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Database: UniProt
Entry: A0A091G0E8_9AVES
LinkDB: A0A091G0E8_9AVES
Original site: A0A091G0E8_9AVES 
ID   A0A091G0E8_9AVES        Unreviewed;       285 AA.
AC   A0A091G0E8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   SubName: Full=Troponin T, cardiac muscle isoforms {ECO:0000313|EMBL:KFO75950.1};
DE   Flags: Fragment;
GN   ORFNames=N303_06465 {ECO:0000313|EMBL:KFO75950.1};
OS   Cuculus canorus (common cuckoo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX   NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO75950.1, ECO:0000313|Proteomes:UP000053760};
RN   [1] {ECO:0000313|EMBL:KFO75950.1, ECO:0000313|Proteomes:UP000053760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO75950.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003363}.
CC   -!- SIMILARITY: Belongs to the troponin T family.
CC       {ECO:0000256|ARBA:ARBA00008330}.
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DR   EMBL; KL447652; KFO75950.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091G0E8; -.
DR   STRING; 55661.A0A091G0E8; -.
DR   Proteomes; UP000053760; Unassembled WGS sequence.
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; TROPONIN T; 1.
DR   PANTHER; PTHR11521:SF5; TROPONIN T, CARDIAC MUSCLE; 1.
DR   Pfam; PF00992; Troponin; 1.
DR   SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053760}.
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          124..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          222..256
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..55
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..215
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO75950.1"
FT   NON_TER         285
FT                   /evidence="ECO:0000313|EMBL:KFO75950.1"
SQ   SEQUENCE   285 AA;  34139 MW;  71A2607554176F5F CRC64;
     EEEYVEEEEE EWIEEEDGQE ELVEEVEEET EETKAEEQED ETKAPEEDGE GDREQEPGEG
     ESKPKPKVFM PNLVPPKIPD GERLDFDDIH RKRMEKDLNE LQALIEAHFE SRKKEEEELI
     SLKDRIEQRR AERAEQQRIR SEREKERQAR MAEERARKEE EEARKRAEEE ARKKKALSNM
     LHFGGYMQKS EKKGGKKQTE REKKKKILSE RRKPLNIDHL SEDKLREKAK ELWQTIRDLE
     AEKFDLQEKF KRQKYEINVL RNRVSDHQKV SKGARGKTMV GGRWK
//
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