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Protein

Troponin C, slow skeletal and cardiac muscles

Gene

TNNC1

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 bindingi65 – 76121Add
BLAST
Calcium bindingi105 – 116122Add
BLAST
Calcium bindingi141 – 152123Add
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, slow skeletal and cardiac muscles
Short name:
TN-C
Gene namesi
Name:TNNC1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 12

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161Troponin C, slow skeletal and cardiac musclesPRO_0000073701Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP09860.
PRIDEiP09860.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000002212.

Structurei

Secondary structure

1
161
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 114Combined sources
Helixi14 – 2714Combined sources
Turni28 – 303Combined sources
Helixi32 – 343Combined sources
Helixi38 – 4710Combined sources
Helixi54 – 6411Combined sources
Beta strandi68 – 725Combined sources
Helixi74 – 8512Combined sources
Beta strandi86 – 905Combined sources
Helixi93 – 10412Combined sources
Beta strandi109 – 1135Combined sources
Helixi114 – 1174Combined sources
Helixi118 – 1214Combined sources
Beta strandi124 – 1263Combined sources
Helixi130 – 14011Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi144 – 1496Combined sources
Helixi150 – 1589Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ4NMR-A3-161[»]
1DTLX-ray2.15A1-161[»]
1FI5NMR-A81-161[»]
1LA0NMR-A1-161[»]
1SBJNMR-A81-161[»]
1SCVNMR-A81-161[»]
2CTNNMR-A3-89[»]
3CTNNMR-A86-161[»]
ProteinModelPortaliP09860.
SMRiP09860. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09860.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 5136EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini52 – 8736EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini92 – 12736EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini128 – 16134EF-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.
InParanoidiP09860.
KOiK05865.
OMAiMNDIYKA.
OrthoDBiEOG76X61W.
PhylomeDBiP09860.
TreeFamiTF318191.

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. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDIYKAAVE QLTEEQKNEF KAAFDIFVLG AEDGCISTKE LGKVMRMLGQ
60 70 80 90 100
NPTPEELQEM IDEVDEDGSG TVDFDEFLVM MVRCMKDDSK GKTEEELSDL
110 120 130 140 150
FRMFDKNADG YIDLEELKIM LQATGETITE DDIEELMKDG DKNNDGRIDY
160
DEFLEFMKGV E
Length:161
Mass (Da):18,431
Last modified:July 1, 1989 - v1
Checksum:i426BBC46D117B247
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16024 mRNA. Translation: AAA48654.1.
D13037 mRNA. Translation: BAA02369.1.
PIRiA27204.
RefSeqiNP_990464.1. NM_205133.1.
UniGeneiGga.3041.

Genome annotation databases

EnsembliENSGALT00000002214; ENSGALP00000002212; ENSGALG00000001459.
GeneIDi396032.
KEGGigga:396032.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M16024 mRNA. Translation: AAA48654.1.
D13037 mRNA. Translation: BAA02369.1.
PIRiA27204.
RefSeqiNP_990464.1. NM_205133.1.
UniGeneiGga.3041.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ4NMR-A3-161[»]
1DTLX-ray2.15A1-161[»]
1FI5NMR-A81-161[»]
1LA0NMR-A1-161[»]
1SBJNMR-A81-161[»]
1SCVNMR-A81-161[»]
2CTNNMR-A3-89[»]
3CTNNMR-A86-161[»]
ProteinModelPortaliP09860.
SMRiP09860. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000002212.

Proteomic databases

PaxDbiP09860.
PRIDEiP09860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000002214; ENSGALP00000002212; ENSGALG00000001459.
GeneIDi396032.
KEGGigga:396032.

Organism-specific databases

CTDi7134.

Phylogenomic databases

eggNOGiKOG0027. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118901.
HOGENOMiHOG000233018.
HOVERGENiHBG012180.
InParanoidiP09860.
KOiK05865.
OMAiMNDIYKA.
OrthoDBiEOG76X61W.
PhylomeDBiP09860.
TreeFamiTF318191.

Enzyme and pathway databases

ReactomeiR-GGA-390522. Striated Muscle Contraction.

Miscellaneous databases

EvolutionaryTraceiP09860.
PROiP09860.

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. 3 hits.
PS50222. EF_HAND_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The nontranscribed chicken calmodulin pseudogene cross-hybridizes with mRNA from the slow-muscle troponin C gene."
    Putkey J.A., Carroll S.L., Means A.R.
    Mol. Cell. Biol. 7:1549-1553(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Slow skeletal muscle.
  2. "Molecular cloning and expression of chicken cardiac troponin C."
    Toyota N., Shimada Y., Bader D.
    Circ. Res. 65:1241-1246(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart muscle.
  3. "Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain."
    Sia S.K., Li M.X., Spyracopoulos L., Gagne S.M., Liu W., Putkey J.A., Sykes B.D.
    J. Biol. Chem. 272:18216-18221(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-89.
  4. "Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I."
    Gasmi-Seabrook G.M., Howarth J.W., Finley N., Abusamhadneh E., Gaponenko V., Brito R.M., Solaro R.J., Rosevear P.R.
    Biochemistry 38:8313-8322(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 81-161.

Entry informationi

Entry nameiTNNC1_CHICK
AccessioniPrimary (citable) accession number: P09860
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 6, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Slow skeletal muscle Tn-C can bind 3 calcium ions per molecule. Domain I does not bind calcium.

Keywords - Technical termi

3D-structure, Complete proteome, 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.