ID TNNI3_BOVIN Reviewed; 212 AA. AC P08057; Q5ZG22; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 144. DE RecName: Full=Troponin I, cardiac muscle; DE AltName: Full=Cardiac troponin I; GN Name=TNNI3; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Peripheral blood; RA Guziewicz K.; RT "Bovine dilated cardiomyopathy: evidence for a major gene on BTA18."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-212, AND ACETYLATION AT ALA-2. RX PubMed=3042023; DOI=10.1021/bi00408a024; RA Leszyk J., Dumaswala R., Potter J.D., Collins J.H.; RT "Amino acid sequence of bovine cardiac troponin I."; RL Biochemistry 27:2821-2827(1988). RN [3] RP PROTEIN SEQUENCE OF 2-212. RX PubMed=2967699; DOI=10.1016/s0006-291x(88)80426-1; RA Creutz C.E., Snyder S.L., Husted L.D., Beggerly L.K., Fox J.W.; RT "Pattern of repeating aromatic residues in synexin. Similarity to the RT cytoplasmic domain of synaptophysin."; RL Biochem. Biophys. Res. Commun. 152:1298-1303(1988). CC -!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin CC filament regulatory complex which confers calcium-sensitivity to CC striated muscle actomyosin ATPase activity. CC -!- SUBUNIT: Interacts with TRIM63 (By similarity). Binds to actin and CC tropomyosin. Interacts with STK4/MST1 (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated at Ser-24 and Ser-25 by PRKD1; phosphorylation CC reduces myofilament calcium sensitivity. Phosphorylated preferentially CC at Thr-33. Phosphorylation by STK4/MST1 alters its binding affinity to CC TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylated at Ser-44 CC and Ser-46 by PRKCE; phosphorylation increases myocardium contractile CC dysfunction (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ842179; CAH57016.1; -; Genomic_DNA. DR PIR; A29994; A29994. DR RefSeq; NP_001035607.1; NM_001040517.1. DR AlphaFoldDB; P08057; -. DR BMRB; P08057; -. DR SMR; P08057; -. DR FunCoup; P08057; 114. DR IntAct; P08057; 1. DR iPTMnet; P08057; -. DR GeneID; 511094; -. DR KEGG; bta:511094; -. DR CTD; 7137; -. DR VGNC; VGNC:36193; TNNI3. DR eggNOG; KOG3977; Eukaryota. DR HOGENOM; CLU_098686_1_0_1; -. DR InParanoid; P08057; -. DR OrthoDB; 371899at2759; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0097512; C:cardiac myofibril; IDA:CAFA. DR GO; GO:1990584; C:cardiac Troponin complex; IDA:CAFA. DR GO; GO:0005861; C:troponin complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IDA:CAFA. DR GO; GO:0042030; F:ATPase inhibitor activity; IDA:CAFA. DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA. DR GO; GO:0030172; F:troponin C binding; IPI:CAFA. DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central. DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central. DR FunFam; 1.20.5.350:FF:000002; troponin I, fast skeletal muscle; 1. DR Gene3D; 1.20.5.350; -; 1. DR Gene3D; 6.10.250.180; -; 1. DR InterPro; IPR001978; Troponin. DR InterPro; IPR021666; Troponin-I_N. DR InterPro; IPR050875; Troponin_I. DR InterPro; IPR038077; Troponin_sf. DR PANTHER; PTHR13738; TROPONIN I; 1. DR PANTHER; PTHR13738:SF2; TROPONIN I, CARDIAC MUSCLE; 1. DR Pfam; PF00992; Troponin; 1. DR Pfam; PF11636; Troponin-I_N; 1. DR SUPFAM; SSF90250; Troponin coil-coiled subunits; 1. PE 1: Evidence at protein level; KW Acetylation; Actin-binding; Direct protein sequencing; Muscle protein; KW Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2967699, FT ECO:0000269|PubMed:3042023" FT CHAIN 2..212 FT /note="Troponin I, cardiac muscle" FT /id="PRO_0000186149" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 34..81 FT /note="Involved in binding TNC" FT REGION 131..151 FT /note="Involved in binding TNC and actin" FT COMPBIAS 1..11 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 82 FT /note="Involved in TNI-TNT interactions" FT SITE 99 FT /note="Involved in TNI-TNT interactions" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:3042023" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 24 FT /note="Phosphoserine; by PKA and PKD/PRKD1" FT /evidence="ECO:0000250|UniProtKB:P02646" FT MOD_RES 25 FT /note="Phosphoserine; by PKA and PKD/PRKD1" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 28 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 33 FT /note="Phosphothreonine; by STK4/MST1" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 44 FT /note="Phosphoserine; by PKC/PRKCE" FT /evidence="ECO:0000250|UniProtKB:P48787" FT MOD_RES 46 FT /note="Phosphoserine; by PKC/PRKCE" FT /evidence="ECO:0000250|UniProtKB:P48787" FT MOD_RES 53 FT /note="Phosphothreonine; by STK4/MST1" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 80 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 145 FT /note="Phosphothreonine; by STK4/MST1" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 152 FT /note="Phosphoserine; by PAK3" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 183 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P19429" FT MOD_RES 201 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19429" FT CONFLICT 17 FT /note="P -> M (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 212 AA; 24054 MW; B4B15DCCA7BA2B5E CRC64; MADRSGGSTA GDTVPAPPPV RRRSSANYRA YATEPHAKKK SKISASRKLQ LKTLMLQIAK QELEREAEER RGEKGRALST RCQPLELAGL GFAELQDLCR QLHARVDKVD EERYDVEAKV TKNITEIADL NQKIFDLRGK FKRPTLRRVR ISADAMMQAL LGARAKETLD LRAHLKQVKK EDTEKENREV GDWRKNIDAL SGMEGRKKKF EG //