TNNT3_COTJA
ID TNNT3_COTJA Reviewed; 253 AA.
AC P06398; P06397;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Troponin T, fast skeletal muscle isoforms;
GN Name=TNNT3;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2745456; DOI=10.1016/s0021-9258(18)63884-0;
RA Bucher E.A., de la Brousse F.C., Emerson C.P. Jr.;
RT "Developmental and muscle-specific regulation of avian fast skeletal
RT troponin T isoform expression by mRNA splicing.";
RL J. Biol. Chem. 264:12482-12491(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 109-253.
RX PubMed=3840482; DOI=10.1016/s0021-9258(17)38782-3;
RA Hastings K.E.M., Bucher E.A., Emerson C.P. Jr.;
RT "Generation of troponin T isoforms by alternative RNA splicing in avian
RT skeletal muscle. Conserved and divergent features in birds and mammals.";
RL J. Biol. Chem. 260:13699-13703(1985).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P06398-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06398-2; Sequence=VSP_006637;
CC Name=3;
CC IsoId=P06398-3; Sequence=VSP_006638;
CC -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR EMBL; M26600; AAA49506.1; -; mRNA.
DR EMBL; M26599; AAA49505.1; -; mRNA.
DR EMBL; M11685; AAA49504.1; -; mRNA.
DR EMBL; M11684; AAA49503.1; -; mRNA.
DR PIR; A03084; TPQJT1.
DR PIR; A03085; TPQJT2.
DR PIR; A34327; A34327.
DR PIR; B34327; B34327.
DR AlphaFoldDB; P06398; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005861; C:troponin complex; IEA:InterPro.
DR GO; GO:0006942; P:regulation of striated muscle contraction; IEA:InterPro.
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; Alternative splicing; Muscle protein; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..253
FT /note="Troponin T, fast skeletal muscle isoforms"
FT /id="PRO_0000186184"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..178
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 28..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006637"
FT VAR_SEQ 226..238
FT /note="LTLRCRLQELSKF -> VTLRNRIDQAQKH (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006638"
SQ SEQUENCE 253 AA; 30098 MW; 5E37D1A587FAC997 CRC64;
MSDTEEVEHG EEEYEEEEEV QEEEVHEPAP PPEEKPRIKL TAPKIPEGEK VDFDDIQKKR
QNKDLIELQA LIDSHFEARR KEEEELVALK ERIEKRRAER AEQQRIRAEK EKERQARLAE
EKARREEEDA KRKAEDDLKK KKALSSMGAS YSSYLAKADQ KRGKKQTARE TKKKVLAERR
KPLNIDHLNE DKLRDKAKEL WDWLYQLQTE KYDFTEQIKR KKYEILTLRC RLQELSKFSK
KAGAKGKVGG RWK