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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
 
 
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