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Database: UniProt
Entry: A2A6K0_MOUSE
LinkDB: A2A6K0_MOUSE
Original site: A2A6K0_MOUSE 
ID   A2A6K0_MOUSE            Unreviewed;       135 AA.
AC   A2A6K0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Troponin I, fast skeletal muscle {ECO:0000256|ARBA:ARBA00039349};
DE   AltName: Full=Troponin I, fast-twitch isoform {ECO:0000256|ARBA:ARBA00042462};
DE   Flags: Fragment;
GN   Name=Tnni2 {ECO:0000313|Ensembl:ENSMUSP00000121819.2,
GN   ECO:0000313|MGI:MGI:105070};
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 {ECO:0000313|Ensembl:ENSMUSP00000121819.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000121819.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121819.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000121819.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000121819.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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       {ECO:0000256|ARBA:ARBA00001988}.
CC   -!- SUBUNIT: Binds to actin and tropomyosin.
CC       {ECO:0000256|ARBA:ARBA00038767}.
CC   -!- SIMILARITY: Belongs to the troponin I family.
CC       {ECO:0000256|ARBA:ARBA00009930}.
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DR   AlphaFoldDB; A2A6K0; -.
DR   SMR; A2A6K0; -.
DR   MaxQB; A2A6K0; -.
DR   ProteomicsDB; 351502; -.
DR   Antibodypedia; 4359; 481 antibodies from 34 providers.
DR   Ensembl; ENSMUST00000145287.8; ENSMUSP00000121819.2; ENSMUSG00000031097.16.
DR   AGR; MGI:105070; -.
DR   MGI; MGI:105070; Tnni2.
DR   VEuPathDB; HostDB:ENSMUSG00000031097; -.
DR   GeneTree; ENSGT01030000234588; -.
DR   OMA; KRHRAIT; -.
DR   ChiTaRS; Tnni2; mouse.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000031097; Expressed in digastric muscle group and 131 other cell types or tissues.
DR   ExpressionAtlas; A2A6K0; baseline and differential.
DR   GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.350; -; 1.
DR   InterPro; IPR001978; Troponin.
DR   InterPro; IPR038077; Troponin_sf.
DR   PANTHER; PTHR13738; TROPONIN I; 1.
DR   PANTHER; PTHR13738:SF15; TROPONIN I, FAST SKELETAL MUSCLE; 1.
DR   Pfam; PF00992; Troponin; 1.
DR   SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE   1: Evidence at protein level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW   Proteomics identification {ECO:0007829|MaxQB:A2A6K0,
KW   ECO:0007829|ProteomicsDB:A2A6K0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   REGION          29..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         135
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000121819.2"
SQ   SEQUENCE   135 AA;  15735 MW;  9B0FFDC89270F4AB CRC64;
     MGDEEKRNRA ITARRQHLKS VMLQIAATEL EKEESRRESE KENYLSEHCP PLHIPGSMSE
     VQELCKQLHA KIDVAEEEKY DMEVKVQKSS KELEDMNQKL FDLRGKFKRP PLRRVRMSAD
     AMLKALLGSK HKVCM
//
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