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{{short description|Protein family}}
⚫
[[Image:Troponino.svg|thumb|400px|Troponin]]
[[File:Cardiac sarcomere structure.png|thumb|266x266px|Cardiac sarcomere structure, featuring troponin C]]
{{Infobox diagnostic
| name = Troponin C
| image =
| alt =
| caption =
| pronounce =
| purpose =
| test of = [[Troponin]]
| based on =
| synonyms =
| reference_range =
| calculator =
| DiseasesDB = <!--{{DiseasesDB2|numeric_id}}-->
| ICD10 = <!--{{ICD10|Group|Major|minor|LinkGroup|LinkMajor}} or {{ICD10PCS|code|char1/char2/char3/char4}}-->
| ICD9 =
| ICDO =
| MedlinePlus = <!--article_number-->
| eMedicine = <!--article_number-->
| MeshID =
| OPS301 = <!--{{OPS301|code}}-->
| LOINC = <!--{{LOINC|code}}-->
}}

⚫
[[Image:Troponino.svg|thumb|261x261px|Troponin]]
'''Troponin C''' is a protein which is part of the [[troponin]] complex. It contains four calcium-binding [[EF hand]]s, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of [[thin filament]]s, along with [[actin]] and [[tropomyosin]]. It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of [[troponin I]] (TnI). The C lobe can bind either Ca<sup>2+</sup> or Mg<sup>2+</sup>. The N lobe, which binds only Ca<sup>2+</sup>, is the regulatory lobe and binds to the C domain of troponin I after calcium binding.
'''Troponin C''' is a protein which is part of the [[troponin]] complex. It contains four calcium-binding [[EF hand]]s, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of [[thin filament]]s, along with [[actin]] and [[tropomyosin]]. It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of [[troponin I]] (TnI). The C lobe can bind either Ca<sup>2+</sup> or Mg<sup>2+</sup>. The N lobe, which binds only Ca<sup>2+</sup>, is the regulatory lobe and binds to the C domain of troponin I after calcium binding.

== Isoforms ==
{{Infobox protein
| name = Troponin C, slow skeletal and cardiac muscles
| AltNames =
| image =
| width =
| caption =
| Symbol = [[TNNC1]]
| AltSymbols =
| EntrezGene =
| HGNCid = 11943
| OMIM = 191040
| PDB =
| RefSeq = NM_003280
| UniProt = P63316
| EC_number =
| Chromosome = 3
| Arm = p
| Band = 21.1
| LocusSupplementaryData =
}}
{{Infobox protein
| name = Troponin C, skeletal muscle
| AltNames =
| image =
| width =
| caption =
| Symbol = [[TNNC2]]
| AltSymbols =
| EntrezGene =
| HGNCid = 11944
| OMIM = 191039
| PDB =
| RefSeq = NP_003270.1
| UniProt = P02585
| EC_number =
| Chromosome = 20
| Arm = q
| Band = 13.12
| LocusSupplementaryData =
}}


The tissue specific subtypes are:
The tissue specific subtypes are:
* Slow troponin C, [[TNNC1]] (3p21.3-p14.3, {{OMIM|191040}})
* Slow troponin C, [[TNNC1]] (3p21.1 {{OMIM|191040}})
* Fast troponin C, [[TNNC2]] (20q12-q13.11, {{OMIM|191039}})
* Fast troponin C, [[TNNC2]] (20q12-q13.11, {{OMIM|191039}})

<br />


== Mutations ==
== Mutations ==
Point mutations can occur in troponin C inducing alterations to Ca<sup>2+</sup> and Mg<sup>2+</sup> binding and protein structure<ref>{{Cite journal|last=Kalyva|first=Athanasia|last2=Parthenakis|first2=Fragiskos I.|last3=Marketou|first3=Maria E.|last4=Kontaraki|first4=Joanna E.|last5=Vardas|first5=Panos E.|date=2014-04|title=Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies|url=http://link.springer.com/10.1007/s10974-014-9382-0|journal=Journal of Muscle Research and Cell Motility|language=en|volume=35|issue=2|pages=161–178|doi=10.1007/s10974-014-9382-0|issn=0142-4319}}</ref>, leading to abnormalities in muscle contraction<ref>{{Cite journal|last=Cheng|first=Yuanhua|last2=Regnier|first2=Michael|date=2016-07-01|title=Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility|url=http://www.sciencedirect.com/science/article/pii/S0003986116300236|journal=Archives of Biochemistry and Biophysics|series=Special Issue: Myofilament Modulation of Contraction|volume=601|pages=11–21|doi=10.1016/j.abb.2016.02.004|issn=0003-9861|pmc=PMC4899195|pmid=26851561}}</ref><ref>{{Cite journal|last=Pinto|first=Jose Renato|last2=Parvatiyar|first2=Michelle S.|last3=Jones|first3=Michelle A.|last4=Liang|first4=Jingsheng|last5=Ackerman|first5=Michael J.|last6=Potter|first6=James D.|date=2009-07-10|title=A Functional and Structural Study of Troponin C Mutations Related to Hypertrophic Cardiomyopathy|url=http://www.jbc.org/lookup/doi/10.1074/jbc.M109.007021|journal=Journal of Biological Chemistry|language=en|volume=284|issue=28|pages=19090–19100|doi=10.1074/jbc.M109.007021|issn=0021-9258|pmc=PMC2707221|pmid=19439414}}</ref>. In cardiac muscle, they are related to '''[[Dilated cardiomyopathy]] (DCM)''' and '''[[Hypertrophic cardiomyopathy]] (HCM)'''.
Point mutations can occur in troponin C inducing alterations to Ca<sup>2+</sup> and Mg<sup>2+</sup> binding and protein structure,<ref>{{cite journal | vauthors = Kalyva A, Parthenakis FI, Marketou ME, Kontaraki JE, Vardas PE | title = Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies | journal = Journal of Muscle Research and Cell Motility | volume = 35 | issue = 2 | pages = 161–78 | date = April 2014 | pmid = 24744096 | doi = 10.1007/s10974-014-9382-0 | s2cid = 1726747 }}</ref> leading to abnormalities in muscle contraction.<ref>{{cite journal | vauthors = Cheng Y, Regnier M | title = Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility | journal = Archives of Biochemistry and Biophysics | volume = 601 | pages = 11–21 | date = July 2016 | pmid = 26851561 | pmc = 4899195 | doi = 10.1016/j.abb.2016.02.004 | series = Special Issue: Myofilament Modulation of Contraction }}</ref><ref>{{cite journal | vauthors = Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD | title = A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy | journal = The Journal of Biological Chemistry | volume = 284 | issue = 28 | pages = 19090–100 | date = July 2009 | pmid = 19439414 | pmc = 2707221 | doi = 10.1074/jbc.M109.007021 | doi-access = free }}</ref> In cardiac muscle, they are related to [[dilated cardiomyopathy]] (DCM) and [[hypertrophic cardiomyopathy]] (HCM).


These known point mutations are:
These known point mutations are:
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* I148V
* I148V


==See also==
== See also ==
* [[Troponin]]
* [[Troponin]]
* [[Troponin T]]
* [[Troponin T]]
* [[Troponin I]]
* [[Troponin I]]
* [[Calcium-binding protein]]
* [[Calcium-binding protein]]
* [[Sliding filament model]]


==External links==
== References ==
{{Reflist}}

== External links ==
* {{MeshName|Troponin+C}}
* {{MeshName|Troponin+C}}


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{{Cytoskeletal Proteins}}
{{Cytoskeletal Proteins}}
{{Calcium-binding proteins}}
{{Calcium-binding proteins}}

<references />
[[Category:Troponin]]
[[Category:Troponin]]

Latest revision as of 18:37, 31 August 2023

Cardiac sarcomere structure, featuring troponin C
Troponin C
Test ofTroponin
Troponin

Troponin C is a protein which is part of the troponin complex. It contains four calcium-binding EF hands, although different isoforms may have fewer than four functional calcium-binding subdomains. It is a component of thin filaments, along with actin and tropomyosin. It contains an N lobe and a C lobe. The C lobe serves a structural purpose and binds to the N domain of troponin I (TnI). The C lobe can bind either Ca2+ or Mg2+. The N lobe, which binds only Ca2+, is the regulatory lobe and binds to the C domain of troponin I after calcium binding.

Isoforms

[edit]
Troponin C, slow skeletal and cardiac muscles
Identifiers
SymbolTNNC1
HGNC11943
OMIM191040
RefSeqNM_003280
UniProtP63316
Other data
LocusChr. 3 p21.1
Search for
StructuresSwiss-model
DomainsInterPro
Troponin C, skeletal muscle
Identifiers
SymbolTNNC2
HGNC11944
OMIM191039
RefSeqNP_003270.1
UniProtP02585
Other data
LocusChr. 20 q13.12
Search for
StructuresSwiss-model
DomainsInterPro

The tissue specific subtypes are:

Mutations

[edit]

Point mutations can occur in troponin C inducing alterations to Ca2+ and Mg2+ binding and protein structure,[1] leading to abnormalities in muscle contraction.[2][3] In cardiac muscle, they are related to dilated cardiomyopathy (DCM) and hypertrophic cardiomyopathy (HCM).

These known point mutations are:

See also

[edit]

References

[edit]
  1. ^ Kalyva A, Parthenakis FI, Marketou ME, Kontaraki JE, Vardas PE (April 2014). "Biochemical characterisation of Troponin C mutations causing hypertrophic and dilated cardiomyopathies". Journal of Muscle Research and Cell Motility. 35 (2): 161–78. doi:10.1007/s10974-014-9382-0. PMID 24744096. S2CID 1726747.
  2. ^ Cheng Y, Regnier M (July 2016). "Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility". Archives of Biochemistry and Biophysics. Special Issue: Myofilament Modulation of Contraction. 601: 11–21. doi:10.1016/j.abb.2016.02.004. PMC 4899195. PMID 26851561.
  3. ^ Pinto JR, Parvatiyar MS, Jones MA, Liang J, Ackerman MJ, Potter JD (July 2009). "A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy". The Journal of Biological Chemistry. 284 (28): 19090–100. doi:10.1074/jbc.M109.007021. PMC 2707221. PMID 19439414.
[edit]
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