.007021;
Pinto J.R., Parvatiyar M.S., Jones M.A., Liang J., Ackerman M.J.,
Potter J.D.;
"A functional and structural study of troponin C mutations related to
hypertrophic cardiomyopathy.";
J. Biol. Chem. 284:19090-19100(2009).
-!- FUNCTION: Troponin is the central regulatory protein of striated
muscle contraction. Tn consists of three components: Tn-I which is
the inhibitor of actomyosin ATPase, Tn-T which contains the
binding site for tropomyosin and Tn-C. The binding of calcium to
Tn-C abolishes the inhibitory action of Tn on actin filaments.
-!- INTERACTION:
P19237:TNNI1; NbExp=3; IntAct=EBI-3906339, EBI-746692;
-!- DISEASE: Cardiomyopathy, dilated 1Z (CMD1Z) [MIM:611879]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:15542288}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 13 (CMH13)
[MIM:613243]: A hereditary heart disorder characterized by
ventricular hypertrophy, which is usually asymmetric and often
involves the interventricular septum. The symptoms include
dyspnea, syncope, collapse, palpitations, and chest pain. They can
be readily provoked by exercise. The disorder has inter- and
intrafamilial variability ranging from benign to malignant forms
with high risk of cardiac failure and sudden cardiac death.
{ECO:0000269|PubMed:11385718, ECO:0000269|PubMed:16302972,
ECO:0000269|PubMed:18572189, ECO:0000269|PubMed:19439414}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Cardiac muscle Tn-C can bind 3 calcium ions per
molecule. Domain I does not bind calcium.
-!- SIMILARITY: Belongs to the troponin C family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X07897; CAA30736.1; -; mRNA.
EMBL; M37984; AAA36772.1; -; Genomic_DNA.
EMBL; AF020769; AAB91994.1; -; mRNA.
EMBL; BC030244; AAH30244.1; -; mRNA.
CCDS; CCDS2857.1; -.
RefSeq; NP_003271.1; NM_003280.2.
UniGene; Hs.118845; -.
PDB; 1AP4; NMR; -; A=1-89.
PDB; 1IH0; NMR; -; A=91-161.
PDB; 1J1D; X-ray; 2.61 A; A/D=1-161.
PDB; 1J1E; X-ray; 3.30 A; A/D=1-161.
PDB; 1LXF; NMR; -; C=1-89.
PDB; 1MXL; NMR; -; C=1-89.
PDB; 1OZS; NMR; -; A=90-161.
PDB; 1SPY; NMR; -; A=1-89.
PDB; 1WRK; X-ray; 2.15 A; A/B=1-88.
PDB; 1WRL; X-ray; 2.60 A; A/B/C/D/E/F=1-88.
PDB; 2JT0; NMR; -; A=1-161.
PDB; 2JT3; NMR; -; A=1-161.
PDB; 2JT8; NMR; -; A=1-161.
PDB; 2JTZ; NMR; -; A=1-161.
PDB; 2JXL; NMR; -; A=1-89.
PDB; 2KDH; NMR; -; A=91-161.
PDB; 2KFX; NMR; -; T=1-89.
PDB; 2KGB; NMR; -; C=1-89.
PDB; 2KRD; NMR; -; C=1-89.
PDB; 2L1R; NMR; -; A=1-89.
PDB; 2L98; NMR; -; A=91-161.
PDB; 2MKP; NMR; -; C=1-89.
PDB; 2MLE; NMR; -; C=91-161.
PDB; 2MLF; NMR; -; C=91-161.
PDB; 2MZP; NMR; -; C=1-89.
PDB; 2N79; NMR; -; C=1-89.
PDB; 2N7L; NMR; -; C=1-89.
PDB; 3RV5; X-ray; 2.20 A; A/B/C/D=1-89.
PDB; 3SD6; X-ray; 1.37 A; A=1-89.
PDB; 3SWB; X-ray; 1.67 A; A=1-89.
PDB; 4GJE; X-ray; 1.60 A; A=1-89.
PDB; 4GJF; X-ray; 1.90 A; A=1-89.
PDB; 4GJG; X-ray; 2.00 A; A=1-89.
PDB; 4Y99; X-ray; 2.00 A; A=1-161.
PDB; 5VLN; NMR; -; A=1-92.
PDB; 5W88; NMR; -; A=1-90.
PDB; 5WCL; NMR; -; A=1-92.
PDBsum; 1AP4; -.
PDBsum; 1IH0; -.
PDBsum; 1J1D; -.
PDBsum; 1J1E; -.
PDBsum; 1LXF; -.
PDBsum; 1MXL; -.
PDBsum; 1OZS; -.
PDBsum; 1SPY; -.
PDBsum; 1WRK; -.
PDBsum; 1WRL; -.
PDBsum; 2JT0; -.
PDBsum; 2JT3; -.
PDBsum; 2JT8; -.
PDBsum; 2JTZ; -.
PDBsum; 2JXL; -.
PDBsum; 2KDH; -.
PDBsum; 2KFX; -.
PDBsum; 2KGB; -.
PDBsum; 2KRD; -.
PDBsum; 2L1R; -.
PDBsum; 2L98; -.
PDBsum; 2MKP; -.
PDBsum; 2MLE; -.
PDBsum; 2MLF; -.
PDBsum; 2MZP; -.
PDBsum; 2N79; -.
PDBsum; 2N7L; -.
PDBsum; 3RV5; -.
PDBsum; 3SD6; -.
PDBsum; 3SWB; -.
PDBsum; 4GJE; -.
PDBsum; 4GJF; -.
PDBsum; 4GJG; -.
PDBsum; 4Y99; -.
PDBsum; 5VLN; -.
PDBsum; 5W88; -.
PDBsum; 5WCL; -.
ProteinModelPortal; P63316; -.
SMR; P63316; -.
BioGrid; 112988; 22.
IntAct; P63316; 8.
STRING; 9606.ENSP00000232975; -.
ChEMBL; CHEMBL2095202; -.
DrugBank; DB01375; Aluminium monostearate.
DrugBank; DB01244; Bepridil.
DrugBank; DB01373; Calcium.
DrugBank; DB01023; Felodipine.
DrugBank; DB00922; Levosimendan.
DrugBank; DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide.
DrugBank; DB00831; Trifluoperazine.
iPTMnet; P63316; -.
PhosphoSitePlus; P63316; -.
BioMuta; TNNC1; -.
DMDM; 54042075; -.
EPD; P63316; -.
PaxDb; P63316; -.
PeptideAtlas; P63316; -.
PRIDE; P63316; -.
DNASU; 7134; -.
Ensembl; ENST00000232975; ENSP00000232975; ENSG00000114854.
GeneID; 7134; -.
KEGG; hsa:7134; -.
CTD; 7134; -.
DisGeNET; 7134; -.
EuPathDB; HostDB:ENSG00000114854.7; -.
GeneCards; TNNC1; -.
GeneReviews; TNNC1; -.
HGNC; HGNC:11943; TNNC1.
HPA; CAB002450; -.
HPA; HPA044848; -.
HPA; HPA056897; -.
MalaCards; TNNC1; -.
MIM; 191040; gene.
MIM; 611879; phenotype.
MIM; 613243; phenotype.
neXtProt; NX_P63316; -.
OpenTargets; ENSG00000114854; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
PharmGKB; PA36632; -.
eggNOG; KOG0027; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118901; -.
HOGENOM; HOG000233018; -.
HOVERGEN; HBG012180; -.
InParanoid; P63316; -.
KO; K05865; -.
OMA; MNDIYKA; -.
OrthoDB; EOG091G0QHM; -.
PhylomeDB; P63316; -.
TreeFam; TF318191; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
ChiTaRS; TNNC1; human.
EvolutionaryTrace; P63316; -.
GeneWiki; Troponin_C_type_1; -.
GenomeRNAi; 7134; -.
PRO; PR:P63316; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114854; -.
CleanEx; HS_TNNC1; -.
ExpressionAtlas; P63316; baseline and differential.
Genevisible; P63316; HS.
GO; GO:1990584; C:cardiac Troponin complex; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005861; C:troponin complex; IDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0031013; F:troponin I binding; IDA:BHF-UCL.
GO; GO:0031014; F:troponin T binding; IPI:UniProtKB.
GO; GO:0060048; P:cardiac muscle contraction; IDA:CAFA.
GO; GO:0002086; P:diaphragm contraction; IEA:Ensembl.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0043462; P:regulation of ATPase activity; ISS:BHF-UCL.
GO; GO:0006937; P:regulation of muscle contraction; IDA:BHF-UCL.
GO; GO:0032972; P:regulation of muscle filament sliding speed; ISS:BHF-UCL.
GO; GO:0010038; P:response to metal ion; IEA:Ensembl.
GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
GO; GO:0014883; P:transition between fast and slow fiber; IEA:Ensembl.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
CDD; cd00051; EFh; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
Pfam; PF13833; EF-hand_8; 1.
SMART; SM00054; EFh; 4.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 3.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Cardiomyopathy; Complete proteome;
Direct protein sequencing; Disease mutation; Metal-binding;
Muscle protein; Phosphoprotein; Polymorphism; Reference proteome;
Repeat.
CHAIN 1 161 Troponin C, slow skeletal and cardiac
muscles.
/FTId=PRO_0000073697.
DOMAIN 16 51 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 52 87 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 92 127 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 128 161 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 65 76 1.
CA_BIND 105 116 2.
CA_BIND 141 152 3.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:3951483}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000250|UniProtKB:P19123}.
VARIANT 8 8 A -> V (in CMH13; increases calcium
sensitivity of the myofilaments;
dbSNP:rs267607125).
{ECO:0000269|PubMed:18572189,
ECO:0000269|PubMed:19439414}.
/FTId=VAR_063070.
VARIANT 29 29 L -> Q (in CMH13; impairs protein kinase
A dependent signaling from cardiac
troponin I to troponin C;
dbSNP:rs267607123).
{ECO:0000269|PubMed:11385718,
ECO:0000269|PubMed:16302972}.
/FTId=VAR_019776.
VARIANT 84 84 C -> Y (in CMH13; increases calcium
sensitivity of the myofilaments;
dbSNP:rs267607126).
{ECO:0000269|PubMed:18572189,
ECO:0000269|PubMed:19439414}.
/FTId=VAR_063071.
VARIANT 134 134 E -> D (in CMH13; no changes in calcium
sensitivity of the myofilaments;
dbSNP:rs397516847).
{ECO:0000269|PubMed:18572189,
ECO:0000269|PubMed:19439414}.
/FTId=VAR_063072.
VARIANT 145 145 D -> E (in CMH13; increases calcium
sensitivity of the myofilaments;
dbSNP:rs267607124).
{ECO:0000269|PubMed:18572189,
ECO:0000269|PubMed:19439414}.
/FTId=VAR_063073.
VARIANT 159 159 G -> R (in CMD1Z).
{ECO:0000269|PubMed:15542288}.
/FTId=VAR_043988.
CONFLICT 96 96 Missing (in Ref. 4; AAB91994).
{ECO:0000305}.
CONFLICT 115 115 D -> E (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 3 9 {ECO:0000244|PDB:3SD6}.
HELIX 14 25 {ECO:0000244|PDB:3SD6}.
TURN 30 32 {ECO:0000244|PDB:3SD6}.
STRAND 35 37 {ECO:0000244|PDB:3SD6}.
HELIX 38 47 {ECO:0000244|PDB:3SD6}.
STRAND 51 53 {ECO:0000244|PDB:2JT8}.
HELIX 54 64 {ECO:0000244|PDB:3SD6}.
STRAND 66 68 {ECO:0000244|PDB:4Y99}.
STRAND 71 73 {ECO:0000244|PDB:3SD6}.
HELIX 74 85 {ECO:0000244|PDB:3SD6}.
HELIX 86 89 {ECO:0000244|PDB:2N7L}.
STRAND 90 92 {ECO:0000244|PDB:2JTZ}.
HELIX 94 104 {ECO:0000244|PDB:4Y99}.
STRAND 106 108 {ECO:0000244|PDB:2MLE}.
STRAND 109 112 {ECO:0000244|PDB:4Y99}.
HELIX 114 123 {ECO:0000244|PDB:4Y99}.
STRAND 124 126 {ECO:0000244|PDB:1J1D}.
HELIX 130 140 {ECO:0000244|PDB:4Y99}.
STRAND 144 149 {ECO:0000244|PDB:4Y99}.
HELIX 150 157 {ECO:0000244|PDB:4Y99}.
TURN 158 160 {ECO:0000244|PDB:2JT0}.
SEQUENCE 161 AA; 18403 MW; 34DCCC46D503A312 CRC64;
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ NPTPEELQEM
IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKSEEELSDL FRMFDKNADG YIDLDELKIM
LQATGETITE DDIEELMKDG DKNNDGRIDY DEFLEFMKGV E


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