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TNNT3_CHICK
ID   TNNT3_CHICK             Reviewed;         263 AA.
AC   P12620; P12618; P12619; P12621;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Troponin T, fast skeletal muscle isoforms;
GN   Name=TNNT3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TNT-1; TNT-2; TNT-3 AND TNT-4).
RX   PubMed=3198600; DOI=10.1016/s0021-9258(18)37355-1;
RA   Smillie L.B., Golosinska K., Reinach F.C.;
RT   "Sequences of complete cDNAs encoding four variants of chicken skeletal
RT   muscle troponin T.";
RL   J. Biol. Chem. 263:18816-18820(1988).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 58-112, X-RAY CRYSTALLOGRAPHY
RP   (3.0 ANGSTROMS) OF 157-262, AND FUNCTION.
RX   PubMed=15784741; DOI=10.1073/pnas.0408882102;
RA   Vinogradova M.V., Stone D.B., Malanina G.G., Karatzaferi C., Cooke R.,
RA   Mendelson R.A., Fletterick R.J.;
RT   "Ca(2+)-regulated structural changes in troponin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:5038-5043(2005).
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       {ECO:0000269|PubMed:15784741}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=TNT-3;
CC         IsoId=P12620-1; Sequence=Displayed;
CC       Name=TNT-1;
CC         IsoId=P12620-2; Sequence=VSP_006633;
CC       Name=TNT-2;
CC         IsoId=P12620-3; Sequence=VSP_006634, VSP_006636;
CC       Name=TNT-4;
CC         IsoId=P12620-4; Sequence=VSP_006634, VSP_006635;
CC   -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR   EMBL; M22156; AAA49102.1; -; mRNA.
DR   EMBL; M22158; AAA49103.1; -; mRNA.
DR   EMBL; M22155; AAA49101.1; -; mRNA.
DR   EMBL; M22154; AAA49100.1; -; mRNA.
DR   PIR; A31957; A31957.
DR   PIR; B31957; B31957.
DR   PIR; C31957; C31957.
DR   PIR; D31957; D31957.
DR   RefSeq; XP_015142056.1; XM_015286570.1. [P12620-1]
DR   RefSeq; XP_015142059.1; XM_015286573.1. [P12620-3]
DR   RefSeq; XP_015142062.1; XM_015286576.1. [P12620-4]
DR   PDB; 1YTZ; X-ray; 3.00 A; T=157-263.
DR   PDB; 1YV0; X-ray; 7.00 A; T=157-263.
DR   PDB; 2W49; EM; 35.00 A; 1/4/7/Y=160-249.
DR   PDB; 2W4U; EM; 35.00 A; 1/4/7/Y=160-249.
DR   PDB; 2Z5H; X-ray; 2.89 A; T=58-112.
DR   PDBsum; 1YTZ; -.
DR   PDBsum; 1YV0; -.
DR   PDBsum; 2W49; -.
DR   PDBsum; 2W4U; -.
DR   PDBsum; 2Z5H; -.
DR   AlphaFoldDB; P12620; -.
DR   SMR; P12620; -.
DR   IntAct; P12620; 2.
DR   MINT; P12620; -.
DR   STRING; 9031.ENSGALP00000010605; -.
DR   GeneID; 395761; -.
DR   CTD; 7140; -.
DR   VEuPathDB; HostDB:geneid_395761; -.
DR   eggNOG; KOG3634; Eukaryota.
DR   HOGENOM; CLU_076377_2_0_1; -.
DR   InParanoid; P12620; -.
DR   OrthoDB; 1480247at2759; -.
DR   EvolutionaryTrace; P12620; -.
DR   PRO; PR:P12620; -.
DR   Proteomes; UP000000539; 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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Muscle protein;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..263
FT                   /note="Troponin T, fast skeletal muscle isoforms"
FT                   /id="PRO_0000186183"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          107..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..188
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"
FT   VAR_SEQ         12..35
FT                   /note="EEYEEEAHEAEEVHEEEVHEPAPP -> AHEAEEVHEEAHHEEAHHAEAHHE
FT                   EAHAHAEEVHE (in isoform TNT-1)"
FT                   /evidence="ECO:0000303|PubMed:3198600"
FT                   /id="VSP_006633"
FT   VAR_SEQ         12..17
FT                   /note="Missing (in isoform TNT-2 and isoform TNT-4)"
FT                   /evidence="ECO:0000303|PubMed:3198600"
FT                   /id="VSP_006634"
FT   VAR_SEQ         39..44
FT                   /note="Missing (in isoform TNT-4)"
FT                   /evidence="ECO:0000303|PubMed:3198600"
FT                   /id="VSP_006635"
FT   VAR_SEQ         236..248
FT                   /note="VTLRNRIDQAQKH -> LTLRCRLQELSKF (in isoform TNT-2)"
FT                   /evidence="ECO:0000303|PubMed:3198600"
FT                   /id="VSP_006636"
FT   TURN            70..73
FT                   /evidence="ECO:0007829|PDB:2Z5H"
FT   HELIX           74..77
FT                   /evidence="ECO:0007829|PDB:2Z5H"
FT   TURN            78..84
FT                   /evidence="ECO:0007829|PDB:2Z5H"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:2Z5H"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:2Z5H"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:2Z5H"
FT   HELIX           164..188
FT                   /evidence="ECO:0007829|PDB:1YTZ"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:1YTZ"
FT   HELIX           202..244
FT                   /evidence="ECO:0007829|PDB:1YTZ"
SQ   SEQUENCE   263 AA;  31142 MW;  DBBB46419CCE6FAC CRC64;
     MSDTEEVEHG EEEYEEEAHE AEEVHEEEVH EPAPPPEEAP EEEEKPRIKL TAPKIPEGEK
     VDFDDIQKKR QNKDLIELQA LIDSHFEARR KEEEELVALK ERIEKRRAER AEQQRIRAEK
     EKERQARLAE EKARREEEDA KRKAEDDLKK KKALSSMGAS YSSYLAKADQ KRGKKQTARE
     TKKKVLAERR KPLNIDHLNE DKLRDKAKEL WDWLYQLQTE KYDFAEQIKR KKYEIVTLRN
     RIDQAQKHSK KAGAKGKVGG RWK
 
 
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