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Troponin T, skeletal muscle (Protein intended thorax) (Protein upheld)

 TNNT_DROME              Reviewed;         397 AA.
P19351; E1JJP1; E1JJP2; E1JJP3; E4NKN4; F2FB91; Q59E46; Q59E47;
Q6T2Y5; Q6T2Y6; Q6T2Y7; Q6T2Y8; Q6T2Y9; Q8SZI3; Q960L9; Q9VYB3;
Q9VYB4; Q9VYB5;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 3.
25-OCT-2017, entry version 138.
RecName: Full=Troponin T, skeletal muscle;
AltName: Full=Protein intended thorax;
AltName: Full=Protein upheld;
Name=up; Synonyms=int; ORFNames=CG7107;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=Canton-S; TISSUE=Asynchronous muscle;
PubMed=2852258; DOI=10.1016/0022-2836(88)90360-9;
Bullard B., Leonard K., Larkins A., Butcher G., Karlik C.,
Fyrberg E.A.;
"Troponin of asynchronous flight muscle.";
J. Mol. Biol. 204:621-637(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SEQUENCE REVISION, FUNCTION,
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
STRAIN=Canton-S;
PubMed=2124273; DOI=10.1016/0022-2836(90)90390-8;
Fryberg E.A., Fryberg C.C., Beall C., Saville D.L.;
"Drosophila melanogaster troponin-T mutations engender three distinct
syndromes of myofibrillar abnormalities.";
J. Mol. Biol. 216:657-675(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
Herranz-Barranco R.;
"Gene evolution of the troponin complex in insects.";
Thesis (2003), Universidad Autonoma de Madrid (UAM), Spain.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 9).
Nongthomba U., Ansari M., Sparrow J.;
"Drosophila TpnT exon 10 is alternatively spliced.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[6]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 10), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-8 (ISOFORMS 2/3/6/8/9).
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
STRAIN=Berkeley; TISSUE=Embryo;
Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
[9]
GLYCYLATION.
PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
Janke C.;
"Evolutionary divergence of enzymatic mechanisms for posttranslational
polyglycylation.";
Cell 137:1076-1087(2009).
-!- FUNCTION: Troponin T is the tropomyosin-binding subunit of
troponin, the thin filament regulatory complex which confers
calcium-sensitivity to striated muscle actomyosin ATPase activity.
{ECO:0000269|PubMed:2124273}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=13;
Name=1; Synonyms=A;
IsoId=P19351-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2; Synonyms=T-2;
IsoId=P19351-2; Sequence=VSP_015192;
Name=3; Synonyms=T-1;
IsoId=P19351-3; Sequence=VSP_015192, VSP_015194;
Name=4; Synonyms=G;
IsoId=P19351-4; Sequence=VSP_015195;
Note=No experimental confirmation available.;
Name=5; Synonyms=K;
IsoId=P19351-5; Sequence=VSP_041843, VSP_015194, VSP_015195;
Note=Ref.8 (ADR83716) sequence is in conflict in position:
9:S->SS. {ECO:0000305};
Name=6; Synonyms=E, T-4;
IsoId=P19351-6; Sequence=VSP_015191;
Name=7; Synonyms=B;
IsoId=P19351-7; Sequence=VSP_015193;
Name=8; Synonyms=T-3;
IsoId=P19351-8; Sequence=VSP_015192, VSP_015193;
Name=9; Synonyms=T-5;
IsoId=P19351-9; Sequence=VSP_015191, VSP_015196;
Name=10; Synonyms=D;
IsoId=P19351-10; Sequence=VSP_015189;
Note=No experimental confirmation available.;
Name=11; Synonyms=I;
IsoId=P19351-11; Sequence=VSP_015196;
Note=No experimental confirmation available.;
Name=12; Synonyms=L;
IsoId=P19351-12; Sequence=VSP_041843, VSP_041844, VSP_015195;
Note=No experimental confirmation available.;
Name=13; Synonyms=J;
IsoId=P19351-13; Sequence=VSP_015193, VSP_015196;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 3 is expressed in the hypoderm.
Isoform 8 is expressed in the dorsal vessel. Isoform 6 is
expressed in adult TDT muscle and isoform 9 in adult IFM, flight
and jump muscles. {ECO:0000269|PubMed:2124273}.
-!- DEVELOPMENTAL STAGE: Isoform 2 is expressed only in larvae.
-!- PTM: Some glutamate residues are polyglycylated by TTLL3B. This
modification occurs exclusively on glutamate residues and results
in polyglycine chains on the gamma-carboxyl group.
-!- DISRUPTION PHENOTYPE: Flies exhibit 3 distinct syndromes of
myofibrillar abnormalities; elimination of thin filaments except
where they are bound by electron-dense material presumed to be Z-
disk proteins, degeneration of muscles and reduction in the
diameter of the myofibril lattice. {ECO:0000269|PubMed:2124273}.
-!- SIMILARITY: Belongs to the troponin T family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL48497.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X54504; CAA38366.1; -; mRNA.
EMBL; AY439172; AAR24583.1; -; Genomic_DNA.
EMBL; AY439172; AAR24584.1; -; Genomic_DNA.
EMBL; AY439172; AAR24585.1; -; Genomic_DNA.
EMBL; AY439172; AAR24586.1; -; Genomic_DNA.
EMBL; AY439172; AAR24587.1; -; Genomic_DNA.
EMBL; AY665838; AAU09446.1; -; mRNA.
EMBL; AE014298; AAF48288.2; -; Genomic_DNA.
EMBL; AE014298; AAF48289.2; -; Genomic_DNA.
EMBL; AE014298; AAF48290.1; -; Genomic_DNA.
EMBL; AE014298; AAX52491.1; -; Genomic_DNA.
EMBL; AE014298; AAX52492.1; -; Genomic_DNA.
EMBL; AE014298; AAX52493.2; -; Genomic_DNA.
EMBL; AE014298; ACZ95277.1; -; Genomic_DNA.
EMBL; AE014298; ACZ95278.1; -; Genomic_DNA.
EMBL; AE014298; ACZ95279.1; -; Genomic_DNA.
EMBL; AY051989; AAK93413.1; -; mRNA.
EMBL; AY070875; AAL48497.1; ALT_SEQ; mRNA.
EMBL; BT125831; ADR83716.1; -; mRNA.
EMBL; BT126178; ADZ99430.1; -; mRNA.
PIR; S02708; S02708.
PIR; S13251; S13251.
RefSeq; NP_001014737.1; NM_001014737.2. [P19351-4]
RefSeq; NP_001014738.2; NM_001014738.3. [P19351-5]
RefSeq; NP_001014739.1; NM_001014739.2. [P19351-6]
RefSeq; NP_001162741.1; NM_001169270.2. [P19351-9]
RefSeq; NP_001162742.1; NM_001169271.2. [P19351-11]
RefSeq; NP_001162743.1; NM_001169272.2. [P19351-13]
RefSeq; NP_001162744.1; NM_001169273.2. [P19351-12]
RefSeq; NP_001259522.1; NM_001272593.2. [P19351-3]
RefSeq; NP_001259523.1; NM_001272594.2. [P19351-2]
RefSeq; NP_001259524.1; NM_001272595.2. [P19351-8]
RefSeq; NP_001285213.1; NM_001298284.1. [P19351-8]
RefSeq; NP_001285214.1; NM_001298285.1. [P19351-8]
RefSeq; NP_001285215.1; NM_001298286.1. [P19351-10]
RefSeq; NP_525088.2; NM_080349.3. [P19351-1]
RefSeq; NP_727718.1; NM_167375.2. [P19351-7]
RefSeq; NP_727719.1; NM_167376.2. [P19351-10]
UniGene; Dm.20472; -.
ProteinModelPortal; P19351; -.
SMR; P19351; -.
BioGrid; 58691; 42.
IntAct; P19351; 2.
MINT; MINT-879747; -.
STRING; 7227.FBpp0073682; -.
PaxDb; P19351; -.
PeptideAtlas; P19351; -.
PRIDE; P19351; -.
EnsemblMetazoa; FBtr0073851; FBpp0073682; FBgn0004169. [P19351-1]
EnsemblMetazoa; FBtr0073852; FBpp0073683; FBgn0004169. [P19351-7]
EnsemblMetazoa; FBtr0073853; FBpp0073684; FBgn0004169. [P19351-10]
EnsemblMetazoa; FBtr0100561; FBpp0100013; FBgn0004169. [P19351-6]
EnsemblMetazoa; FBtr0100563; FBpp0100015; FBgn0004169. [P19351-4]
EnsemblMetazoa; FBtr0301919; FBpp0291133; FBgn0004169. [P19351-9]
EnsemblMetazoa; FBtr0301920; FBpp0291134; FBgn0004169. [P19351-11]
EnsemblMetazoa; FBtr0301921; FBpp0291135; FBgn0004169. [P19351-13]
EnsemblMetazoa; FBtr0301922; FBpp0291136; FBgn0004169. [P19351-5]
EnsemblMetazoa; FBtr0301923; FBpp0291137; FBgn0004169. [P19351-12]
EnsemblMetazoa; FBtr0310136; FBpp0301821; FBgn0004169. [P19351-3]
EnsemblMetazoa; FBtr0310137; FBpp0301822; FBgn0004169. [P19351-2]
EnsemblMetazoa; FBtr0310138; FBpp0301823; FBgn0004169. [P19351-8]
EnsemblMetazoa; FBtr0340617; FBpp0309481; FBgn0004169. [P19351-8]
EnsemblMetazoa; FBtr0340618; FBpp0309482; FBgn0004169. [P19351-8]
EnsemblMetazoa; FBtr0345131; FBpp0311352; FBgn0004169. [P19351-10]
GeneID; 32314; -.
KEGG; dme:Dmel_CG7107; -.
CTD; 104073; -.
FlyBase; FBgn0004169; up.
eggNOG; KOG3634; Eukaryota.
eggNOG; ENOG410XS6A; LUCA.
GeneTree; ENSGT00730000112220; -.
InParanoid; P19351; -.
KO; K12046; -.
OMA; KEYISEW; -.
OrthoDB; EOG091G0G1D; -.
PhylomeDB; P19351; -.
GenomeRNAi; 32314; -.
PRO; PR:P19351; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004169; -.
ExpressionAtlas; P19351; differential.
Genevisible; P19351; DM.
GO; GO:0005865; C:striated muscle thin filament; IDA:FlyBase.
GO; GO:0005861; C:troponin complex; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IDA:FlyBase.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:FlyBase.
GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
GO; GO:0048644; P:muscle organ morphogenesis; IMP:FlyBase.
GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
GO; GO:0006937; P:regulation of muscle contraction; IEA:InterPro.
GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:FlyBase.
InterPro; IPR027707; TNNT.
InterPro; IPR001978; Troponin.
PANTHER; PTHR11521; PTHR11521; 1.
Pfam; PF00992; Troponin; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Muscle protein;
Reference proteome.
CHAIN 1 397 Troponin T, skeletal muscle.
/FTId=PRO_0000186185.
COMPBIAS 342 397 Asp/Glu-rich (highly acidic).
VAR_SEQ 1 91 Missing (in isoform 10).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_015189.
VAR_SEQ 9 31 Missing (in isoform 6 and isoform 9).
{ECO:0000303|Ref.4}.
/FTId=VSP_015191.
VAR_SEQ 9 9 Missing (in isoform 2, isoform 3 and
isoform 8). {ECO:0000303|PubMed:2124273,
ECO:0000303|PubMed:2852258}.
/FTId=VSP_015192.
VAR_SEQ 10 10 Missing (in isoform 5 and isoform 12).
{ECO:0000303|Ref.8}.
/FTId=VSP_041843.
VAR_SEQ 24 31 Missing (in isoform 7, isoform 8 and
isoform 13). {ECO:0000303|Ref.8}.
/FTId=VSP_015193.
VAR_SEQ 24 24 K -> KK (in isoform 3 and isoform 5).
{ECO:0000303|Ref.8}.
/FTId=VSP_015194.
VAR_SEQ 25 31 Missing (in isoform 12). {ECO:0000305}.
/FTId=VSP_041844.
VAR_SEQ 155 155 Missing (in isoform 4, isoform 5 and
isoform 12). {ECO:0000303|Ref.8}.
/FTId=VSP_015195.
VAR_SEQ 288 311 WDEISKDSNEKIWNEKKEQYTGRQ -> YNTVYAETLEKTW
QERQERFTQRT (in isoform 9, isoform 11 and
isoform 13). {ECO:0000303|Ref.4}.
/FTId=VSP_015196.
CONFLICT 119 119 R -> A (in Ref. 1; no nucleotide entry
and 2; CAA38366). {ECO:0000305}.
CONFLICT 193 193 G -> A (in Ref. 1; no nucleotide entry
and 2; CAA38366). {ECO:0000305}.
CONFLICT 364 364 A -> D (in Ref. 1; no nucleotide entry
and 2; CAA38366). {ECO:0000305}.
SEQUENCE 397 AA; 47448 MW; 9D1E9074548CB8D5 CRC64;
MSDDEEYTSS EEEEVVEETR EETKPPQTPA EGEGDPEFIK RQDQKRSDLD DQLKEYITEW
RKQRSKEEDE LKKLKEKQAK RKVTRAEEEQ KMAQRKKEEE ERRVREAEEK KQREIEEKRM
RLEEAEKKRQ AMLQAMKDKD KKGPNFTIAK KDAGVLGLSS AAMERNKTKE QLEEEKKISL
SFRIKPLAIE GFGEAKLREK AQELWELIVK LETEKYDLEE RQKRQDYDLK ELKERQKQQL
RHKALKKGLD PEALTGKYPP KIQVASKYER RVDTRSYDDK KKLFEGGWDE ISKDSNEKIW
NEKKEQYTGR QKSKLPKWFG ERPGKKAGEP ETPEGEEDAK ADEDIVEDDE EVEEEVVEEE
DEEAEEDEEE EEEEEEEEEE EEEEEEEEEE EEEEEEE


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