TNNI3_RAT
ID TNNI3_RAT Reviewed; 211 AA.
AC P23693; Q4PP23;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Troponin I, cardiac muscle;
DE AltName: Full=Cardiac troponin I;
GN Name=Tnni3; Synonyms=Ctni, Tni;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1988058; DOI=10.1021/bi00217a018;
RA Murphy A.M., Jones L. II, Sims H.F., Strauss A.W.;
RT "Molecular cloning of rat cardiac troponin I and analysis of troponin I
RT isoform expression in developing rat heart.";
RL Biochemistry 30:707-712(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1935696; DOI=10.1242/dev.112.4.1041;
RA Ausoni S., de Nardi C., Moretti P., Gorza L., Schiaffino S.;
RT "Developmental expression of rat cardiac troponin I mRNA.";
RL Development 112:1041-1051(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1886137; DOI=10.1016/0022-2828(91)90050-v;
RA Martin A.F., Orlowski J.;
RT "Molecular cloning and developmental expression of the rat cardiac-specific
RT isoform of troponin I.";
RL J. Mol. Cell. Cardiol. 23:583-588(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9065755; DOI=10.1042/bj3220393;
RA Murphy A.M., Thompson W.R., Peng L.F., Jones L. II;
RT "Regulation of the rat cardiac troponin I gene by the transcription factor
RT GATA-4.";
RL Biochem. J. 322:393-401(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart muscle;
RA Chandra M., Tschirgi M.L.;
RT "Troponin T regulates low-frequency cardiac muscle mechano-dynamics.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH TRIM63.
RX PubMed=15601779; DOI=10.1073/pnas.0404341102;
RA Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C.;
RT "Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that
RT degrades cardiac troponin I.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-200, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- INTERACTION:
CC P23693; Q5VU43-11: PDE4DIP; Xeno; NbExp=2; IntAct=EBI-10817583, EBI-10769071;
CC -!- PTM: Phosphorylated at Ser-23 and Ser-24 by PRKD1; phosphorylation
CC reduces myofilament calcium sensitivity. Phosphorylated preferentially
CC at Thr-32. Phosphorylation by STK4/MST1 alters its binding affinity to
CC TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylated at Ser-43
CC and Ser-45 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; M57679; AAA63504.1; -; mRNA.
DR EMBL; X58499; CAA41402.1; -; mRNA.
DR EMBL; M92074; AAA42294.1; -; mRNA.
DR EMBL; U77354; AAB52234.1; -; Genomic_DNA.
DR EMBL; DQ062462; AAY63993.1; -; mRNA.
DR PIR; A60124; A60124.
DR PIR; I56441; I56441.
DR RefSeq; NP_058840.1; NM_017144.2.
DR AlphaFoldDB; P23693; -.
DR SMR; P23693; -.
DR BioGRID; 247923; 2.
DR IntAct; P23693; 1.
DR STRING; 10116.ENSRNOP00000024640; -.
DR iPTMnet; P23693; -.
DR PhosphoSitePlus; P23693; -.
DR PaxDb; P23693; -.
DR PRIDE; P23693; -.
DR Ensembl; ENSRNOT00000024640; ENSRNOP00000024640; ENSRNOG00000018250.
DR GeneID; 29248; -.
DR KEGG; rno:29248; -.
DR UCSC; RGD:62052; rat.
DR CTD; 7137; -.
DR RGD; 62052; Tnni3.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR HOGENOM; CLU_098686_1_0_1; -.
DR InParanoid; P23693; -.
DR OMA; CKEIHQK; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; P23693; -.
DR TreeFam; TF313374; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:P23693; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018250; Expressed in heart and 17 other tissues.
DR Genevisible; P23693; RN.
DR GO; GO:0097512; C:cardiac myofibril; ISO:RGD.
DR GO; GO:1990584; C:cardiac Troponin complex; ISO:RGD.
DR GO; GO:0043292; C:contractile fiber; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030016; C:myofibril; IDA:RGD.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0005861; C:troponin complex; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030172; F:troponin C binding; ISO:RGD.
DR GO; GO:0031014; F:troponin T binding; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; IDA:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISO:RGD.
DR GO; GO:0006937; P:regulation of muscle contraction; ISO:RGD.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:RGD.
DR GO; GO:0001980; P:regulation of systemic arterial blood pressure by ischemic conditions; ISO:RGD.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
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; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08057"
FT CHAIN 2..211
FT /note="Troponin I, cardiac muscle"
FT /id="PRO_0000186155"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..80
FT /note="Involved in binding TNC"
FT REGION 130..151
FT /note="Involved in binding TNC and actin"
FT SITE 81
FT /note="Involved in TNI-TNT interactions"
FT SITE 98
FT /note="Involved in TNI-TNT interactions"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P08057"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 23
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P02646"
FT MOD_RES 24
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 27
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 32
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 43
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 45
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000250|UniProtKB:P48787"
FT MOD_RES 52
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 130
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 144
FT /note="Phosphothreonine; by STK4/MST1"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 151
FT /note="Phosphoserine; by PAK3"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19429"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 8
FT /note="A -> S (in Ref. 3; AAA42294)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="I -> T (in Ref. 3; AAA42294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 24160 MW; 17586B0FDB682B4C CRC64;
MADESSDAAG EPQPAPAPVR RRSSANYRAY ATEPHAKKKS KISASRKLQL KTLMLQIAKQ
EMEREAEERR GEKGRVLSTR CQPLVLDGLG FEELQDLCRQ LHARVDKVDE ERYDVEAKVT
KNITEIADLT QKIYDLRGKF KRPTLRRVRI SADAMMQALL GTRAKESLDL RAHLKQVKKE
DIEKENREVG DWRKNIDALS GMEGRKKKFE G
