TNNT2_RAT
ID TNNT2_RAT Reviewed; 299 AA.
AC P50753;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Troponin T, cardiac muscle;
DE Short=TnTc;
DE AltName: Full=Cardiac muscle troponin T;
DE Short=cTnT;
GN Name=Tnnt2;
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=2760070; DOI=10.1016/s0021-9258(18)71702-x;
RA Jin J.-P., Lin J.C.;
RT "Isolation and characterization of cDNA clones encoding embryonic and adult
RT isoforms of rat cardiac troponin T.";
RL J. Biol. Chem. 264:14471-14477(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1433301; DOI=10.1016/0022-2836(92)90540-z;
RA Jin J.-P., Huang Q.-Q., Yeh H.-I., Lin J.J.-C.;
RT "Complete nucleotide sequence and structural organization of rat cardiac
RT troponin T gene. A single gene generates embryonic and adult isoforms via
RT developmentally regulated alternative splicing.";
RL J. Mol. Biol. 227:1269-1276(1992).
RN [3]
RP PHOSPHORYLATION AT THR-214 BY RAF1.
RX PubMed=19381846; DOI=10.1007/s10974-009-9176-y;
RA Pfleiderer P., Sumandea M.P., Rybin V.O., Wang C., Steinberg S.F.;
RT "Raf-1: a novel cardiac troponin T kinase.";
RL J. Muscle Res. Cell Motil. 30:67-72(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP 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 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=2;
CC Name=1; Synonyms=Embryonic;
CC IsoId=P50753-1; Sequence=Displayed;
CC Name=2; Synonyms=Adult;
CC IsoId=P50753-2; Sequence=VSP_006657;
CC -!- PTM: Phosphorylation at Thr-214 by PRKCA induces significant reduction
CC in myofilament calcium sensitivity and actomyosin ATPase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR EMBL; M26051; AAA42296.1; -; mRNA.
DR EMBL; M26052; AAA42297.1; -; mRNA.
DR EMBL; M80829; AAB07676.1; -; Genomic_DNA.
DR PIR; A44781; A44781.
DR PIR; B44781; B44781.
DR PIR; S30443; S30443.
DR RefSeq; NP_036808.1; NM_012676.1. [P50753-1]
DR RefSeq; XP_006249900.1; XM_006249838.2. [P50753-2]
DR RefSeq; XP_008767759.1; XM_008769537.2. [P50753-1]
DR RefSeq; XP_017454159.1; XM_017598670.1. [P50753-2]
DR AlphaFoldDB; P50753; -.
DR SMR; P50753; -.
DR BioGRID; 246955; 2.
DR STRING; 10116.ENSRNOP00000049297; -.
DR iPTMnet; P50753; -.
DR PhosphoSitePlus; P50753; -.
DR PaxDb; P50753; -.
DR PRIDE; P50753; -.
DR GeneID; 24837; -.
DR KEGG; rno:24837; -.
DR UCSC; RGD:3882; rat. [P50753-1]
DR CTD; 7139; -.
DR RGD; 3882; Tnnt2.
DR VEuPathDB; HostDB:ENSRNOG00000033734; -.
DR eggNOG; KOG3634; Eukaryota.
DR InParanoid; P50753; -.
DR OMA; RIXEERA; -.
DR OrthoDB; 1480247at2759; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P50753; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000033734; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; P50753; baseline and differential.
DR Genevisible; P50753; RN.
DR GO; GO:0097512; C:cardiac myofibril; ISO:RGD.
DR GO; GO:1990584; C:cardiac Troponin complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030016; C:myofibril; IDA:RGD.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0005865; C:striated muscle thin filament; ISS:UniProtKB.
DR GO; GO:0005861; C:troponin complex; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
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; IPI:RGD.
DR GO; GO:0051764; P:actin crosslink formation; IDA:RGD.
DR GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; IDA:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IMP:RGD.
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; ISS:UniProtKB.
DR GO; GO:0006937; P:regulation of muscle contraction; IDA:RGD.
DR GO; GO:0032972; P:regulation of muscle filament sliding speed; IMP:BHF-UCL.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:UniProtKB.
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 Acetylation; Alternative splicing; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09741"
FT CHAIN 2..299
FT /note="Troponin T, cardiac muscle"
FT /id="PRO_0000186176"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
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"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 205
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 209
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P50752"
FT MOD_RES 214
FT /note="Phosphothreonine; by PKC/PRKCA and RAF1"
FT /evidence="ECO:0000305|PubMed:19381846"
FT MOD_RES 295
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT VAR_SEQ 18..27
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006657"
FT CONFLICT 205
FT /note="T -> A (in Ref. 2; AAB07676)"
FT /evidence="ECO:0000305"
FT MOD_RES P50753-2:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 299 AA; 35730 MW; B6042E2AD53B30B5 CRC64;
MSDAEEEVVE YEEEQEEEDW SEEEEDEQEE AVEEEDGEAE PDPEGEAEAE EDKAEEVGPD
EEARDAEDGP VEDSKPKPSR LFMPNLVPPK IPDGERVDFD DIHRKRMEKD LNELQTLIEA
HFENRKKEEE ELISLKDRIE KRRAERAEQQ RIRNEREKER QNRLAEERAR REEEENRRKA
EDEARKKKAL SNMMHFGGYI QKAQTERKSG KRQTEREKKK KILAERRKVL AIDHLNEDQL
REKAKELWQS IHNLEAEKFD LQEKFKQQKY EINVLRNRIN DNQKVSKTRG KAKVTGRWK
