TNNI3_MOUSE
ID TNNI3_MOUSE Reviewed; 211 AA.
AC P48787;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Troponin I, cardiac muscle;
DE AltName: Full=Cardiac troponin I;
GN Name=Tnni3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8276817; DOI=10.1016/s0021-9258(17)42354-4;
RA Ausoni S., Campione M., Picard A., Moretti P., Vittadello M., de Nardi C.,
RA Schiaffino S.;
RT "Structure and regulation of the mouse cardiac troponin I gene.";
RL J. Biol. Chem. 269:339-346(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Heart;
RX PubMed=8195157; DOI=10.1016/s0021-9258(17)36593-6;
RA Guo X., Wattanapermpool J., Palmiter K.A., Murphy A.M., Solaro R.J.;
RT "Mutagenesis of cardiac troponin I. Role of the unique NH2-terminal peptide
RT in myofilament activation.";
RL J. Biol. Chem. 269:15210-15216(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION AT SER-43 AND SER-45.
RX PubMed=16445938; DOI=10.1016/j.yjmcc.2005.12.009;
RA Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J., Buttrick P.M.,
RA Goldspink P.H.;
RT "Partial replacement of cardiac troponin I with a non-phosphorylatable
RT mutant at serines 43/45 attenuates the contractile dysfunction associated
RT with PKCepsilon phosphorylation.";
RL J. Mol. Cell. Cardiol. 40:465-473(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP STRUCTURE BY NMR OF 1-32, AND PHOSPHORYLATION AT SER-23 AND SER-24.
RX PubMed=17854829; DOI=10.1016/j.jmb.2007.08.035;
RA Howarth J.W., Meller J., Solaro R.J., Trewhella J., Rosevear P.R.;
RT "Phosphorylation-dependent conformational transition of the cardiac
RT specific N-extension of troponin I in cardiac troponin.";
RL J. Mol. Biol. 373:706-722(2007).
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-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) (By similarity).
CC Phosphorylated at Ser-43 and Ser-45 by PRKCE; phosphorylation increases
CC myocardium contractile dysfunction. {ECO:0000250,
CC ECO:0000269|PubMed:16445938, ECO:0000269|PubMed:17854829}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; Z22784; CAA80459.1; -; Genomic_DNA.
DR EMBL; U09181; AAA19657.1; -; mRNA.
DR EMBL; BC061171; AAH61171.1; -; mRNA.
DR CCDS; CCDS39736.1; -.
DR PIR; A53805; A53805.
DR RefSeq; NP_033432.1; NM_009406.4.
DR PDB; 2JPW; NMR; -; A=1-32.
DR PDB; 6KLT; EM; 12.00 A; C=49-163.
DR PDB; 6KLU; EM; 12.00 A; C=50-167.
DR PDBsum; 2JPW; -.
DR PDBsum; 6KLT; -.
DR PDBsum; 6KLU; -.
DR AlphaFoldDB; P48787; -.
DR SMR; P48787; -.
DR BioGRID; 204266; 4.
DR ComplexPortal; CPX-16; Cardiac Troponin complex.
DR IntAct; P48787; 5.
DR MINT; P48787; -.
DR STRING; 10090.ENSMUSP00000096458; -.
DR iPTMnet; P48787; -.
DR PhosphoSitePlus; P48787; -.
DR PaxDb; P48787; -.
DR PRIDE; P48787; -.
DR ProteomicsDB; 259143; -.
DR Antibodypedia; 4354; 2575 antibodies from 52 providers.
DR DNASU; 21954; -.
DR Ensembl; ENSMUST00000098859; ENSMUSP00000096458; ENSMUSG00000035458.
DR GeneID; 21954; -.
DR KEGG; mmu:21954; -.
DR UCSC; uc009exv.1; mouse.
DR CTD; 7137; -.
DR MGI; MGI:98783; Tnni3.
DR VEuPathDB; HostDB:ENSMUSG00000035458; -.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR HOGENOM; CLU_098686_1_0_1; -.
DR InParanoid; P48787; -.
DR OMA; CKEIHQK; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; P48787; -.
DR TreeFam; TF313374; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR BioGRID-ORCS; 21954; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Tnni3; mouse.
DR EvolutionaryTrace; P48787; -.
DR PRO; PR:P48787; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P48787; protein.
DR Bgee; ENSMUSG00000035458; Expressed in myocardium and 110 other tissues.
DR ExpressionAtlas; P48787; baseline and differential.
DR Genevisible; P48787; MM.
DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
DR GO; GO:1990584; C:cardiac Troponin complex; ISO:MGI.
DR GO; GO:0043292; C:contractile fiber; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030016; C:myofibril; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0005861; C:troponin complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISO:MGI.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030172; F:troponin C binding; ISO:MGI.
DR GO; GO:0031014; F:troponin T binding; ISO:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR GO; GO:0060047; P:heart contraction; ISO:MGI.
DR GO; GO:0007507; P:heart development; IDA:MGI.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISO:MGI.
DR GO; GO:0006937; P:regulation of muscle contraction; IDA:MGI.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISO:MGI.
DR GO; GO:0001980; P:regulation of systemic arterial blood pressure by ischemic conditions; IMP:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0006941; P:striated muscle contraction; IDA:MGI.
DR GO; GO:0001570; P:vasculogenesis; IDA:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISO:MGI.
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 3D-structure; 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_0000186153"
FT REGION 1..24
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:0000250|UniProtKB:P19429"
FT MOD_RES 23
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:17854829"
FT MOD_RES 24
FT /note="Phosphoserine; by PKA and PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:17854829"
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:0000269|PubMed:16445938"
FT MOD_RES 45
FT /note="Phosphoserine; by PKC/PRKCE"
FT /evidence="ECO:0000269|PubMed:16445938"
FT MOD_RES 52
FT /note="Phosphothreonine; by STK4/MST1"
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"
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:21183079"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:2JPW"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:2JPW"
SQ SEQUENCE 211 AA; 24259 MW; FB886B0E87B8D49D CRC64;
MADESSDAAG EPQPAPAPVR RRSSANYRAY ATEPHAKKKS KISASRKLQL KTLMLQIAKQ
EMEREAEERR GEKGRVLRTR CQPLELDGLG FEELQDLCRQ LHARVDKVDE ERYDVEAKVT
KNITEIADLT QKIYDLRGKF KRPTLRRVRI SADAMMQALL GTRAKESLDL RAHLKQVKKE
DIEKENREVG DWRKNIDALS GMEGRKKKFE G
