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Protein

Troponin I, cardiac muscle

Gene

TNNI3

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 4 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
Sitei80 – 801Involved in TNI-TNT interactions
Sitei97 – 971Involved in TNI-TNT interactions

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi137 – 14913By similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Troponin I, cardiac muscle
Alternative name(s):
Cardiac troponin I
Gene namesi
Name:TNNI3
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Troponin I, cardiac musclePRO_0000186154Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylalanine1 Publication
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei22 – 221Phosphoserine; by PHK, PKA and PKD/PRKD12 Publications
Modified residuei23 – 231Phosphoserine; by PKA and PKD/PRKD11 Publication
Modified residuei26 – 261PhosphotyrosineBy similarity
Modified residuei31 – 311Phosphothreonine; by STK4/MST1By similarity
Modified residuei42 – 421Phosphoserine; by PKC/PRKCEBy similarity
Modified residuei44 – 441Phosphoserine; by PKC/PRKCEBy similarity
Modified residuei51 – 511Phosphothreonine; by STK4/MST1By similarity
Modified residuei77 – 771PhosphoserineBy similarity
Modified residuei78 – 781PhosphothreonineBy similarity
Modified residuei129 – 1291Phosphothreonine; by STK4/MST1By similarity
Modified residuei143 – 1431Phosphothreonine; by STK4/MST1By similarity
Modified residuei151 – 1511Phosphoserine; by PAK3By similarity
Modified residuei182 – 1821PhosphothreonineBy similarity
Modified residuei200 – 2001PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated at Ser-22 and Ser-23 by PRKD1; phosphorylation reduces myofilament calcium sensitivity. Phosphorylated preferentially at Thr-31. Phosphorylation by STK4/MST1 alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylated at Ser-42 and Ser-44 by PRKCE; phosphorylation increases myocardium contractile dysfunction (By similarity). Ser-22 is one of three sites in the region of residues 1-48 that are phosphorylated by phosphorylase kinase.By similarity2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

PTM databases

iPTMnetiP02646.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
PASKQ96RG22EBI-8614386,EBI-1042651From a different organism.

Protein-protein interaction databases

IntActiP02646. 1 interaction.
MINTiMINT-8146737.

Structurei

3D structure databases

ProteinModelPortaliP02646.
SMRiP02646. Positions 1-31, 40-192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 7948Involved in binding TNCAdd
BLAST
Regioni129 – 15022Involved in binding TNC and actinAdd
BLAST

Sequence similaritiesi

Belongs to the troponin I family.Curated

Phylogenomic databases

HOVERGENiHBG052737.
InParanoidiP02646.

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.

P02646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADESRDAAGE ARPAPAPVRR RSSANYRAYA TEPHAKSKKK ISASRKLQLK
60 70 80 90 100
TLMLQIAKQE LEREAEERRG EKGRALSTRC QPLELAGLGF AELQDLCRQL
110 120 130 140 150
HARVDKVDEE RYDVEAKVTK NITEIADLTQ KIFDLRGKFK RPTLRLRVRI
160 170 180 190 200
SADAMMQALL GTRAKETLDL RAHLKQVKKE DTEKENREVG DWRKNIDLLS
210
GMEGRKKKFE G
Length:211
Mass (Da):24,123
Last modified:September 13, 2004 - v2
Checksum:iA15B2683C53B2F1C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171Missing AA sequence (PubMed:1008822).Curated
Sequence conflicti21 – 266RSSANY → SD AA sequence (PubMed:1008822).Curated

Sequence databases

PIRiA90296. TPRBIC.

Cross-referencesi

Sequence databases

PIRiA90296. TPRBIC.

3D structure databases

ProteinModelPortaliP02646.
SMRiP02646. Positions 1-31, 40-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP02646. 1 interaction.
MINTiMINT-8146737.

PTM databases

iPTMnetiP02646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052737.
InParanoidiP02646.

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

  1. "The amino acid sequence of rabbit cardiac troponin I."
    Grand R.J.A., Wilkinson J.M., Mole L.E.
    Biochem. J. 159:633-641(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "The amino acid sequence of rabbit slow-muscle troponin I."
    Grand R.J.A., Wilkinson J.M.
    Biochem. J. 167:183-192(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "A common motif of two adjacent phosphoserines in bovine, rabbit and human cardiac troponin I."
    Mittmann K., Jaquet K., Heilmeyer L.M.G. Jr.
    FEBS Lett. 273:41-45(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 6-36, ACETYLATION AT ALA-1, PHOSPHORYLATION AT SER-22 AND SER-23.
    Tissue: Heart.
  4. "Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart."
    Solaro R.J., Moir A.J.G., Perry S.V.
    Nature 262:615-617(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-22.

Entry informationi

Entry nameiTNNI3_RABIT
AccessioniPrimary (citable) accession number: P02646
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 13, 2004
Last modified: January 20, 2016
This is version 74 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.