ID   TNNT3_BOVIN             Reviewed;         271 AA.
AC   Q8MKI3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Troponin T, fast skeletal muscle;
DE            Short=TnTf;
GN   Name=Tnnt3;
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   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Holstein; TISSUE=Skeletal muscle;
RX   PubMed=12772845; DOI=10.2527/2003.8151185x;
RA   Muroya S., Nakajima I., Chikuni K.;
RT   "Amino acid sequences of multiple fast and slow troponin T isoforms
RT   expressed in adult bovine skeletal muscles.";
RL   J. Anim. Sci. 81:1185-1192(2003).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR   EMBL; AB085593; BAB92976.1; -; mRNA.
DR   AlphaFoldDB; Q8MKI3; -.
DR   BMRB; Q8MKI3; -.
DR   STRING; 9913.ENSBTAP00000054396; -.
DR   PaxDb; Q8MKI3; -.
DR   PRIDE; Q8MKI3; -.
DR   eggNOG; KOG3634; Eukaryota.
DR   HOGENOM; CLU_076377_1_0_1; -.
DR   InParanoid; Q8MKI3; -.
DR   TreeFam; TF313321; -.
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:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0006942; P:regulation of striated muscle contraction; IEA:InterPro.
DR   GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR   GO; GO:0003009; P:skeletal muscle contraction; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Muscle protein; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02641"
FT   CHAIN           2..271
FT                   /note="Troponin T, fast skeletal muscle"
FT                   /id="PRO_0000345625"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..194
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:0000250|UniProtKB:P09739"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         161
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZ47"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         221
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
SQ   SEQUENCE   271 AA;  32126 MW;  BB28B6153E01D5C9 CRC64;
     MSDEEVEHVE EEYEEEEEAQ EEAPPPPAEV PEVHEEVHEV HEPEEVQEEE KPRPRLTAPK
     IPEGEKVDFD DIQKKRQNKD LMELQALIDS HFEARKKEEE ELVALKERIE KRRAERAEQQ
     RIRAEKERER QNRLAEEKAR REEEDAKRRA EDDLKKKKAL SSMGANYSSY LAKADQKRGK
     KQTAREMKKK VLAERRKPLN IDHLSEDKLR DKAKELWDTL YQLETDKFEY GEKLKRQKYD
     ITNLRSRIDQ AQKHSKKAGT APKGKVGGRW K