GENTAUR Molecular Products.

 TNNI_DROME              Reviewed;         269 AA.
 P36188; Q0KHR0; Q9VWY1; Q9VWY2; Q9VWY3; Q9VWY4;
 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
 23-JAN-2007, sequence version 3.
 18-JUL-2018, entry version 157.
 RecName: Full=Troponin I;
          Short=Tn I;
 AltName: Full=Protein heldup;
 AltName: Full=Protein wings apart-A;
 Name=wupA; Synonyms=HDP, TnI; ORFNames=CG7178;
 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 [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 2
 AND 9), AND FUNCTION.
 STRAIN=Canton-S; TISSUE=Embryo, and Larva;
 PubMed=1899228; DOI=10.1101/gad.5.1.132;
 Barbas J.A., Galceran J., Krah-Jentgens I., de la Pompa J.L.,
 Canal I., Pongs O., Ferrus A.;
 "Troponin I is encoded in the haplolethal region of the Shaker gene
 complex of Drosophila.";
 Genes Dev. 5:132-140(1991).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
 STRAIN=Oregon-R; TISSUE=Pupae;
 PubMed=1908472; DOI=10.1083/jcb.114.5.941;
 Beall C.J., Fyrberg E.;
 "Muscle abnormalities in Drosophila melanogaster heldup mutants are
 caused by missing or aberrant troponin-I isoforms.";
 J. Cell Biol. 114:941-951(1991).
 [3]
 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).
 [4]
 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).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
 STRAIN=Berkeley; TISSUE=Head;
 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).
 [6]
 ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
 PubMed=7680094; DOI=10.1128/MCB.13.3.1433;
 Barbas J.A., Galceran J., Torroja L., Prado A., Ferrus A.;
 "Abnormal muscle development in the heldup3 mutant of Drosophila
 melanogaster is caused by a splicing defect affecting selected
 troponin I isoforms.";
 Mol. Cell. Biol. 13:1433-1439(1993).
 -!- FUNCTION: Troponin I is the ATPase inhibitory subunit of troponin
     in the thin filament regulatory complex. Involved in the
     development and maintenance of muscle and nervous system. May also
     be involved in the cytoskeletal apparatus.
     {ECO:0000269|PubMed:1899228}.
 -!- SUBUNIT: Binds to actin and tropomyosin.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=10;
       Comment=Exon 3 is either present or absent, exon 6 has 4
       mutually exclusive forms (6a1, 6a2, 6b1 and 6b2) and C-terminal
       exons 9 and 10 are mutually exclusive.;
     Name=10; Synonyms=G;
       IsoId=P36188-1; Sequence=Displayed;
     Name=1;
       IsoId=P36188-2; Sequence=VSP_006626, VSP_006627, VSP_006630;
     Name=2; Synonyms=A;
       IsoId=P36188-3; Sequence=VSP_006626, VSP_006627;
     Name=3;
       IsoId=P36188-4; Sequence=VSP_006626, VSP_006628, VSP_006630;
     Name=4; Synonyms=B;
       IsoId=P36188-5; Sequence=VSP_006626, VSP_006628;
     Name=5;
       IsoId=P36188-6; Sequence=VSP_006626, VSP_006630;
     Name=6; Synonyms=C, F;
       IsoId=P36188-7; Sequence=VSP_006626;
     Name=7;
       IsoId=P36188-8; Sequence=VSP_006626, VSP_006629, VSP_006630;
     Name=8; Synonyms=D, E;
       IsoId=P36188-9; Sequence=VSP_006626, VSP_006629;
     Name=9;
       IsoId=P36188-10; Sequence=VSP_006630;
 -!- TISSUE SPECIFICITY: All isoforms are expressed in somatic muscle.
     Isoforms containing exon 6a1 (isoforms 1 and 2) are expressed in
     all muscles but highest expression is in abdominal muscle and
     splanchnic muscle of the gut. Isoforms containing exon 6b1
     (isoforms 5, 6, 9 and 10) are highly expressed in the tergal
     depressor of trochanter (TDT) muscle.
     {ECO:0000269|PubMed:7680094}.
 -!- DEVELOPMENTAL STAGE: Isoforms containing exon 3 (isoform 9 and
     isoform 10) are expressed in adults. Isoforms containing exon 6a1
     (isoforms 1 and 2) are expressed at all developmental stages.
     Isoforms containing exon 6a2 (isoforms 3 and 4) are weakly
     expressed in embryos and larvae and very weakly in adults.
     Isoforms containing exon 6b1 (isoforms 5, 6, 9 and 10) are weakly
     expressed in larva and increase during metamorphosis. Isoforms
     containing exon 6b2 (isoforms 7 and 8) are weakly expressed in
     embryos and larvae and at a higher level in adults.
     {ECO:0000269|PubMed:7680094}.
 -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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 EMBL; X58188; CAA41171.1; -; Genomic_DNA.
 EMBL; X59376; CAA42020.1; -; mRNA.
 EMBL; AE014298; AAF48802.2; -; Genomic_DNA.
 EMBL; AE014298; AAF48803.2; -; Genomic_DNA.
 EMBL; AE014298; AAF48804.2; -; Genomic_DNA.
 EMBL; AE014298; AAN09458.1; -; Genomic_DNA.
 EMBL; AE014298; AAN09460.1; -; Genomic_DNA.
 EMBL; AY122145; AAM52657.1; -; mRNA.
 PIR; A38594; A38594.
 PIR; A40547; A40547.
 PIR; A48147; A48147.
 PIR; B38594; B38594.
 PIR; B48147; B48147.
 PIR; C48147; C48147.
 PIR; D48147; D48147.
 RefSeq; NP_523398.1; NM_078674.4. [P36188-7]
 RefSeq; NP_728137.1; NM_167603.3. [P36188-7]
 RefSeq; NP_728138.1; NM_167604.4. [P36188-9]
 RefSeq; NP_728139.1; NM_167605.3. [P36188-9]
 RefSeq; NP_728140.1; NM_167606.3. [P36188-5]
 RefSeq; NP_728141.1; NM_167607.3. [P36188-3]
 RefSeq; NP_728142.1; NM_167608.3. [P36188-1]
 UniGene; Dm.1717; -.
 ProteinModelPortal; P36188; -.
 SMR; P36188; -.
 BioGrid; 59114; 48.
 DIP; DIP-22750N; -.
 IntAct; P36188; 9.
 STRING; 7227.FBpp0074298; -.
 PaxDb; P36188; -.
 PeptideAtlas; P36188; -.
 PRIDE; P36188; -.
 EnsemblMetazoa; FBtr0074520; FBpp0074294; FBgn0283471. [P36188-3]
 EnsemblMetazoa; FBtr0074521; FBpp0074295; FBgn0283471. [P36188-5]
 EnsemblMetazoa; FBtr0074522; FBpp0074296; FBgn0283471. [P36188-7]
 EnsemblMetazoa; FBtr0074523; FBpp0074297; FBgn0283471. [P36188-9]
 EnsemblMetazoa; FBtr0074524; FBpp0074298; FBgn0283471. [P36188-1]
 EnsemblMetazoa; FBtr0074525; FBpp0074299; FBgn0283471. [P36188-7]
 EnsemblMetazoa; FBtr0074526; FBpp0074300; FBgn0283471. [P36188-9]
 EnsemblMetazoa; FBtr0308235; FBpp0300555; FBgn0283471. [P36188-10]
 EnsemblMetazoa; FBtr0308236; FBpp0300556; FBgn0283471. [P36188-8]
 EnsemblMetazoa; FBtr0308237; FBpp0300557; FBgn0283471. [P36188-2]
 GeneID; 32794; -.
 KEGG; dme:Dmel_CG7178; -.
 CTD; 32794; -.
 FlyBase; FBgn0283471; wupA.
 eggNOG; KOG3977; Eukaryota.
 eggNOG; ENOG410Y9IX; LUCA.
 GeneTree; ENSGT00730000112188; -.
 InParanoid; P36188; -.
 OMA; KMFDTGG; -.
 OrthoDB; EOG091G1571; -.
 PhylomeDB; P36188; -.
 ChiTaRS; wupA; fly.
 GenomeRNAi; 32794; -.
 PRO; PR:P36188; -.
 Proteomes; UP000000803; Chromosome X.
 Bgee; FBgn0004028; -.
 ExpressionAtlas; P36188; differential.
 Genevisible; P36188; DM.
 GO; GO:0005861; C:troponin complex; IBA:GO_Central.
 GO; GO:0003779; F:actin binding; NAS:UniProtKB.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0048738; P:cardiac muscle tissue development; IMP:FlyBase.
 GO; GO:0060047; P:heart contraction; IMP:FlyBase.
 GO; GO:0007507; P:heart development; IMP:FlyBase.
 GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
 GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
 GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
 GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
 GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
 GO; GO:0000280; P:nuclear division; IMP:FlyBase.
 GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
 GO; GO:0007519; P:skeletal muscle tissue development; IMP:FlyBase.
 Gene3D; 1.20.5.350; -; 1.
 InterPro; IPR001978; Troponin.
 InterPro; IPR038077; Troponin_sf.
 Pfam; PF00992; Troponin; 1.
 2: Evidence at transcript level;
 Acetylation; Actin-binding; Alternative splicing; Calcium;
 Complete proteome; Metal-binding; Methylation; Muscle protein;
 Reference proteome.
 INIT_MET      1      1       Removed. {ECO:0000250}.
 CHAIN         2    269       Troponin I.
                              /FTId=PRO_0000186159.
 CA_BIND     197    208       {ECO:0000250}.
 REGION      162    171       Troponin T-interaction. {ECO:0000250}.
 REGION      189    202       Actin-binding. {ECO:0000250}.
 MOD_RES       2      2       N-acetylalanine. {ECO:0000250}.
 MOD_RES     201    201       N6,N6,N6-trimethyllysine. {ECO:0000250}.
 MOD_RES     205    205       N6,N6,N6-trimethyllysine. {ECO:0000250}.
 VAR_SEQ       6     66       Missing (in isoform 1, isoform 2, isoform
                              3, isoform 4, isoform 5, isoform 6,
                              isoform 7 and isoform 8).
                              {ECO:0000303|PubMed:12537569,
                              ECO:0000303|PubMed:1908472}.
                              /FTId=VSP_006626.
 VAR_SEQ     151    183       GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> DTLK
                              SLIKQHYDRINKLEDQKYDLEYVVKRKDV (in isoform
                              1 and isoform 2). {ECO:0000305}.
                              /FTId=VSP_006627.
 VAR_SEQ     151    183       GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> DTIQ
                              SVCKDYHSKILKLESEKYDFEYDVARKDY (in isoform
                              3 and isoform 4). {ECO:0000305}.
                              /FTId=VSP_006628.
 VAR_SEQ     151    183       GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> AELQ
                              TICKQYWQRVYSLEGDKFDLEHVQKVKAQ (in isoform
                              7 and isoform 8).
                              {ECO:0000303|PubMed:12537569}.
                              /FTId=VSP_006629.
 VAR_SEQ     249    269       PDWSKGKPGDAKVKEEVEAEA -> IKDAAVLNKAKK (in
                              isoform 1, isoform 3, isoform 5, isoform
                              7 and isoform 9). {ECO:0000305}.
                              /FTId=VSP_006630.
 SEQUENCE   269 AA;  30082 MW;  21A48CC974ED0D6F CRC64;
 MADDEKKAAA PAAAPAAAAK PAAPAAAPAA NGKAAPAANG KAAPAAAAAP AGPPKDPNDP
 KVKAEEAKKA KQAEIERKRA EVRKRMEEAS KAKKAKKGFM TPERKKKLRL LLRKKAAEEL
 KKEQERKAAE RRRIIEERCG SPRNLSDASE GELQEICEEY YERMYICEGQ KWDLEYEVRK
 KDWEINDLNA QVNDLRGKFV KPALKKVSKY ENKFAKLQKK AAEFNFRNQL KVVKKKEFTL
 EEEEKEKKPD WSKGKPGDAK VKEEVEAEA

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