ID   TNNI2_RAT               Reviewed;         182 AA.
AC   P27768;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Troponin I, fast skeletal muscle;
DE   AltName: Full=Troponin I, fast-twitch isoform;
GN   Name=Tnni2; Synonyms=Trp1;
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].
RA   Gravel M., Hastings K.E.M.;
RT   "Sequence of a cDNA encoding the rat fast skeletal muscle isoform of
RT   troponin I.";
RL   Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, 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; M73701; AAA42149.1; -; mRNA.
DR   RefSeq; NP_058881.1; NM_017185.1.
DR   AlphaFoldDB; P27768; -.
DR   BMRB; P27768; -.
DR   SMR; P27768; -.
DR   STRING; 10116.ENSRNOP00000068190; -.
DR   CarbonylDB; P27768; -.
DR   iPTMnet; P27768; -.
DR   PhosphoSitePlus; P27768; -.
DR   PaxDb; P27768; -.
DR   Ensembl; ENSRNOT00000027487; ENSRNOP00000027487; ENSRNOG00000020276.
DR   GeneID; 29389; -.
DR   KEGG; rno:29389; -.
DR   UCSC; RGD:62050; rat.
DR   CTD; 7136; -.
DR   RGD; 62050; Tnni2.
DR   eggNOG; KOG3977; Eukaryota.
DR   GeneTree; ENSGT01030000234588; -.
DR   InParanoid; P27768; -.
DR   OMA; KRHRAIT; -.
DR   OrthoDB; 1566919at2759; -.
DR   PhylomeDB; P27768; -.
DR   Reactome; R-RNO-390522; Striated Muscle Contraction.
DR   PRO; PR:P27768; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000020276; Expressed in skeletal muscle tissue and 16 other tissues.
DR   ExpressionAtlas; P27768; baseline and differential.
DR   Genevisible; P27768; RN.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0005861; C:troponin complex; IDA:RGD.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0031014; F:troponin T binding; ISO:RGD.
DR   GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0006937; P:regulation of muscle contraction; IDA:RGD.
DR   GO; GO:0003009; P:skeletal muscle contraction; 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; Muscle protein; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02643"
FT   CHAIN           2..182
FT                   /note="Troponin I, fast skeletal muscle"
FT                   /id="PRO_0000186146"
FT   REGION          2..48
FT                   /note="Involved in binding TNC"
FT   REGION          29..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..117
FT                   /note="Involved in binding TNC and actin"
FT   COMPBIAS        29..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0000250|UniProtKB:P02643"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02643"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   182 AA;  21328 MW;  6640081F44AA0EDA CRC64;
     MGDEEKRNRA ITARRQHLKS VMLQIAATEL EKEESRRESE KQNYLSEHCP PLHIPGSMSE
     VQELCKQLHA KIDAAEEEKY DMEVKVQKSS KELEDMNQKL FDLRGKFKRP PLRRVRMSAD
     AMLKALLGSK HKVCMDLRAN LKQVKKEDTE KERDLRDVGD WRKNIEEKSG MEGRKKMFES
     ES