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Troponin I, cardiac muscle (Cardiac troponin I)

 TNNI3_RAT               Reviewed;         211 AA.
P23693; Q4PP23;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 116.
RecName: Full=Troponin I, cardiac muscle;
AltName: Full=Cardiac troponin I;
Name=Tnni3; Synonyms=Ctni, Tni;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1988058; DOI=10.1021/bi00217a018;
Murphy A.M., Jones L. II, Sims H.F., Strauss A.W.;
"Molecular cloning of rat cardiac troponin I and analysis of troponin
I isoform expression in developing rat heart.";
Biochemistry 30:707-712(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1935696;
Ausoni S., de Nardi C., Moretti P., Gorza L., Schiaffino S.;
"Developmental expression of rat cardiac troponin I mRNA.";
Development 112:1041-1051(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1886137; DOI=10.1016/0022-2828(91)90050-V;
Martin A.F., Orlowski J.;
"Molecular cloning and developmental expression of the rat cardiac-
specific isoform of troponin I.";
J. Mol. Cell. Cardiol. 23:583-588(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9065755; DOI=10.1042/bj3220393;
Murphy A.M., Thompson W.R., Peng L.F., Jones L. II;
"Regulation of the rat cardiac troponin I gene by the transcription
factor GATA-4.";
Biochem. J. 322:393-401(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Heart muscle;
Chandra M., Tschirgi M.L.;
"Troponin T regulates low-frequency cardiac muscle mechano-dynamics.";
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH TRIM63.
PubMed=15601779; DOI=10.1073/pnas.0404341102;
Kedar V., McDonough H., Arya R., Li H.-H., Rockman H.A., Patterson C.;
"Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that
degrades cardiac troponin I.";
Proc. Natl. Acad. Sci. U.S.A. 101:18135-18140(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-200, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Troponin I is the inhibitory subunit of troponin, the
thin filament regulatory complex which confers calcium-sensitivity
to striated muscle actomyosin ATPase activity.
-!- SUBUNIT: Interacts with TRIM63 (By similarity). Binds to actin and
tropomyosin. Interacts with STK4/MST1 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q5VU43-11:PDE4DIP (xeno); NbExp=2; IntAct=EBI-10817583, EBI-10769071;
-!- PTM: 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).
Phosphorylated at Ser-43 and Ser-45 by PRKCE; phosphorylation
increases myocardium contractile dysfunction (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M57679; AAA63504.1; -; mRNA.
EMBL; X58499; CAA41402.1; -; mRNA.
EMBL; M92074; AAA42294.1; -; mRNA.
EMBL; U77354; AAB52234.1; -; Genomic_DNA.
EMBL; DQ062462; AAY63993.1; -; mRNA.
PIR; A60124; A60124.
PIR; I56441; I56441.
RefSeq; NP_058840.1; NM_017144.2.
UniGene; Rn.64141; -.
ProteinModelPortal; P23693; -.
SMR; P23693; -.
BioGrid; 247923; 1.
IntAct; P23693; 1.
STRING; 10116.ENSRNOP00000024640; -.
iPTMnet; P23693; -.
PhosphoSitePlus; P23693; -.
PaxDb; P23693; -.
PRIDE; P23693; -.
Ensembl; ENSRNOT00000024640; ENSRNOP00000024640; ENSRNOG00000018250.
GeneID; 29248; -.
KEGG; rno:29248; -.
UCSC; RGD:62052; rat.
CTD; 7137; -.
RGD; 62052; Tnni3.
eggNOG; KOG3977; Eukaryota.
eggNOG; ENOG410Y9IX; LUCA.
GeneTree; ENSGT00390000002746; -.
HOGENOM; HOG000293300; -.
HOVERGEN; HBG052737; -.
InParanoid; P23693; -.
KO; K12044; -.
OMA; KMFDTGG; -.
OrthoDB; EOG091G0NOD; -.
PhylomeDB; P23693; -.
TreeFam; TF313374; -.
Reactome; R-RNO-390522; Striated Muscle Contraction.
Reactome; R-RNO-5578775; Ion homeostasis.
PRO; PR:P23693; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000018250; -.
Genevisible; P23693; RN.
GO; GO:0097512; C:cardiac myofibril; ISO:RGD.
GO; GO:1990584; C:cardiac Troponin complex; ISO:RGD.
GO; GO:0043292; C:contractile fiber; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030016; C:myofibril; IDA:RGD.
GO; GO:0030017; C:sarcomere; IDA:MGI.
GO; GO:0005861; C:troponin complex; ISO:RGD.
GO; GO:0003779; F:actin binding; ISO:RGD.
GO; GO:0051015; F:actin filament binding; ISO:RGD.
GO; GO:0019855; F:calcium channel inhibitor activity; ISO:RGD.
GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0030172; F:troponin C binding; ISO:RGD.
GO; GO:0031014; F:troponin T binding; ISO:RGD.
GO; GO:0060048; P:cardiac muscle contraction; IDA:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
GO; GO:0060047; P:heart contraction; ISO:RGD.
GO; GO:0007507; P:heart development; ISO:RGD.
GO; GO:0032780; P:negative regulation of ATPase activity; ISO:RGD.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISO:RGD.
GO; GO:0006937; P:regulation of muscle contraction; ISO:RGD.
GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:RGD.
GO; GO:0001980; P:regulation of systemic arterial blood pressure by ischemic conditions; ISO:RGD.
GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
GO; GO:0001570; P:vasculogenesis; ISO:RGD.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:RGD.
InterPro; IPR001978; Troponin.
InterPro; IPR021666; Troponin-I_N.
Pfam; PF00992; Troponin; 1.
Pfam; PF11636; Troponin-I_N; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Calcium; Complete proteome; Metal-binding;
Muscle protein; Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P08057}.
CHAIN 2 211 Troponin I, cardiac muscle.
/FTId=PRO_0000186155.
CA_BIND 138 149 {ECO:0000250}.
REGION 33 80 Involved in binding TNC.
REGION 130 151 Involved in binding TNC and actin.
SITE 81 81 Involved in TNI-TNT interactions.
SITE 98 98 Involved in TNI-TNT interactions.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P08057}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 23 23 Phosphoserine; by PKA and PKD/PRKD1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 24 24 Phosphoserine; by PKA and PKD/PRKD1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 27 27 Phosphotyrosine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 32 32 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 43 43 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P48787}.
MOD_RES 45 45 Phosphoserine; by PKC/PRKCE.
{ECO:0000250|UniProtKB:P48787}.
MOD_RES 52 52 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 79 79 Phosphothreonine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 130 130 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 144 144 Phosphothreonine; by STK4/MST1.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 151 151 Phosphoserine; by PAK3.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000250|UniProtKB:P19429}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CONFLICT 8 8 A -> S (in Ref. 3; AAA42294).
{ECO:0000305}.
CONFLICT 182 182 I -> T (in Ref. 3; AAA42294).
{ECO:0000305}.
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


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