TNNT2_RABIT
ID TNNT2_RABIT Reviewed; 301 AA.
AC P09741; P09742;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Troponin T, cardiac muscle;
DE Short=TnTc;
DE AltName: Full=Cardiac muscle troponin T;
DE Short=cTnT;
GN Name=TNNT2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8261593; DOI=10.1161/01.res.74.1.41;
RA Greig A., Hirschberg Y., Anderson P.A.W., Hainsworth C., Malouf N.N.,
RA Oakeley A.E., Kay B.K.;
RT "Molecular basis of cardiac troponin T isoform heterogeneity in rabbit
RT heart.";
RL Circ. Res. 74:41-47(1994).
RN [2]
RP PROTEIN SEQUENCE OF 2-301, AND ACETYLATION AT SER-2.
RC TISSUE=Heart;
RX PubMed=3782144; DOI=10.1016/s0021-9258(19)75959-6;
RA Pearlstone J.R., Carpenter M.R., Smillie L.B.;
RT "Amino acid sequence of rabbit cardiac troponin T.";
RL J. Biol. Chem. 261:16795-16810(1986).
RN [3]
RP PHOSPHORYLATION AT SER-2.
RX PubMed=7458911; DOI=10.1042/bj1890219;
RA Gusev N.B., Dobrovolskii A.B., Severin S.E.;
RT "Isolation and some properties of troponin T kinase from rabbit skeletal
RT muscle.";
RL Biochem. J. 189:219-226(1980).
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 -!- SUBUNIT: Binds with troponins I and C to make the thin-filament
CC regulatory complex, troponin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=CTNT1;
CC IsoId=P09741-1; Sequence=Displayed;
CC Name=CTNT2;
CC IsoId=P09741-2; Sequence=VSP_006651;
CC Name=CTNT3;
CC IsoId=P09741-3; Sequence=VSP_006652;
CC Name=CTNT4;
CC IsoId=P09741-4; Sequence=VSP_006651, VSP_006652;
CC -!- TISSUE SPECIFICITY: The major isoform in adult heart is CTNT4.
CC -!- PTM: Phosphorylation at Thr-216 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51160.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L40178; AAB51160.1; ALT_INIT; mRNA.
DR PIR; A25345; A25345.
DR PIR; A61032; A61032.
DR PIR; B25345; B25345.
DR PIR; I46903; I46903.
DR AlphaFoldDB; P09741; -.
DR iPTMnet; P09741; -.
DR PRIDE; P09741; -.
DR InParanoid; P09741; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005865; C:striated muscle thin filament; ISS:UniProtKB.
DR GO; GO:0005861; C:troponin complex; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
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: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; IEA:InterPro.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
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; Direct protein sequencing;
KW Muscle protein; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3782144"
FT CHAIN 2..301
FT /note="Troponin T, cardiac muscle"
FT /id="PRO_0000186175"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..72
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..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3782144"
FT MOD_RES 2
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:7458911"
FT MOD_RES 207
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 211
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P50752"
FT MOD_RES 216
FT /note="Phosphothreonine; by PKC/PRKCA and RAF1"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 297
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT VAR_SEQ 17..22
FT /note="Missing (in isoform CTNT2 and isoform CTNT4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006651"
FT VAR_SEQ 24..33
FT /note="Missing (in isoform CTNT3 and isoform CTNT4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006652"
FT CONFLICT 14..33
FT /note="EQEAEEAAAEEEDWREDEDE -> QQAG (in Ref. 2; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..32
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38..41
FT /note="EEEE -> AGGG (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="D -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="D -> ER (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="E -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..214
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 35876 MW; 88777671C9F35541 CRC64;
MSDLEEVVEE YEEEQEAEEA AAEEEDWRED EDEQEAGEEE EAGGGREAEA ETEETQAEED
GQEEEDKEDE DGPVEESKPK PRPFMPNLVP PKIPDGERVD FDDIHRKRME KDLNELQTLI
EAHFENRKKE EEELVSLKDR IEKRRADAEQ LRIRAEREKE RQNRLAEERA RREEEESRRK
AEDEARKKKA LSNMMHFGGY IQKQAQTERK SGKRQTEREK KKKILAERRK VLAIDHLNED
QLREKAKELW QSIYNLEAEK FDLQEKFKQQ KYEINVLRNR INDNQKVSKT RGKAKVTGRW
K
