P19351 · TNNT_DROME

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentstriated muscle thin filament
Cellular Componenttroponin complex
Molecular Functioncalcium ion binding
Molecular Functiontropomyosin binding
Biological Processintracellular calcium ion homeostasis
Biological Processmesoderm development
Biological Processmitochondrion organization
Biological Processmuscle cell cellular homeostasis
Biological Processmuscle contraction
Biological Processmuscle organ morphogenesis
Biological Processmuscle thin filament assembly
Biological Processmyofibril assembly
Biological Processregulation of cardiac muscle contraction by calcium ion signaling
Biological Processsarcomere organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Troponin T, skeletal muscle
  • Alternative names
    • Protein intended thorax
    • Protein upheld

Gene names

    • Name
      up
    • Synonyms
      int
    • ORF names
      CG7107

Organism names

  • Taxonomic identifier
  • Strains
    • Canton-S
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    P19351
  • Secondary accessions
    • E1JJP1
    • E1JJP2
    • E1JJP3
    • E4NKN4
    • F2FB91

Proteomes

Organism-specific databases

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.

TypeIDPosition(s)Description
ChainPRO_00001861851-397Troponin T, skeletal muscle

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

Tissue specificity

Isoform 3 is expressed in the hypoderm. Isoform 8 is expressed in the dorsal vessel. Isoform 6 is expressed in adult TDT muscle and isoform 9 in adult IFM, flight and jump muscles.

Developmental stage

Isoform 2 is expressed only in larvae.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-18Acidic residues
Region1-148Disordered
Compositional bias19-147Basic and acidic residues
Compositional bias234-250Basic and acidic residues
Region234-261Disordered
Compositional bias294-334Basic and acidic residues
Region294-397Disordered
Compositional bias335-397Acidic residues

Sequence similarities

Belongs to the troponin T family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

  • Sequence status
    Complete

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.

  • Name
    1
  • Synonyms
    A
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    397
  • Mass (Da)
    47,448
  • Last updated
    2005-08-30 v3
  • Checksum
    9D1E9074548CB8D5
MSDDEEYTSSEEEEVVEETREETKPPQTPAEGEGDPEFIKRQDQKRSDLDDQLKEYITEWRKQRSKEEDELKKLKEKQAKRKVTRAEEEQKMAQRKKEEEERRVREAEEKKQREIEEKRMRLEEAEKKRQAMLQAMKDKDKKGPNFTIAKKDAGVLGLSSAAMERNKTKEQLEEEKKISLSFRIKPLAIEGFGEAKLREKAQELWELIVKLETEKYDLEERQKRQDYDLKELKERQKQQLRHKALKKGLDPEALTGKYPPKIQVASKYERRVDTRSYDDKKKLFEGGWDEISKDSNEKIWNEKKEQYTGRQKSKLPKWFGERPGKKAGEPETPEGEEDAKADEDIVEDDEEVEEEVVEEEDEEAEEDEEEEEEEEEEEEEEEEEEEEEEEEEEEEEE

P19351-2

  • Name
    2
  • Synonyms
    T-2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 9-9: Missing

P19351-3

  • Name
    3
  • Synonyms
    T-1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P19351-4

  • Name
    4
  • Synonyms
    G
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P19351-5

  • Name
    5
  • Synonyms
    K
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P19351-6

  • Name
    6
  • Synonyms
    E, T-4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P19351-7

  • Name
    7
  • Synonyms
    B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P19351-8

  • Name
    8
  • Synonyms
    T-3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P19351-9

  • Name
    9
  • Synonyms
    T-5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 9-31: Missing
    • 288-311: WDEISKDSNEKIWNEKKEQYTGRQ → YNTVYAETLEKTWQERQERFTQRT

P19351-10

  • Name
    10
  • Synonyms
    D
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

P19351-11

  • Name
    11
  • Synonyms
    I
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 288-311: WDEISKDSNEKIWNEKKEQYTGRQ → YNTVYAETLEKTWQERQERFTQRT

P19351-12

P19351-13

  • Name
    13
  • Synonyms
    J
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 24-31: Missing
    • 288-311: WDEISKDSNEKIWNEKKEQYTGRQ → YNTVYAETLEKTWQERQERFTQRT

Computationally mapped potential isoform sequences

There are 7 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E1JJP0E1JJP0_DROMEup374
M9PHJ0M9PHJ0_DROMEup396
B9EQV5B9EQV5_DROMEup373
M9PHR2M9PHR2_DROMEup397
M9PJM6M9PJM6_DROMEup388
M9NH07M9NH07_DROMEup394
X2JBP9X2JBP9_DROMEup306

Sequence caution

The sequence AAL48497.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-18Acidic residues
Alternative sequenceVSP_0151891-91in isoform 10
Alternative sequenceVSP_0151929in isoform 2, isoform 3 and isoform 8
Sequence conflict9In isoform P19351-5; in Ref. 8; ADR83716
Alternative sequenceVSP_0151919-31in isoform 6 and isoform 9
Alternative sequenceVSP_04184310in isoform 5 and isoform 12
Compositional bias19-147Basic and acidic residues
Alternative sequenceVSP_01519424in isoform 3 and isoform 5
Alternative sequenceVSP_01519324-31in isoform 7, isoform 8 and isoform 13
Alternative sequenceVSP_04184425-31in isoform 12
Sequence conflict119in Ref. 1; no nucleotide entry and 2; CAA38366
Alternative sequenceVSP_015195155in isoform 4, isoform 5 and isoform 12
Sequence conflict193in Ref. 1; no nucleotide entry and 2; CAA38366
Compositional bias234-250Basic and acidic residues
Alternative sequenceVSP_015196288-311in isoform 9, isoform 11 and isoform 13
Compositional bias294-334Basic and acidic residues
Compositional bias335-397Acidic residues
Sequence conflict364in Ref. 1; no nucleotide entry and 2; CAA38366

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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