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Identification
HMDB Protein ID HMDBP08057
Secondary Accession Numbers
  • 13768
Name Troponin C, slow skeletal and cardiac muscles
Synonyms
  1. TN-C
Gene Name TNNC1
Protein Type Unknown
Biological Properties
General Function Involved in calcium ion binding
Specific 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
Pathways
  • Acebutolol Action Pathway
  • Alprenolol Action Pathway
  • Amiodarone Action Pathway
  • Amlodipine Action Pathway
  • Arbutamine Action Pathway
  • Atenolol Action Pathway
  • Betaxolol Action Pathway
  • Bevantolol Action Pathway
  • Bisoprolol Action Pathway
  • Bopindolol Action Pathway
  • Bupranolol Action Pathway
  • Carteolol Action Pathway
  • Carvedilol Action Pathway
  • Diltiazem Action Pathway
  • Disopyramide Action Pathway
  • Dobutamine Action Pathway
  • Epinephrine Action Pathway
  • Esmolol Action Pathway
  • Felodipine Action Pathway
  • Flecainide Action Pathway
  • Fosphenytoin (Antiarrhythmic) Action Pathway
  • Ibutilide Action Pathway
  • Isoprenaline Action Pathway
  • Isradipine Action Pathway
  • Labetalol Action Pathway
  • Levobunolol Action Pathway
  • Lidocaine (Antiarrhythmic) Action Pathway
  • Metipranolol Action Pathway
  • Metoprolol Action Pathway
  • Mexiletine Action Pathway
  • Muscle/Heart Contraction
  • Nadolol Action Pathway
  • Nebivolol Action Pathway
  • Nifedipine Action Pathway
  • Nimodipine Action Pathway
  • Nisoldipine Action Pathway
  • Nitrendipine Action Pathway
  • Oxprenolol Action Pathway
  • Penbutolol Action Pathway
  • Phenytoin (Antiarrhythmic) Action Pathway
  • Pindolol Action Pathway
  • Practolol Action Pathway
  • Procainamide (Antiarrhythmic) Action Pathway
  • Propranolol Action Pathway
  • Quinidine Action Pathway
  • Sotalol Action Pathway
  • Timolol Action Pathway
  • Tocainide Action Pathway
  • Verapamil Action Pathway
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
binding
calcium ion binding
Cellular Location Not Available
Gene Properties
Chromosome Location Chromosome:3
Locus 3p21.1
SNPs TNNC1
Gene Sequence
>486 bp
ATGGATGACATCTACAAGGCTGCGGTAGAGCAGCTGACAGAAGAGCAGAAAAATGAGTTC
AAGGCAGCCTTCGACATCTTCGTGCTGGGCGCTGAGGATGGCTGCATCAGCACCAAGGAG
CTGGGCAAGGTGATGAGGATGCTGGGCCAGAACCCCACCCCTGAGGAGCTGCAGGAGATG
ATCGATGAGGTGGACGAGGACGGCAGCGGCACGGTGGACTTTGATGAGTTCCTGGTCATG
ATGGTTCGGTGCATGAAGGACGACAGCAAAGGGAAATCTGAGGAGGAGCTGTCTGACCTC
TTCCGCATGTTTGACAAAAATGCTGATGGCTACATCGACCTGGATGAGCTGAAGATAATG
CTGCAGGCTACAGGCGAGACCATCACGGAGGACGACATCGAGGAGCTCATGAAGGACGGA
GACAAGAACAACGACGGCCGCATCGACTATGATGAGTTCCTGGAGTTCATGAAGGGTGTG
GAGTAG
Protein Properties
Number of Residues 161
Molecular Weight 18402.4
Theoretical pI 3.78
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Troponin C, slow skeletal and cardiac muscles
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEM
IDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKIM
LQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
GenBank ID Protein 4507615
UniProtKB/Swiss-Prot ID P63316
UniProtKB/Swiss-Prot Entry Name TNNC1_HUMAN
PDB IDs
GenBank Gene ID NM_003280.2
GeneCard ID TNNC1
GenAtlas ID TNNC1
HGNC ID HGNC:11943
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Roher A, Lieska N, Spitz W: The amino acid sequence of human cardiac troponin-C. Muscle Nerve. 1986 Jan;9(1):73-7. [PubMed:3951483 ]
  3. Gahlmann R, Wade R, Gunning P, 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. 1988 May 20;201(2):379-91. [PubMed:3166492 ]
  4. 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. 1990 Dec 5;265(34):21247-53. [PubMed:2250022 ]
  5. Spyracopoulos L, Li MX, Sia SK, Gagne SM, Chandra M, Solaro RJ, Sykes BD: Calcium-induced structural transition in the regulatory domain of human cardiac troponin C. Biochemistry. 1997 Oct 7;36(40):12138-46. [PubMed:9315850 ]
  6. 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. 1997 Jun 15;246(3):611-7. [PubMed:9219516 ]
  7. Lindhout DA, Sykes BD: 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. 2003 Jul 18;278(29):27024-34. Epub 2003 May 5. [PubMed:12732641 ]
  8. Hoffmann B, Schmidt-Traub H, Perrot A, Osterziel KJ, Gessner R: First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy. Hum Mutat. 2001 Jun;17(6):524. [PubMed:11385718 ]
  9. Mogensen J, Murphy RT, Shaw T, Bahl A, Redwood C, Watkins H, Burke M, Elliott PM, McKenna WJ: Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy. J Am Coll Cardiol. 2004 Nov 16;44(10):2033-40. [PubMed:15542288 ]
  10. 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. 2005 Dec;272(23):6087-97. [PubMed:16302972 ]
  11. Landstrom AP, Parvatiyar MS, Pinto JR, Marquardt ML, Bos JM, Tester DJ, Ommen SR, Potter JD, Ackerman MJ: Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C. J Mol Cell Cardiol. 2008 Aug;45(2):281-8. doi: 10.1016/j.yjmcc.2008.05.003. Epub 2008 May 11. [PubMed:18572189 ]
  12. Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD: A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy. J Biol Chem. 2009 Jul 10;284(28):19090-100. doi: 10.1074/jbc.M109.007021. Epub 2009 May 12. [PubMed:19439414 ]