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Protein

Troponin I, cardiac muscle

Gene

Tnni3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei81 – 811Involved in TNI-TNT interactions
Sitei98 – 981Involved in TNI-TNT interactions

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi138 – 14912By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cardiac muscle contraction Source: MGI
  • cellular calcium ion homeostasis Source: MGI
  • heart contraction Source: MGI
  • heart development Source: MGI
  • negative regulation of ATPase activity Source: MGI
  • regulation of muscle contraction Source: MGI
  • regulation of smooth muscle contraction Source: Ensembl
  • regulation of systemic arterial blood pressure by ischemic conditions Source: MGI
  • striated muscle contraction Source: MGI
  • vasculogenesis Source: MGI
  • ventricular cardiac muscle tissue morphogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.
R-MMU-5578775. Ion homeostasis.

Names & Taxonomyi

Protein namesi
Recommended name:
Troponin I, cardiac muscle
Alternative name(s):
Cardiac troponin I
Gene namesi
Name:Tnni3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98783. Tnni3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • sarcomere Source: MGI
  • troponin complex Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 211210Troponin I, cardiac musclePRO_0000186153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei5 – 51PhosphoserineBy similarity
Modified residuei6 – 61PhosphoserineBy similarity
Modified residuei23 – 231Phosphoserine; by PKA and PKD/PRKD11 Publication
Modified residuei24 – 241Phosphoserine; by PKA and PKD/PRKD11 Publication
Modified residuei27 – 271PhosphotyrosineBy similarity
Modified residuei32 – 321Phosphothreonine; by STK4/MST1By similarity
Modified residuei43 – 431Phosphoserine; by PKC/PRKCE1 Publication
Modified residuei45 – 451Phosphoserine; by PKC/PRKCE1 Publication
Modified residuei52 – 521Phosphothreonine; by STK4/MST1By similarity
Modified residuei79 – 791PhosphothreonineBy similarity
Modified residuei130 – 1301Phosphothreonine; by STK4/MST1By similarity
Modified residuei144 – 1441Phosphothreonine; by STK4/MST1By similarity
Modified residuei151 – 1511PhosphoserineBy similarity
Modified residuei167 – 1671PhosphoserineBy similarity
Modified residuei200 – 2001PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation reduces myofilament calcium sensitivity. Phosphorylated preferentially at Thr-32. Phosphorylation by STK4/MST1 alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T) (By similarity). Phosphorylated at Ser-43 and Ser-45 by PRKCE; phosphorylation increases myocardium contractile dysfunction.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP48787.
PRIDEiP48787.

PTM databases

iPTMnetiP48787.
PhosphoSiteiP48787.

Expressioni

Gene expression databases

BgeeiP48787.
CleanExiMM_TNNI3.
ExpressionAtlasiP48787. baseline and differential.
GenevisibleiP48787. MM.

Interactioni

Subunit structurei

Interacts with TRIM63 (By similarity). Binds to actin and tropomyosin. Interacts with STK4/MST1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204266. 3 interactions.
IntActiP48787. 6 interactions.
MINTiMINT-4138144.
STRINGi10090.ENSMUSP00000096458.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 94Combined sources
Helixi24 – 318Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JPWNMR-A1-32[»]
ProteinModelPortaliP48787.
SMRiP48787. Positions 1-32, 36-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48787.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 8048Involved in binding TNCAdd
BLAST
Regioni130 – 15122Involved in binding TNC and actinAdd
BLAST

Sequence similaritiesi

Belongs to the troponin I family.Curated

Phylogenomic databases

eggNOGiKOG3977. Eukaryota.
ENOG410Y9IX. LUCA.
HOGENOMiHOG000293300.
HOVERGENiHBG052737.
InParanoidiP48787.
KOiK12044.
OMAiCRQLHTR.
OrthoDBiEOG71G9WD.
PhylomeDBiP48787.
TreeFamiTF313374.

Family and domain databases

InterProiIPR001978. Troponin.
IPR021666. Troponin-I_N.
[Graphical view]
PfamiPF00992. Troponin. 1 hit.
PF11636. Troponin-I_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P48787-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADESSDAAG EPQPAPAPVR RRSSANYRAY ATEPHAKKKS KISASRKLQL
60 70 80 90 100
KTLMLQIAKQ EMEREAEERR GEKGRVLRTR CQPLELDGLG FEELQDLCRQ
110 120 130 140 150
LHARVDKVDE ERYDVEAKVT KNITEIADLT QKIYDLRGKF KRPTLRRVRI
160 170 180 190 200
SADAMMQALL GTRAKESLDL RAHLKQVKKE DIEKENREVG DWRKNIDALS
210
GMEGRKKKFE G
Length:211
Mass (Da):24,259
Last modified:January 23, 2007 - v2
Checksum:iFB886B0E87B8D49D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22784 Genomic DNA. Translation: CAA80459.1.
U09181 mRNA. Translation: AAA19657.1.
BC061171 mRNA. Translation: AAH61171.1.
CCDSiCCDS39736.1.
PIRiA53805.
RefSeqiNP_033432.1. NM_009406.3.
UniGeneiMm.27674.

Genome annotation databases

EnsembliENSMUST00000098859; ENSMUSP00000096458; ENSMUSG00000035458.
GeneIDi21954.
KEGGimmu:21954.
UCSCiuc009exv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22784 Genomic DNA. Translation: CAA80459.1.
U09181 mRNA. Translation: AAA19657.1.
BC061171 mRNA. Translation: AAH61171.1.
CCDSiCCDS39736.1.
PIRiA53805.
RefSeqiNP_033432.1. NM_009406.3.
UniGeneiMm.27674.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JPWNMR-A1-32[»]
ProteinModelPortaliP48787.
SMRiP48787. Positions 1-32, 36-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204266. 3 interactions.
IntActiP48787. 6 interactions.
MINTiMINT-4138144.
STRINGi10090.ENSMUSP00000096458.

PTM databases

iPTMnetiP48787.
PhosphoSiteiP48787.

Proteomic databases

PaxDbiP48787.
PRIDEiP48787.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098859; ENSMUSP00000096458; ENSMUSG00000035458.
GeneIDi21954.
KEGGimmu:21954.
UCSCiuc009exv.1. mouse.

Organism-specific databases

CTDi7137.
MGIiMGI:98783. Tnni3.

Phylogenomic databases

eggNOGiKOG3977. Eukaryota.
ENOG410Y9IX. LUCA.
HOGENOMiHOG000293300.
HOVERGENiHBG052737.
InParanoidiP48787.
KOiK12044.
OMAiCRQLHTR.
OrthoDBiEOG71G9WD.
PhylomeDBiP48787.
TreeFamiTF313374.

Enzyme and pathway databases

ReactomeiR-MMU-390522. Striated Muscle Contraction.
R-MMU-5578775. Ion homeostasis.

Miscellaneous databases

EvolutionaryTraceiP48787.
PROiP48787.
SOURCEiSearch...

Gene expression databases

BgeeiP48787.
CleanExiMM_TNNI3.
ExpressionAtlasiP48787. baseline and differential.
GenevisibleiP48787. MM.

Family and domain databases

InterProiIPR001978. Troponin.
IPR021666. Troponin-I_N.
[Graphical view]
PfamiPF00992. Troponin. 1 hit.
PF11636. Troponin-I_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and regulation of the mouse cardiac troponin I gene."
    Ausoni S., Campione M., Picard A., Moretti P., Vittadello M., de Nardi C., Schiaffino S.
    J. Biol. Chem. 269:339-346(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mutagenesis of cardiac troponin I. Role of the unique NH2-terminal peptide in myofilament activation."
    Guo X., Wattanapermpool J., Palmiter K.A., Murphy A.M., Solaro R.J.
    J. Biol. Chem. 269:15210-15216(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CD-1.
    Tissue: Heart.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.
  4. "Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation."
    Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J., Buttrick P.M., Goldspink P.H.
    J. Mol. Cell. Cardiol. 40:465-473(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-43 AND SER-45.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart.
  6. "Phosphorylation-dependent conformational transition of the cardiac specific N-extension of troponin I in cardiac troponin."
    Howarth J.W., Meller J., Solaro R.J., Trewhella J., Rosevear P.R.
    J. Mol. Biol. 373:706-722(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-32, PHOSPHORYLATION AT SER-23 AND SER-24.

Entry informationi

Entry nameiTNNI3_MOUSE
AccessioniPrimary (citable) accession number: P48787
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.