TNNT2_BOVIN
ID TNNT2_BOVIN Reviewed; 285 AA.
AC P13789; P13790;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Troponin T, cardiac muscle;
DE Short=TnTc;
DE AltName: Full=Cardiac muscle troponin T;
DE Short=cTnT;
GN Name=TNNT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE OF 2-285.
RX PubMed=3122824; DOI=10.1021/bi00396a027;
RA Leszyk J., Dumaswala R., Potter J.D., Gusev N.B., Verin A.D.,
RA Tobacman L.S., Collins J.H.;
RT "Bovine cardiac troponin T: amino acid sequences of the two isoforms.";
RL Biochemistry 26:7035-7042(1987).
RN [2]
RP PROTEIN SEQUENCE OF 2-6 AND 284-285, PHOSPHORYLATION AT SER-2, AND BLOCKAGE
RP OF N-TERMINUS.
RX PubMed=6615417; DOI=10.1042/bj2130123;
RA Gusev N.B., Barskaya N.V., Verin A.D., Duzhenkova I.V., Khuchua Z.A.,
RA Zheltova A.O.;
RT "Some properties of cardiac troponin T structure.";
RL Biochem. J. 213:123-129(1983).
RN [3]
RP PROTEIN SEQUENCE OF 181-201, AND PHOSPHORYLATION.
RX PubMed=7748902; DOI=10.1016/0167-4838(95)00028-s;
RA Jaquet K., Fukunaga K., Miyamoto E., Meyer H.E.;
RT "A site phosphorylated in bovine cardiac troponin T by cardiac CaM kinase
RT II.";
RL Biochim. Biophys. Acta 1248:193-195(1995).
RN [4]
RP PHOSPHORYLATION AT THR-191; THR-200 AND THR-281.
RX PubMed=2584239; DOI=10.1016/s0021-9258(19)47130-5;
RA Noland T.A. Jr., Raynor R.L., Kuo J.F.;
RT "Identification of sites phosphorylated in bovine cardiac troponin I and
RT troponin T by protein kinase C and comparative substrate activity of
RT synthetic peptides containing the phosphorylation sites.";
RL J. Biol. Chem. 264:20778-20785(1989).
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;
CC IsoId=P13789-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13789-2; Sequence=VSP_006631;
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Phosphorylation at Thr-200 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 PIR; A28008; A28008.
DR AlphaFoldDB; P13789; -.
DR IntAct; P13789; 1.
DR MINT; P13789; -.
DR STRING; 9913.ENSBTAP00000054984; -.
DR iPTMnet; P13789; -.
DR PaxDb; P13789; -.
DR PRIDE; P13789; -.
DR eggNOG; KOG3634; Eukaryota.
DR InParanoid; P13789; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005861; C:troponin complex; IBA:GO_Central.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0030172; F:troponin C binding; IBA:GO_Central.
DR GO; GO:0031013; F:troponin I binding; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0006937; P:regulation of muscle contraction; IEA:InterPro.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
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:0000250|UniProtKB:P09741"
FT CHAIN 2..285
FT /note="Troponin T, cardiac muscle"
FT /id="PRO_0000186172"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
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, ECO:0000305"
FT MOD_RES 2
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:6615417"
FT MOD_RES 191
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000305|PubMed:2584239"
FT MOD_RES 195
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P50752"
FT MOD_RES 200
FT /note="Phosphothreonine; by PKC/PRKCA and RAF1"
FT /evidence="ECO:0000305|PubMed:2584239"
FT MOD_RES 281
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000305|PubMed:2584239"
FT VAR_SEQ 17..22
FT /note="AAEEEH -> N (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006631"
SQ SEQUENCE 285 AA; 33914 MW; 31290F00B6082499 CRC64;
MSDVEEAVEE YEEQEEAAEE EHEEAVEEEA GGEAEAGEPC TAEDGEEEEG REAEDGPVEE
FKPKPRPFMP NLVPPKIPDG ERVDFDDIHR KRMEKDLNEL QTLIEAHFEN RKKEEEELVS
LKDRIEKRRA ERAEQQRIRA EREKERQTRL AEERARREEE ESRRKAEDEA RKKKALSNMM
HFGGYIQKAQ TERKSGKRQT EREKKKKILA ERRKVLAIDH LNEDQLREKA KELWQMIYDL
EAEKFDLQEK FKQQKYEINV LRNRINDNQK VSKTRGKAKV TGRWK
