TNNT3_PIG
ID TNNT3_PIG Reviewed; 271 AA.
AC Q75NG9;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Troponin T, fast skeletal muscle;
DE Short=TnTf;
GN Name=TNNT3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Landrace x Large White x Duroc; TISSUE=Skeletal muscle;
RX PubMed=16556993; DOI=10.1271/bbb.70.726;
RA Kitamura S., Muroya S., Nakajima I., Chikuni K., Nishimura T.;
RT "Amino acid sequences of porcine fast and slow troponin T isoforms.";
RL Biosci. Biotechnol. Biochem. 70:726-728(2006).
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; AB176599; BAD15381.1; -; mRNA.
DR RefSeq; NP_001001863.1; NM_001001863.1.
DR AlphaFoldDB; Q75NG9; -.
DR BMRB; Q75NG9; -.
DR PeptideAtlas; Q75NG9; -.
DR PRIDE; Q75NG9; -.
DR Ensembl; ENSSSCT00025029337; ENSSSCP00025012457; ENSSSCG00025020932.
DR Ensembl; ENSSSCT00045008325; ENSSSCP00045005669; ENSSSCG00045004918.
DR Ensembl; ENSSSCT00060044605; ENSSSCP00060019024; ENSSSCG00060032941.
DR Ensembl; ENSSSCT00065085065; ENSSSCP00065037152; ENSSSCG00065061768.
DR Ensembl; ENSSSCT00065085270; ENSSSCP00065037253; ENSSSCG00065061768.
DR Ensembl; ENSSSCT00070031488; ENSSSCP00070026249; ENSSSCG00070015620.
DR GeneID; 414906; -.
DR KEGG; ssc:414906; -.
DR CTD; 7140; -.
DR InParanoid; Q75NG9; -.
DR OMA; EAKTVFM; -.
DR OrthoDB; 1480247at2759; -.
DR Reactome; R-SSC-390522; Striated Muscle Contraction.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR GO; GO:0005861; C:troponin complex; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
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:1903612; P:positive regulation of calcium-dependent ATPase activity; IEA:Ensembl.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IEA:Ensembl.
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_0000345626"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..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 24..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..192
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; 32176 MW; EC87F0FAC7EFE55E CRC64;
MSDEEVEHVE EEYEEEEEAQ EEAPPPPAEV HEVHEEVHEV HEPEEVQEEE KPRPKLTAPK
IPEGEKVDFD DIQKKRQNKD LMELQALIDS HFEARKKEEE ELVALKERIE KRRAERAEQQ
RIRAEKERER QNRLAEEKAR REEEEAKRRA EDDLKKKKAL SSMGANYSSY LAKADQKRGK
KQTAREMKKK VLAERRKPLN IDHLSEDKLR DKAKELWDAL YQLEIDKFEY GEKLKRQKYD
IINLRSRIDQ AQKHSKKAGT TPKGKVGGRW K