TNNI3_BOVIN
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 03-AUG-2022, entry version 130.
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}.
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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 IntAct; P08057; 1.
DR STRING; 9913.ENSBTAP00000008425; -.
DR iPTMnet; P08057; -.
DR PaxDb; P08057; -.
DR PRIDE; P08057; -.
DR GeneID; 511094; -.
DR KEGG; bta:511094; -.
DR CTD; 7137; -.
DR eggNOG; KOG3977; Eukaryota.
DR HOGENOM; CLU_098686_1_0_1; -.
DR InParanoid; P08057; -.
DR OrthoDB; 1566919at2759; -.
DR TreeFam; TF313374; -.
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:0003779; F:actin binding; IEA:UniProtKB-KW.
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 Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR021666; Troponin-I_N.
DR InterPro; IPR038077; Troponin_sf.
DR Pfam; PF00992; Troponin; 1.
DR Pfam; PF11636; Troponin-I_N; 1.
DR SUPFAM; SSF90250; SSF90250; 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 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
