TNNT3_RAT
ID TNNT3_RAT Reviewed; 259 AA.
AC P09739; P09740; Q304F4; Q4PPA0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Troponin T, fast skeletal muscle;
DE Short=TnTf;
DE AltName: Full=Fast skeletal muscle troponin T;
DE Short=fTnT;
GN Name=Tnnt3;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=3735424; DOI=10.1016/0022-2836(86)90157-9;
RA Breitbart R.E., Nadal-Ginard B.;
RT "Complete nucleotide sequence of the fast skeletal troponin T gene.
RT Alternatively spliced exons exhibit unusual interspecies divergence.";
RL J. Mol. Biol. 188:313-324(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=2986851; DOI=10.1016/0092-8674(85)90062-5;
RA Breitbart R.E., Nguyen H.T., Medford R.M., Destree A.T., Mahdavi V.,
RA Nadal-Ginard B.;
RT "Intricate combinatorial patterns of exon splicing generate multiple
RT regulated troponin T isoforms from a single gene.";
RL Cell 41:67-82(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Fast-twitch skeletal muscle;
RX PubMed=16839517; DOI=10.1016/j.abb.2006.06.008;
RA Gallon C.E., Tschirgi M.L., Chandra M.;
RT "Differences in myofilament calcium sensitivity in rat psoas fibers
RT reconstituted with troponin T isoforms containing the alpha- and beta-
RT exons.";
RL Arch. Biochem. Biophys. 456:127-134(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-78; SER-149; SER-156;
RP SER-157; SER-193 AND TYR-209, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-2 (ISOFORMS 3; 6 AND 7), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 {ECO:0000269|PubMed:16839517}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Combinatorial alternative splicing of 5 short exons in the 5'
CC region of this gene may generate up to 32 distinct N-terminal
CC isoforms. These N-terminal isoforms may be further combined with one
CC of two mutually exclusive C-terminal exons (alpha or beta) to produce
CC up to 64 distinct isoforms. For simplicity, only individual splice
CC events are explicitly described here. {ECO:0000269|PubMed:2986851,
CC ECO:0000269|PubMed:3735424};
CC Name=1; Synonyms=Beta;
CC IsoId=P09739-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=P09739-2; Sequence=VSP_006664;
CC Name=3; Synonyms=Ia-2;
CC IsoId=P09739-3; Sequence=VSP_006658;
CC Name=4; Synonyms=Ib-1;
CC IsoId=P09739-4; Sequence=VSP_006659;
CC Name=5; Synonyms=Ic-1;
CC IsoId=P09739-5; Sequence=VSP_006660;
CC Name=6; Synonyms=IIa-1;
CC IsoId=P09739-6; Sequence=VSP_006661;
CC Name=7; Synonyms=IVb;
CC IsoId=P09739-7; Sequence=VSP_006663;
CC -!- MISCELLANEOUS: [Isoform 2]: Increased calcium sensitivity of
CC myofilaments relative to isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Lacks exon 4. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Lacks exon 5. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Lacks exon 6. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Lacks exon 7. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Lacks exon 8. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR EMBL; M15202; AAA96440.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96441.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96442.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96443.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96444.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96445.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96446.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96447.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96448.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96449.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96450.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96451.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96452.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96453.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96454.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96455.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96456.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96457.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96458.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96459.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96460.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96461.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96462.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96463.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96464.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96465.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96466.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96467.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96468.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96469.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96470.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96471.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96472.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96473.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96474.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96475.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96476.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96477.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96478.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96479.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96480.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96481.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96482.1; -; Genomic_DNA.
DR EMBL; M15202; AAA96483.1; -; Genomic_DNA.
DR EMBL; DQ062204; AAY59901.1; -; mRNA.
DR EMBL; DQ273678; ABB51539.1; -; mRNA.
DR PIR; A24824; A24824.
DR RefSeq; NP_001257593.1; NM_001270664.1.
DR RefSeq; NP_001257594.1; NM_001270665.1. [P09739-1]
DR RefSeq; NP_001257595.1; NM_001270666.1.
DR RefSeq; NP_001257597.1; NM_001270668.1.
DR RefSeq; NP_001257599.1; NM_001270670.1.
DR RefSeq; NP_001257600.1; NM_001270671.1. [P09739-3]
DR RefSeq; NP_001257602.1; NM_001270673.1. [P09739-7]
DR RefSeq; NP_001257605.1; NM_001270676.1.
DR RefSeq; NP_001257607.1; NM_001270678.1.
DR RefSeq; NP_113720.1; NM_031532.2. [P09739-6]
DR RefSeq; XP_006230743.1; XM_006230681.3.
DR RefSeq; XP_006230745.1; XM_006230683.3.
DR RefSeq; XP_006230747.1; XM_006230685.3.
DR RefSeq; XP_006230748.1; XM_006230686.3.
DR RefSeq; XP_017444281.1; XM_017588792.1. [P09739-5]
DR RefSeq; XP_017444282.1; XM_017588793.1.
DR RefSeq; XP_017444283.1; XM_017588794.1.
DR AlphaFoldDB; P09739; -.
DR BMRB; P09739; -.
DR BioGRID; 246956; 1.
DR STRING; 10116.ENSRNOP00000049386; -.
DR iPTMnet; P09739; -.
DR PhosphoSitePlus; P09739; -.
DR PaxDb; P09739; -.
DR GeneID; 24838; -.
DR KEGG; rno:24838; -.
DR UCSC; RGD:3883; rat. [P09739-1]
DR CTD; 7140; -.
DR RGD; 3883; Tnnt3.
DR VEuPathDB; HostDB:ENSRNOG00000020332; -.
DR eggNOG; KOG3634; Eukaryota.
DR HOGENOM; CLU_076377_1_0_1; -.
DR InParanoid; P09739; -.
DR OrthoDB; 1480247at2759; -.
DR PhylomeDB; P09739; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P09739; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020332; Expressed in quadriceps femoris and 16 other tissues.
DR ExpressionAtlas; P09739; baseline and differential.
DR Genevisible; P09739; RN.
DR GO; GO:0005861; C:troponin complex; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0005523; F:tropomyosin binding; ISO:RGD.
DR GO; GO:0030172; F:troponin C binding; ISO:RGD.
DR GO; GO:0031013; F:troponin I binding; ISO:RGD.
DR GO; GO:0031014; F:troponin T binding; NAS:RGD.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:1903612; P:positive regulation of calcium-dependent ATPase activity; ISO:RGD.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:0006937; P:regulation of muscle contraction; IDA:RGD.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IMP:RGD.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR GO; GO:0003009; P:skeletal muscle contraction; ISO:RGD.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR027707; TNNT.
DR InterPro; IPR027708; Tnnt3.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR PANTHER; PTHR11521; PTHR11521; 1.
DR PANTHER; PTHR11521:SF4; PTHR11521:SF4; 1.
DR Pfam; PF00992; Troponin; 1.
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:P02641"
FT CHAIN 2..259
FT /note="Troponin T, fast skeletal muscle"
FT /id="PRO_0000186181"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..180
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:P02641"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 209
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 10..15
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006658"
FT VAR_SEQ 16..21
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006659"
FT VAR_SEQ 22..26
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_006660"
FT VAR_SEQ 28..31
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_006661"
FT VAR_SEQ 32..36
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_006663"
FT VAR_SEQ 230..242
FT /note="TTLRSRIDQAQKH -> MNVRARVEMLAKF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16839517"
FT /id="VSP_006664"
FT MOD_RES P09739-3:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P09739-6:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES P09739-7:2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 259 AA; 30750 MW; 37BDCF3394F2B5B7 CRC64;
MSDEETEQVE EQYEEEEEAQ EEEVQEEAPE PEEVQEEEKP RPKLTAPKIP EGEKVDFDDI
QKKRQNKDLM ELQALIDSHF EARKKEEEEL IALKERIEKR RAERAEQQRI RAEKERERQN
RLAEEKARRE EEDAKRRAED DLKKKKALSS MGANYSSYLA KADQKRGKKQ TAREMKKKIL
AERRKPLNID HLSDDKLRDK AKELWDTLYQ LETDKFEFGE KLKRQKYDIT TLRSRIDQAQ
KHSKKAGATA KGKVGGRWK
