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Protein

Troponin C, skeletal muscle

Gene

TNNC2

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi31 – 42121Add
BLAST
Calcium bindingi67 – 78122Add
BLAST
Calcium bindingi107 – 118123Add
BLAST
Calcium bindingi143 – 154124Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-GGA-390522. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Troponin C, skeletal muscle
Gene namesi
Name:TNNC2
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 20

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311T → I: Decreases calcium affinity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 163162Troponin C, skeletal musclePRO_0000073707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Ala)

Proteomic databases

PaxDbiP02588.
PRIDEiP02588.

Interactioni

Protein-protein interaction databases

IntActiP02588. 2 interactions.
MINTiMINT-252237.
STRINGi9031.ENSGALP00000011046.

Structurei

Secondary structure

1
163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 144Combined sources
Helixi17 – 3014Combined sources
Beta strandi31 – 344Combined sources
Beta strandi35 – 384Combined sources
Helixi40 – 4910Combined sources
Helixi56 – 6611Combined sources
Beta strandi68 – 703Combined sources
Beta strandi72 – 754Combined sources
Helixi76 – 8712Combined sources
Helixi89 – 924Combined sources
Helixi97 – 10610Combined sources
Beta strandi111 – 1144Combined sources
Helixi116 – 1249Combined sources
Turni125 – 1273Combined sources
Helixi132 – 14211Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi147 – 1504Combined sources
Helixi152 – 1609Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVSX-ray1.75A/B2-91[»]
1BLQNMR-A2-91[»]
1CTANMR-A/B94-127[»]
1CTDNMR-A/B94-127[»]
1EW7model-C3-162[»]
1JC2NMR-A89-163[»]
1NCXX-ray1.80A2-163[»]
1NCYX-ray2.10A2-163[»]
1NCZX-ray1.80A2-163[»]
1NPQNMR-A2-91[»]
1PONNMR-A94-127[»]
B130-163[»]
1SKTNMR-A2-91[»]
1SMGNMR-A2-91[»]
1TNPNMR-A2-91[»]
1TNQNMR-A2-91[»]
1TNWNMR-A2-163[»]
1TNXNMR-A2-163[»]
1TOPX-ray1.78A2-163[»]
1YTZX-ray3.00C2-163[»]
1YV0X-ray7.00C2-163[»]
1ZACNMR-A2-91[»]
2W49electron microscopy35.000/3/6/95-163[»]
2W4Uelectron microscopy35.000/3/6/95-163[»]
4TNCX-ray2.00A3-163[»]
ProteinModelPortaliP02588.
SMRiP02588. Positions 2-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02588.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 5336EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini54 – 8936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 12936EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini130 – 16334EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the troponin C family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP02588.
KOiK12042.
OMAiNADGMLD.
PhylomeDBiP02588.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02588-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASMTDQQAE ARAFLSEEMI AEFKAAFDMF DADGGGDIST KELGTVMRML
60 70 80 90 100
GQNPTKEELD AIIEEVDEDG SGTIDFEEFL VMMVRQMKED AKGKSEEELA
110 120 130 140 150
NCFRIFDKNA DGFIDIEELG EILRATGEHV TEEDIEDLMK DSDKNNDGRI
160
DFDEFLKMME GVQ
Length:163
Mass (Da):18,375
Last modified:January 23, 2007 - v3
Checksum:iC4E1D9F40FFED3BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19027 mRNA. Translation: AAA49097.1. Sequence problems.
PIRiA03015. TPCHCS.
RefSeqiNP_990781.1. NM_205450.2.
UniGeneiGga.823.

Genome annotation databases

EnsembliENSGALT00000011060; ENSGALP00000011046; ENSGALG00000006835.
GeneIDi396434.
KEGGigga:396434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19027 mRNA. Translation: AAA49097.1. Sequence problems.
PIRiA03015. TPCHCS.
RefSeqiNP_990781.1. NM_205450.2.
UniGeneiGga.823.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AVSX-ray1.75A/B2-91[»]
1BLQNMR-A2-91[»]
1CTANMR-A/B94-127[»]
1CTDNMR-A/B94-127[»]
1EW7model-C3-162[»]
1JC2NMR-A89-163[»]
1NCXX-ray1.80A2-163[»]
1NCYX-ray2.10A2-163[»]
1NCZX-ray1.80A2-163[»]
1NPQNMR-A2-91[»]
1PONNMR-A94-127[»]
B130-163[»]
1SKTNMR-A2-91[»]
1SMGNMR-A2-91[»]
1TNPNMR-A2-91[»]
1TNQNMR-A2-91[»]
1TNWNMR-A2-163[»]
1TNXNMR-A2-163[»]
1TOPX-ray1.78A2-163[»]
1YTZX-ray3.00C2-163[»]
1YV0X-ray7.00C2-163[»]
1ZACNMR-A2-91[»]
2W49electron microscopy35.000/3/6/95-163[»]
2W4Uelectron microscopy35.000/3/6/95-163[»]
4TNCX-ray2.00A3-163[»]
ProteinModelPortaliP02588.
SMRiP02588. Positions 2-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02588. 2 interactions.
MINTiMINT-252237.
STRINGi9031.ENSGALP00000011046.

Proteomic databases

PaxDbiP02588.
PRIDEiP02588.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000011060; ENSGALP00000011046; ENSGALG00000006835.
GeneIDi396434.
KEGGigga:396434.

Organism-specific databases

CTDi7125.

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP02588.
KOiK12042.
OMAiNADGMLD.
PhylomeDBiP02588.

Enzyme and pathway databases

ReactomeiR-GGA-390522. Striated Muscle Contraction.

Miscellaneous databases

EvolutionaryTraceiP02588.
PROiP02588.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF13499. EF-hand_7. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, expression, and site-directed mutagenesis of chicken skeletal muscle troponin C."
    Reinach F.C., Karlsson R.
    J. Biol. Chem. 263:2371-2376(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Determination of and corrections to sequences of turkey and chicken troponins-C. Effects of Thr-130 to Ile mutation on Ca2+ affinity."
    Golosinska K., Pearlstone J.R., Borgford T., Oikawa K., Kay C.M., Carpenter M.R., Smillie L.B.
    J. Biol. Chem. 266:15797-15809(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-163.
  3. "The amino acid sequence of troponin C from chicken skeletal muscle."
    Wilkinson J.M.
    FEBS Lett. 70:254-256(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-163.
  4. "Molecular structure of troponin C from chicken skeletal muscle at 3-A resolution."
    Sundaralingam M., Bergstrom R., Strasburg G., Rao S.T., Raychowdhory P., Greaser M.L., Wang B.C.
    Science 227:945-948(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  5. "Refined structure of chicken skeletal muscle troponin C in the two-calcium state at 2-A resolution."
    Satyshur K.A., Rao S.T., Pyzalska D., Drendel W., Greaser M.L., Sundaralingam M.
    J. Biol. Chem. 263:1628-1647(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  6. "Structure of chicken skeletal muscle troponin C at 1.78-A resolution."
    Satyshur K.A., Pyzalska D., Rao S.T., Greaser M.L., Sundaralingam M.
    Acta Crystallogr. D 50:40-49(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS).
  7. "Structural details of a calcium-induced molecular switch: X-ray crystallographic analysis of the calcium-saturated N-terminal domain of troponin C at 1.75-A resolution."
    Strynadka N.C., Cherney M., Sielecki A.R., Li M.X., Smillie L.B., James M.N.G.
    J. Mol. Biol. 273:238-255(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
  8. "Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy."
    Shaw G.S., Hodges R.S., Sykes B.D.
    Biochemistry 31:9572-9580(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 94-127.
  9. "NMR solution structure of calcium-saturated skeletal muscle troponin C."
    Slupsky C.M., Sykes B.D.
    Biochemistry 34:15953-15964(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  10. "Low-temperature-induced structural changes in the Apo regulatory domain of skeletal muscle troponin C."
    Tsuda S., Miura A., Gagne S.M., Spyracopoulos L., Sykes B.D.
    Biochemistry 38:5693-5700(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiTNNC2_CHICK
AccessioniPrimary (citable) accession number: P02588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Skeletal muscle troponin C binds four calcium ions.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.