P19351 · TNNT_DROME
- ProteinTroponin T, skeletal muscle
- Geneup
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids397 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | striated muscle thin filament | |
Cellular Component | troponin complex | |
Molecular Function | calcium ion binding | |
Molecular Function | tropomyosin binding | |
Biological Process | intracellular calcium ion homeostasis | |
Biological Process | mesoderm development | |
Biological Process | mitochondrion organization | |
Biological Process | muscle cell cellular homeostasis | |
Biological Process | muscle contraction | |
Biological Process | muscle organ morphogenesis | |
Biological Process | muscle thin filament assembly | |
Biological Process | myofibril assembly | |
Biological Process | regulation of cardiac muscle contraction by calcium ion signaling | |
Biological Process | sarcomere organization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTroponin T, skeletal muscle
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP19351
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Flies exhibit 3 distinct syndromes of myofibrillar abnormalities; elimination of thin filaments except where they are bound by electron-dense material presumed to be Z-disk proteins, degeneration of muscles and reduction in the diameter of the myofibril lattice.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000186185 | 1-397 | Troponin T, skeletal muscle | |||
Sequence: MSDDEEYTSSEEEEVVEETREETKPPQTPAEGEGDPEFIKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQREIEEKRMRLEEAEKKRQAMLQAMKDKDKKGPNFTIAKKDAGVLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLEERQKRQDYDLKELKERQKQQLRHKALKKGLDPEALTGKYPPKIQVASKYERRVDTRSYDDKKKLFEGGWDEISKDSNEKIWNEKKEQYTGRQKSKLPKWFGERPGKKAGEPETPEGEEDAKADEDIVEDDEEVEEEVVEEEDEEAEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEE |
Post-translational modification
Some glutamate residues are polyglycylated by TTLL3B. This modification occurs exclusively on glutamate residues and results in polyglycine chains on the gamma-carboxyl group.
Proteomic databases
Expression
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Acidic residues | ||||
Sequence: MSDDEEYTSSEEEEVVEE | ||||||
Region | 1-148 | Disordered | ||||
Sequence: MSDDEEYTSSEEEEVVEETREETKPPQTPAEGEGDPEFIKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQREIEEKRMRLEEAEKKRQAMLQAMKDKDKKGPNFTI | ||||||
Compositional bias | 19-147 | Basic and acidic residues | ||||
Sequence: TREETKPPQTPAEGEGDPEFIKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQREIEEKRMRLEEAEKKRQAMLQAMKDKDKKGPNFT | ||||||
Compositional bias | 234-250 | Basic and acidic residues | ||||
Sequence: ERQKQQLRHKALKKGLD | ||||||
Region | 234-261 | Disordered | ||||
Sequence: ERQKQQLRHKALKKGLDPEALTGKYPPK | ||||||
Compositional bias | 294-334 | Basic and acidic residues | ||||
Sequence: DSNEKIWNEKKEQYTGRQKSKLPKWFGERPGKKAGEPETPE | ||||||
Region | 294-397 | Disordered | ||||
Sequence: DSNEKIWNEKKEQYTGRQKSKLPKWFGERPGKKAGEPETPEGEEDAKADEDIVEDDEEVEEEVVEEEDEEAEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEE | ||||||
Compositional bias | 335-397 | Acidic residues | ||||
Sequence: GEEDAKADEDIVEDDEEVEEEVVEEEDEEAEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEE |
Sequence similarities
Belongs to the troponin T family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 13 isoforms produced by Alternative splicing.
P19351-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsA
- Length397
- Mass (Da)47,448
- Last updated2005-08-30 v3
- Checksum9D1E9074548CB8D5
P19351-2
- Name2
- SynonymsT-2
- Differences from canonical
- 9-9: Missing
P19351-3
- Name3
- SynonymsT-1
P19351-4
- Name4
- SynonymsG
- Differences from canonical
- 155-155: Missing
P19351-5
- Name5
- SynonymsK
P19351-6
- Name6
- SynonymsE, T-4
- Differences from canonical
- 9-31: Missing
P19351-7
- Name7
- SynonymsB
- Differences from canonical
- 24-31: Missing
P19351-8
- Name8
- SynonymsT-3
P19351-9
- Name9
- SynonymsT-5
P19351-10
- Name10
- SynonymsD
- Differences from canonical
- 1-91: Missing
P19351-11
- Name11
- SynonymsI
- Differences from canonical
- 288-311: WDEISKDSNEKIWNEKKEQYTGRQ → YNTVYAETLEKTWQERQERFTQRT
P19351-12
- Name12
- SynonymsL
P19351-13
- Name13
- SynonymsJ
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-18 | Acidic residues | ||||
Sequence: MSDDEEYTSSEEEEVVEE | ||||||
Alternative sequence | VSP_015189 | 1-91 | in isoform 10 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_015192 | 9 | in isoform 2, isoform 3 and isoform 8 | |||
Sequence: Missing | ||||||
Sequence conflict | 9 | In isoform P19351-5; in Ref. 8; ADR83716 | ||||
Sequence: S → SS | ||||||
Alternative sequence | VSP_015191 | 9-31 | in isoform 6 and isoform 9 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_041843 | 10 | in isoform 5 and isoform 12 | |||
Sequence: Missing | ||||||
Compositional bias | 19-147 | Basic and acidic residues | ||||
Sequence: TREETKPPQTPAEGEGDPEFIKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQREIEEKRMRLEEAEKKRQAMLQAMKDKDKKGPNFT | ||||||
Alternative sequence | VSP_015194 | 24 | in isoform 3 and isoform 5 | |||
Sequence: K → KK | ||||||
Alternative sequence | VSP_015193 | 24-31 | in isoform 7, isoform 8 and isoform 13 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_041844 | 25-31 | in isoform 12 | |||
Sequence: Missing | ||||||
Sequence conflict | 119 | in Ref. 1; no nucleotide entry and 2; CAA38366 | ||||
Sequence: R → A | ||||||
Alternative sequence | VSP_015195 | 155 | in isoform 4, isoform 5 and isoform 12 | |||
Sequence: Missing | ||||||
Sequence conflict | 193 | in Ref. 1; no nucleotide entry and 2; CAA38366 | ||||
Sequence: G → A | ||||||
Compositional bias | 234-250 | Basic and acidic residues | ||||
Sequence: ERQKQQLRHKALKKGLD | ||||||
Alternative sequence | VSP_015196 | 288-311 | in isoform 9, isoform 11 and isoform 13 | |||
Sequence: WDEISKDSNEKIWNEKKEQYTGRQ → YNTVYAETLEKTWQERQERFTQRT | ||||||
Compositional bias | 294-334 | Basic and acidic residues | ||||
Sequence: DSNEKIWNEKKEQYTGRQKSKLPKWFGERPGKKAGEPETPE | ||||||
Compositional bias | 335-397 | Acidic residues | ||||
Sequence: GEEDAKADEDIVEDDEEVEEEVVEEEDEEAEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEE | ||||||
Sequence conflict | 364 | in Ref. 1; no nucleotide entry and 2; CAA38366 | ||||
Sequence: A → D |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X54504 EMBL· GenBank· DDBJ | CAA38366.1 EMBL· GenBank· DDBJ | mRNA | ||
AY439172 EMBL· GenBank· DDBJ | AAR24583.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY439172 EMBL· GenBank· DDBJ | AAR24584.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY439172 EMBL· GenBank· DDBJ | AAR24585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY439172 EMBL· GenBank· DDBJ | AAR24586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY439172 EMBL· GenBank· DDBJ | AAR24587.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY665838 EMBL· GenBank· DDBJ | AAU09446.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF48288.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF48289.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAF48290.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAX52491.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAX52492.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | AAX52493.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | ACZ95277.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | ACZ95278.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE014298 EMBL· GenBank· DDBJ | ACZ95279.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY051989 EMBL· GenBank· DDBJ | AAK93413.1 EMBL· GenBank· DDBJ | mRNA | ||
AY070875 EMBL· GenBank· DDBJ | AAL48497.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BT125831 EMBL· GenBank· DDBJ | ADR83716.1 EMBL· GenBank· DDBJ | mRNA | ||
BT126178 EMBL· GenBank· DDBJ | ADZ99430.1 EMBL· GenBank· DDBJ | mRNA |