TNNI1_RAT
ID TNNI1_RAT Reviewed; 187 AA.
AC P13413;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Troponin I, slow skeletal muscle;
DE AltName: Full=Troponin I, slow-twitch isoform;
GN Name=Tnni1;
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=2760067; DOI=10.1016/s0021-9258(18)71681-5;
RA Koppe R.I., Hallauer P.L., Karpati G., Hastings K.E.M.;
RT "cDNA clone and expression analysis of rodent fast and slow skeletal muscle
RT troponin I mRNAs.";
RL J. Biol. Chem. 264:14327-14333(1989).
RN [2]
RP PROTEIN SEQUENCE OF 147-152, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP 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: Binds to actin and tropomyosin.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; J04993; AAA42295.1; -; mRNA.
DR PIR; B44786; B44786.
DR RefSeq; NP_058880.1; NM_017184.1.
DR AlphaFoldDB; P13413; -.
DR SMR; P13413; -.
DR BioGRID; 248040; 1.
DR STRING; 10116.ENSRNOP00000067933; -.
DR iPTMnet; P13413; -.
DR PhosphoSitePlus; P13413; -.
DR PaxDb; P13413; -.
DR GeneID; 29388; -.
DR KEGG; rno:29388; -.
DR UCSC; RGD:621765; rat.
DR CTD; 7135; -.
DR RGD; 621765; Tnni1.
DR eggNOG; KOG3977; Eukaryota.
DR InParanoid; P13413; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; P13413; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P13413; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005861; C:troponin complex; IDA:RGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; IDA:RGD.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0014883; P:transition between fast and slow fiber; 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; IPR038077; Troponin_sf.
DR Pfam; PF00992; Troponin; 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:0000250|UniProtKB:P02645"
FT CHAIN 2..187
FT /note="Troponin I, slow skeletal muscle"
FT /id="PRO_0000186142"
FT REGION 2..48
FT /note="Involved in binding TNC"
FT REGION 97..118
FT /note="Involved in binding TNC and actin"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P02645"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 187 AA; 21724 MW; 69A62A39D0F471D4 CRC64;
MPEVERKSKI TASRKLMLKS LMLAKAKECW EQEHEEREAE KVRYLSERIP TLQTRGLSLS
ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VLDLRGKFKR PPLRRVRVSA
DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA
AKSPTLQ