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TNNT3_RABIT
ID   TNNT3_RABIT             Reviewed;         279 AA.
AC   P02641; P19349; P19350;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Troponin T, fast skeletal muscle;
DE            Short=TnTf;
DE   AltName: Full=Fast skeletal muscle troponin T;
DE            Short=fTnT;
GN   Name=TNNT3;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-11; 18-44 AND 57-279.
RX   PubMed=320204; DOI=10.1016/s0021-9258(19)75195-3;
RA   Pearlstone J.R., Johnson P., Carpenter M.R., Smillie L.B.;
RT   "Primary structure of rabbit skeletal muscle troponin-T. Sequence
RT   determination of the NH2-terminal fragment CB3 and the complete sequence of
RT   troponin-T.";
RL   J. Biol. Chem. 252:983-989(1977).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-67, AND ALTERNATIVE SPLICING.
RC   STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX   PubMed=8344466; DOI=10.1006/dbio.1993.1208;
RA   Briggs M.M., Schachat F.;
RT   "Origin of fetal troponin T: developmentally regulated splicing of a new
RT   exon in the fast troponin T gene.";
RL   Dev. Biol. 158:503-509(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-67, AND ALTERNATIVE SPLICING.
RC   STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX   PubMed=2373251; DOI=10.1016/0012-1606(90)90075-t;
RA   Briggs M.M., McGinnis H.D., Schachat F.;
RT   "Transitions from fetal to fast troponin T isoforms are coordinated with
RT   changes in tropomyosin and alpha-actinin isoforms in developing rabbit
RT   skeletal muscle.";
RL   Dev. Biol. 140:253-260(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-67, AND ALTERNATIVE SPLICING.
RC   STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RA   Briggs M.M., Schachat F.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 2-44 AND 57-66, ACETYLATION AT SER-2, AND CLEAVAGE OF
RP   INITIATOR METHIONINE.
RC   STRAIN=New Zealand white; TISSUE=Skeletal muscle;
RX   PubMed=2704041; DOI=10.1016/0022-2836(89)90538-x;
RA   Briggs M.M., Schachat F.;
RT   "N-terminal amino acid sequences of three functionally different troponin T
RT   isoforms from rabbit fast skeletal muscle.";
RL   J. Mol. Biol. 206:245-249(1989).
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=9;
CC       Name=TnT1;
CC         IsoId=P02641-1; Sequence=Displayed;
CC       Name=TnT1F;
CC         IsoId=P02641-2; Sequence=VSP_006656;
CC       Name=TnT2;
CC         IsoId=P02641-3; Sequence=VSP_006655;
CC       Name=TnT2F;
CC         IsoId=P02641-4; Sequence=VSP_006653, VSP_006656;
CC       Name=TnT2FA;
CC         IsoId=P02641-5; Sequence=VSP_006655, VSP_006656;
CC       Name=TnT2.5F;
CC         IsoId=P02641-6; Sequence=VSP_006653, VSP_006655, VSP_006656;
CC       Name=TnT3;
CC         IsoId=P02641-7; Sequence=VSP_006654;
CC       Name=TnT3F;
CC         IsoId=P02641-8; Sequence=VSP_006654, VSP_006656;
CC       Name=TnT4F;
CC         IsoId=P02641-9; Sequence=VSP_006653, VSP_006654, VSP_006656;
CC   -!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
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DR   EMBL; U04970; AAA16023.1; -; mRNA.
DR   EMBL; U04971; AAA16024.1; -; mRNA.
DR   EMBL; U04972; AAA16025.1; -; mRNA.
DR   EMBL; U04973; AAA16026.1; -; mRNA.
DR   EMBL; U04974; AAA16027.1; -; mRNA.
DR   EMBL; U04975; AAA16028.1; -; mRNA.
DR   EMBL; U04976; AAA16029.1; -; mRNA.
DR   EMBL; U04977; AAA16030.1; -; mRNA.
DR   EMBL; U04978; AAA16031.1; -; mRNA.
DR   AlphaFoldDB; P02641; -.
DR   BMRB; P02641; -.
DR   SMR; P02641; -.
DR   CORUM; P02641; -.
DR   STRING; 9986.ENSOCUP00000001509; -.
DR   iPTMnet; P02641; -.
DR   eggNOG; KOG3634; Eukaryota.
DR   InParanoid; P02641; -.
DR   Proteomes; UP000001811; 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   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Muscle protein; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2704041,
FT                   ECO:0000269|PubMed:320204"
FT   CHAIN           2..279
FT                   /note="Troponin T, fast skeletal muscle"
FT                   /id="PRO_0000186180"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..200
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        56..82
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:2704041"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZ47"
FT   MOD_RES         176
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   MOD_RES         229
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P09739"
FT   VAR_SEQ         12..17
FT                   /note="Missing (in isoform TnT2F, isoform TnT2.5F and
FT                   isoform TnT4F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006653"
FT   VAR_SEQ         23..39
FT                   /note="Missing (in isoform TnT3, isoform TnT3F and isoform
FT                   TnT4F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006654"
FT   VAR_SEQ         33..39
FT                   /note="Missing (in isoform TnT2, isoform TnT2FA and isoform
FT                   TnT2.5F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006655"
FT   VAR_SEQ         45..56
FT                   /note="Missing (in isoform TnT1F, isoform TnT2F, isoform
FT                   TnT2FA, isoform TnT2.5F, isoform TnT3F and isoform TnT4F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006656"
FT   CONFLICT        20
FT                   /note="Q -> E (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36..37
FT                   /note="VH -> HV (in Ref. 1; AA sequence and 5; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   279 AA;  33034 MW;  1CF35712F2EE5281 CRC64;
     MSDEEVEHVE EQYEEEEEAQ EEAPSPAEVH EPAPEVHVPE EVHEDALEDM REEEEEEEKP
     RPKLTAPKIP EGEKVDFDDI QKKRQNKDLM ELQALIDSHF EARKKEEEEL VALKERIEKR
     RAERAEQQRI RAEKERERQN RLAEEKARRE EEDAKRRAEE DLKKKKALSS MGANYSSYLA
     KADQKRGKKQ TAREMKKKIL AERRKPLNID HLSDEKLRDK AKELWDTLYQ LETDKFEFGE
     KLKRQKYDIM NVRARVEMLA KFSKKAGTTA KGKVGGRWK
 
 
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