TNNT2_SHEEP
ID TNNT2_SHEEP Reviewed; 287 AA.
AC P50751;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Troponin T, cardiac muscle;
DE Short=TnTc;
DE AltName: Full=Cardiac muscle troponin T;
DE Short=cTnT;
GN Name=TNNT2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fetal heart;
RX PubMed=1866215; DOI=10.1203/00006450-199106010-00012;
RA McAuliffe J.J., Robbins J.;
RT "Troponin T expression in normal and pressure-loaded fetal sheep heart.";
RL Pediatr. Res. 29:580-585(1991).
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 -!- DEVELOPMENTAL STAGE: Expressed from midgestation to adult life.
CC -!- PTM: Phosphorylation at Thr-202 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 AlphaFoldDB; P50751; -.
DR PRIDE; P50751; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR GO; GO:0006937; P:regulation of muscle contraction; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; Muscle protein; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09741"
FT CHAIN 2..287
FT /note="Troponin T, cardiac muscle"
FT /id="PRO_0000186177"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
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 197
FT /note="Phosphoserine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P50752"
FT MOD_RES 202
FT /note="Phosphothreonine; by PKC/PRKCA and RAF1"
FT /evidence="ECO:0000250|UniProtKB:P13789"
FT MOD_RES 283
FT /note="Phosphothreonine; by PKC/PRKCA"
FT /evidence="ECO:0000250|UniProtKB:P13789"
SQ SEQUENCE 287 AA; 33764 MW; 0AC80AAE862A080A CRC64;
MSDVEETVDE YEEQEEAAVE EHEESVEEEA GGEARQGGGA SAAEDGEEEE GREAEDGPVE
ESKPQAPGPF MPNLVPPKIP DGERVDFDDI HRKRMEKDLN ELQTLIEAHF ENRKKEEEEL
VSLKDRIEKR RAERAEQQRI RTEREKERQA RLAEERARRE EEESRRKAED EARKKKALSN
MMHFGGYIQK AQAERKSGKR QTEREKKKKI LAERRKVLAI DHLNEDQLRE KARELWQSIY
DLEAEKFDLQ EKFKQQKYEI NVLRNRVNDN QKVSKTRGKA KVTGRWK