TNNT2_MOUSE
ID TNNT2_MOUSE Reviewed; 301 AA.
AC P50752; Q64360; Q64377;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Troponin T, cardiac muscle;
DE Short=TnTc;
DE AltName: Full=Cardiac muscle troponin T;
DE Short=cTnT;
GN Name=Tnnt2;
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 (ISOFORMS A1; A2; A3B AND EMBRYONIC).
RC TISSUE=Heart;
RA Jin J.-P., Wang J., Zhang J.;
RT "Expression of mouse cardiac troponin T isoforms: characterization of a
RT large sample of independent cDNA clones.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION AT THR-207; SER-211; THR-216 AND THR-297.
RX PubMed=12832403; DOI=10.1074/jbc.m306325200;
RA Sumandea M.P., Pyle W.G., Kobayashi T., de Tombe P.P., Solaro R.J.;
RT "Identification of a functionally critical protein kinase C phosphorylation
RT residue of cardiac troponin T.";
RL J. Biol. Chem. 278:35135-35144(2003).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 T is the tropomyosin-binding subunit of troponin,
CC the thin filament regulatory complex which confers calcium-sensitivity
CC to striated muscle actomyosin ATPase activity.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Embryonic; Synonyms=EA;
CC IsoId=P50752-1; Sequence=Displayed;
CC Name=A1;
CC IsoId=P50752-4; Sequence=VSP_007913;
CC Name=A2;
CC IsoId=P50752-3; Sequence=VSP_006649;
CC Name=A3B;
CC IsoId=P50752-2; Sequence=VSP_006649, VSP_006650;
CC -!- PTM: Phosphorylation at Thr-216 by PRKCA induces significant reduction
CC in myofilament calcium sensitivity and actomyosin ATPase activity.
CC {ECO:0000269|PubMed:12832403}.
CC -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR EMBL; L47549; AAA85345.1; -; mRNA.
DR EMBL; L47550; AAA85346.1; -; mRNA.
DR EMBL; L47551; AAA85347.1; -; mRNA.
DR EMBL; L47552; AAA85348.1; -; mRNA.
DR EMBL; L47553; AAA85349.1; -; mRNA.
DR EMBL; L47570; AAA85350.1; -; Genomic_DNA.
DR EMBL; L47599; AAA85351.1; -; mRNA.
DR EMBL; L47600; AAA85352.1; -; mRNA.
DR CCDS; CCDS48376.1; -. [P50752-4]
DR CCDS; CCDS48377.1; -. [P50752-1]
DR CCDS; CCDS48378.1; -. [P50752-3]
DR RefSeq; NP_001123648.1; NM_001130176.1. [P50752-1]
DR RefSeq; NP_001123650.1; NM_001130178.2. [P50752-4]
DR RefSeq; NP_001123651.4; NM_001130179.2.
DR RefSeq; NP_001123652.1; NM_001130180.2. [P50752-3]
DR RefSeq; NP_001123653.4; NM_001130181.2.
DR RefSeq; NP_035749.1; NM_011619.3. [P50752-2]
DR RefSeq; XP_006529456.1; XM_006529393.3. [P50752-1]
DR RefSeq; XP_006529457.1; XM_006529394.3. [P50752-1]
DR RefSeq; XP_006529458.1; XM_006529395.3. [P50752-3]
DR PDB; 6KLT; EM; 12.00 A; B=212-282.
DR PDB; 6KLU; EM; 12.00 A; B=212-285.
DR PDBsum; 6KLT; -.
DR PDBsum; 6KLU; -.
DR AlphaFoldDB; P50752; -.
DR SMR; P50752; -.
DR ComplexPortal; CPX-16; Cardiac Troponin complex.
DR IntAct; P50752; 3.
DR MINT; P50752; -.
DR STRING; 10090.ENSMUSP00000107717; -.
DR iPTMnet; P50752; -.
DR PhosphoSitePlus; P50752; -.
DR CPTAC; non-CPTAC-3675; -.
DR MaxQB; P50752; -.
DR PaxDb; P50752; -.
DR PRIDE; P50752; -.
DR ProteomicsDB; 259280; -. [P50752-1]
DR ProteomicsDB; 259281; -. [P50752-4]
DR ProteomicsDB; 259282; -. [P50752-3]
DR ProteomicsDB; 259283; -. [P50752-2]
DR Antibodypedia; 4204; 1227 antibodies from 45 providers.
DR DNASU; 21956; -.
DR Ensembl; ENSMUST00000027671; ENSMUSP00000027671; ENSMUSG00000026414. [P50752-3]
DR Ensembl; ENSMUST00000112087; ENSMUSP00000107717; ENSMUSG00000026414. [P50752-1]
DR Ensembl; ENSMUST00000178854; ENSMUSP00000136265; ENSMUSG00000026414. [P50752-4]
DR Ensembl; ENSMUST00000189355; ENSMUSP00000139919; ENSMUSG00000026414. [P50752-3]
DR Ensembl; ENSMUST00000189732; ENSMUSP00000139669; ENSMUSG00000026414. [P50752-4]
DR GeneID; 21956; -.
DR KEGG; mmu:21956; -.
DR UCSC; uc007ctu.3; mouse. [P50752-4]
DR UCSC; uc007ctw.3; mouse. [P50752-3]
DR UCSC; uc007ctx.3; mouse. [P50752-2]
DR UCSC; uc011wso.2; mouse. [P50752-1]
DR CTD; 7139; -.
DR MGI; MGI:104597; Tnnt2.
DR VEuPathDB; HostDB:ENSMUSG00000026414; -.
DR eggNOG; KOG3634; Eukaryota.
DR GeneTree; ENSGT00940000154709; -.
DR HOGENOM; CLU_076377_1_0_1; -.
DR InParanoid; P50752; -.
DR OrthoDB; 1480247at2759; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 21956; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Tnnt2; mouse.
DR PRO; PR:P50752; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P50752; protein.
DR Bgee; ENSMUSG00000026414; Expressed in atrioventricular valve and 195 other tissues.
DR ExpressionAtlas; P50752; baseline and differential.
DR Genevisible; P50752; MM.
DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI.
DR GO; GO:1990584; C:cardiac Troponin complex; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0016528; C:sarcoplasm; IDA:MGI.
DR GO; GO:0005865; C:striated muscle thin filament; ISS:UniProtKB.
DR GO; GO:0005861; C:troponin complex; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR GO; GO:0005523; F:tropomyosin binding; ISS:UniProtKB.
DR GO; GO:0030172; F:troponin C binding; ISS:UniProtKB.
DR GO; GO:0031013; F:troponin I binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; ISO:MGI.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0006936; P:muscle contraction; IDA:MGI.
DR GO; GO:0030049; P:muscle filament sliding; ISS:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR GO; GO:0006937; P:regulation of muscle contraction; ISO:MGI.
DR GO; GO:0032972; P:regulation of muscle filament sliding speed; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; IMP:MGI.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR027707; TNNT.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR PANTHER; PTHR11521; PTHR11521; 1.
DR Pfam; PF00992; Troponin; 2.
DR SUPFAM; SSF90250; SSF90250; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Muscle protein;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09741"
FT CHAIN 2..301
FT /note="Troponin T, cardiac muscle"
FT /id="PRO_0000186174"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..68
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P09741"
FT MOD_RES 2
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 207
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000269|PubMed:12832403"
FT MOD_RES 211
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000269|PubMed:12832403"
FT MOD_RES 216
FT /note="Phosphothreonine; by PKC/PRKCA and RAF1"
FT /evidence="ECO:0000305|PubMed:12832403"
FT MOD_RES 297
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000269|PubMed:12832403"
FT VAR_SEQ 18..27
FT /note="Missing (in isoform A2 and isoform A3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_006649"
FT VAR_SEQ 18..26
FT /note="EDWSEEEED -> AVE (in isoform A1)"
FT /evidence="ECO:0000305"
FT /id="VSP_007913"
FT VAR_SEQ 204..206
FT /note="Missing (in isoform A3B)"
FT /evidence="ECO:0000305"
FT /id="VSP_006650"
SQ SEQUENCE 301 AA; 35825 MW; 60B2185A140AF2D5 CRC64;
MSDAEEVVEE YEEEQEEEDW SEEEEDEQEE AVEEEEAGGA EPEPEGEAET EEANVEEVGP
DEEAKDAEEG PVEDTKPKPS RLFMPNLVPP KIPDGERVDF DDIHRKRVEK DLNELQTLIE
AHFENRKKEE EELISLKDRI EKRRAERAEQ QRIRNEREKE RQNRLAEERA RREEEENRRK
AEDEARKKKA LSNMMHFGGY IQKQAQTERK SGKRQTEREK KKKILAERRK ALAIDHLNED
QLREKAKELW QSIHNLEAEK FDLQEKFKQQ KYEINVLRNR INDNQKVSKT RGKAKVTGRW
K
