TNNI1_MOUSE
ID TNNI1_MOUSE Reviewed; 187 AA.
AC Q9WUZ5;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Troponin I, slow skeletal muscle;
DE AltName: Full=Troponin I, slow-twitch isoform;
GN Name=Tnni1;
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 [MRNA].
RC TISSUE=Skeletal muscle;
RA Barton P.J.R.;
RT "Cloning and chromosomal distribution of the mouse troponin gene
RT families.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Lung;
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).
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; AJ242874; CAB48403.1; -; mRNA.
DR EMBL; AK012258; BAB28123.1; -; mRNA.
DR EMBL; BC023170; AAH23170.1; -; mRNA.
DR CCDS; CCDS48374.1; -.
DR RefSeq; NP_001106173.1; NM_001112702.1.
DR RefSeq; NP_067442.1; NM_021467.5.
DR RefSeq; XP_006529445.1; XM_006529382.3.
DR RefSeq; XP_011246276.1; XM_011247974.2.
DR AlphaFoldDB; Q9WUZ5; -.
DR SMR; Q9WUZ5; -.
DR STRING; 10090.ENSMUSP00000122925; -.
DR iPTMnet; Q9WUZ5; -.
DR PhosphoSitePlus; Q9WUZ5; -.
DR MaxQB; Q9WUZ5; -.
DR PaxDb; Q9WUZ5; -.
DR PRIDE; Q9WUZ5; -.
DR ProteomicsDB; 259479; -.
DR Antibodypedia; 3993; 395 antibodies from 30 providers.
DR DNASU; 21952; -.
DR Ensembl; ENSMUST00000148201; ENSMUSP00000123509; ENSMUSG00000026418.
DR Ensembl; ENSMUST00000152075; ENSMUSP00000121343; ENSMUSG00000026418.
DR Ensembl; ENSMUST00000152208; ENSMUSP00000121966; ENSMUSG00000026418.
DR Ensembl; ENSMUST00000154463; ENSMUSP00000122925; ENSMUSG00000026418.
DR GeneID; 21952; -.
DR KEGG; mmu:21952; -.
DR UCSC; uc033flo.1; mouse.
DR CTD; 7135; -.
DR MGI; MGI:105073; Tnni1.
DR VEuPathDB; HostDB:ENSMUSG00000026418; -.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR InParanoid; Q9WUZ5; -.
DR OMA; CIHNTRE; -.
DR OrthoDB; 1566919at2759; -.
DR PhylomeDB; Q9WUZ5; -.
DR TreeFam; TF313374; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 21952; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tnni1; mouse.
DR PRO; PR:Q9WUZ5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9WUZ5; protein.
DR Bgee; ENSMUSG00000026418; Expressed in soleus muscle and 115 other tissues.
DR ExpressionAtlas; Q9WUZ5; baseline and differential.
DR Genevisible; Q9WUZ5; MM.
DR GO; GO:0005861; C:troponin complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
DR GO; GO:0014883; P:transition between fast and slow fiber; IDA:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
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:P02645"
FT CHAIN 2..187
FT /note="Troponin I, slow skeletal muscle"
FT /id="PRO_0000186140"
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:21183079"
SQ SEQUENCE 187 AA; 21698 MW; 69B4BA39D0F471D4 CRC64;
MPEVERKSKI TASRKLMLKS LMLAKAKECW EQEHEEREAE KVRYLSERIP TLQTRGLSLS
ALQDLCRELH AKVEVVDEER YDIEAKCLHN TREIKDLKLK VLDLRGKFKR PPLRRVRVSA
DAMLRALLGS KHKVSMDLRA NLKSVKKEDT EKERPVEVGD WRKNVEAMSG MEGRKKMFDA
AKSPTSQ
