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   27-MAR-2024, entry version 119.
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; 2.
DR   STRING; 10116.ENSRNOP00000067933; -.
DR   iPTMnet; P13413; -.
DR   PhosphoSitePlus; P13413; -.
DR   PaxDb; 10116-ENSRNOP00000067933; -.
DR   GeneID; 29388; -.
DR   KEGG; rno:29388; -.
DR   UCSC; RGD:621765; rat.
DR   AGR; RGD:621765; -.
DR   CTD; 7135; -.
DR   RGD; 621765; Tnni1.
DR   eggNOG; KOG3977; Eukaryota.
DR   InParanoid; P13413; -.
DR   OrthoDB; 2882372at2759; -.
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:0060048; P:cardiac muscle contraction; IBA:GO_Central.
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   Gene3D; 6.10.250.180; -; 1.
DR   InterPro; IPR001978; Troponin.
DR   InterPro; IPR038077; Troponin_sf.
DR   PANTHER; PTHR13738; TROPONIN I; 1.
DR   PANTHER; PTHR13738:SF9; TROPONIN I, SLOW SKELETAL MUSCLE; 1.
DR   Pfam; PF00992; Troponin; 1.
DR   SUPFAM; SSF90250; Troponin coil-coiled subunits; 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
//