ID TNNI_DROME Reviewed; 269 AA.
AC P36188; Q0KHR0; Q9VWY1; Q9VWY2; Q9VWY3; Q9VWY4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Troponin I;
DE Short=Tn I;
DE AltName: Full=Protein heldup;
DE AltName: Full=Protein wings apart-A;
GN Name=wupA; Synonyms=HDP, TnI; ORFNames=CG7178;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 2 AND 9),
RP AND FUNCTION.
RC STRAIN=Canton-S; TISSUE=Embryo, and Larva;
RX PubMed=1899228; DOI=10.1101/gad.5.1.132;
RA Barbas J.A., Galceran J., Krah-Jentgens I., de la Pompa J.L., Canal I.,
RA Pongs O., Ferrus A.;
RT "Troponin I is encoded in the haplolethal region of the Shaker gene complex
RT of Drosophila.";
RL Genes Dev. 5:132-140(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC STRAIN=Oregon-R; TISSUE=Pupae;
RX PubMed=1908472; DOI=10.1083/jcb.114.5.941;
RA Beall C.J., Fyrberg E.;
RT "Muscle abnormalities in Drosophila melanogaster heldup mutants are caused
RT by missing or aberrant troponin-I isoforms.";
RL J. Cell Biol. 114:941-951(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=7680094; DOI=10.1128/mcb.13.3.1433-1439.1993;
RA Barbas J.A., Galceran J., Torroja L., Prado A., Ferrus A.;
RT "Abnormal muscle development in the heldup3 mutant of Drosophila
RT melanogaster is caused by a splicing defect affecting selected troponin I
RT isoforms.";
RL Mol. Cell. Biol. 13:1433-1439(1993).
CC -!- FUNCTION: Troponin I is the ATPase inhibitory subunit of troponin in
CC the thin filament regulatory complex. Involved in the development and
CC maintenance of muscle and nervous system. May also be involved in the
CC cytoskeletal apparatus. {ECO:0000269|PubMed:1899228}.
CC -!- SUBUNIT: Binds to actin and tropomyosin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Comment=Exon 3 is either present or absent, exon 6 has 4 mutually
CC exclusive forms (6a1, 6a2, 6b1 and 6b2) and C-terminal exons 9 and 10
CC are mutually exclusive.;
CC Name=10; Synonyms=G;
CC IsoId=P36188-1; Sequence=Displayed;
CC Name=1;
CC IsoId=P36188-2; Sequence=VSP_006626, VSP_006627, VSP_006630;
CC Name=2; Synonyms=A;
CC IsoId=P36188-3; Sequence=VSP_006626, VSP_006627;
CC Name=3;
CC IsoId=P36188-4; Sequence=VSP_006626, VSP_006628, VSP_006630;
CC Name=4; Synonyms=B;
CC IsoId=P36188-5; Sequence=VSP_006626, VSP_006628;
CC Name=5;
CC IsoId=P36188-6; Sequence=VSP_006626, VSP_006630;
CC Name=6; Synonyms=C, F;
CC IsoId=P36188-7; Sequence=VSP_006626;
CC Name=7;
CC IsoId=P36188-8; Sequence=VSP_006626, VSP_006629, VSP_006630;
CC Name=8; Synonyms=D, E;
CC IsoId=P36188-9; Sequence=VSP_006626, VSP_006629;
CC Name=9;
CC IsoId=P36188-10; Sequence=VSP_006630;
CC -!- TISSUE SPECIFICITY: All isoforms are expressed in somatic muscle.
CC Isoforms containing exon 6a1 (isoforms 1 and 2) are expressed in all
CC muscles but highest expression is in abdominal muscle and splanchnic
CC muscle of the gut. Isoforms containing exon 6b1 (isoforms 5, 6, 9 and
CC 10) are highly expressed in the tergal depressor of trochanter (TDT)
CC muscle. {ECO:0000269|PubMed:7680094}.
CC -!- DEVELOPMENTAL STAGE: Isoforms containing exon 3 (isoform 9 and isoform
CC 10) are expressed in adults. Isoforms containing exon 6a1 (isoforms 1
CC and 2) are expressed at all developmental stages. Isoforms containing
CC exon 6a2 (isoforms 3 and 4) are weakly expressed in embryos and larvae
CC and very weakly in adults. Isoforms containing exon 6b1 (isoforms 5, 6,
CC 9 and 10) are weakly expressed in larva and increase during
CC metamorphosis. Isoforms containing exon 6b2 (isoforms 7 and 8) are
CC weakly expressed in embryos and larvae and at a higher level in adults.
CC {ECO:0000269|PubMed:7680094}.
CC -!- SIMILARITY: Belongs to the troponin I family. {ECO:0000305}.
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DR EMBL; X58188; CAA41171.1; -; Genomic_DNA.
DR EMBL; X59376; CAA42020.1; -; mRNA.
DR EMBL; AE014298; AAF48802.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF48803.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF48804.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09458.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09460.1; -; Genomic_DNA.
DR EMBL; AY122145; AAM52657.1; -; mRNA.
DR PIR; A38594; A38594.
DR PIR; A40547; A40547.
DR PIR; A48147; A48147.
DR PIR; B38594; B38594.
DR PIR; B48147; B48147.
DR PIR; C48147; C48147.
DR PIR; D48147; D48147.
DR RefSeq; NP_523398.1; NM_078674.4. [P36188-7]
DR RefSeq; NP_728137.1; NM_167603.3. [P36188-7]
DR RefSeq; NP_728138.1; NM_167604.4. [P36188-9]
DR RefSeq; NP_728139.1; NM_167605.3. [P36188-9]
DR RefSeq; NP_728140.1; NM_167606.3. [P36188-5]
DR RefSeq; NP_728141.1; NM_167607.3. [P36188-3]
DR RefSeq; NP_728142.1; NM_167608.3. [P36188-1]
DR AlphaFoldDB; P36188; -.
DR SMR; P36188; -.
DR BioGRID; 59114; 57.
DR DIP; DIP-22750N; -.
DR IntAct; P36188; 8.
DR STRING; 7227.FBpp0074298; -.
DR PaxDb; 7227-FBpp0074298; -.
DR PeptideAtlas; P36188; -.
DR DNASU; 32794; -.
DR EnsemblMetazoa; FBtr0074520; FBpp0074294; FBgn0283471. [P36188-3]
DR EnsemblMetazoa; FBtr0074521; FBpp0074295; FBgn0283471. [P36188-5]
DR EnsemblMetazoa; FBtr0074522; FBpp0074296; FBgn0283471. [P36188-7]
DR EnsemblMetazoa; FBtr0074523; FBpp0074297; FBgn0283471. [P36188-9]
DR EnsemblMetazoa; FBtr0074524; FBpp0074298; FBgn0283471. [P36188-1]
DR EnsemblMetazoa; FBtr0074525; FBpp0074299; FBgn0283471. [P36188-7]
DR EnsemblMetazoa; FBtr0074526; FBpp0074300; FBgn0283471. [P36188-9]
DR EnsemblMetazoa; FBtr0308235; FBpp0300555; FBgn0283471. [P36188-10]
DR EnsemblMetazoa; FBtr0308236; FBpp0300556; FBgn0283471. [P36188-8]
DR EnsemblMetazoa; FBtr0308237; FBpp0300557; FBgn0283471. [P36188-2]
DR GeneID; 32794; -.
DR KEGG; dme:Dmel_CG7178; -.
DR AGR; FB:FBgn0283471; -.
DR CTD; 32794; -.
DR FlyBase; FBgn0283471; wupA.
DR VEuPathDB; VectorBase:FBgn0283471; -.
DR eggNOG; KOG3977; Eukaryota.
DR GeneTree; ENSGT01030000234588; -.
DR InParanoid; P36188; -.
DR OMA; MLQVAKH; -.
DR OrthoDB; 2882372at2759; -.
DR PhylomeDB; P36188; -.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR SignaLink; P36188; -.
DR BioGRID-ORCS; 32794; 0 hits in 3 CRISPR screens.
DR ChiTaRS; wupA; fly.
DR GenomeRNAi; 32794; -.
DR PRO; PR:P36188; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0283471; Expressed in crop (Drosophila) and 32 other cell types or tissues.
DR ExpressionAtlas; P36188; baseline and differential.
DR Genevisible; P36188; DM.
DR GO; GO:0005865; C:striated muscle thin filament; HDA:FlyBase.
DR GO; GO:0005861; C:troponin complex; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:FlyBase.
DR GO; GO:0060047; P:heart contraction; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0000280; P:nuclear division; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR Gene3D; 1.20.5.350; -; 1.
DR InterPro; IPR001978; Troponin.
DR InterPro; IPR038077; Troponin_sf.
DR PANTHER; PTHR13738; TROPONIN I; 1.
DR PANTHER; PTHR13738:SF1; TROPONIN I; 1.
DR Pfam; PF00992; Troponin; 1.
DR SUPFAM; SSF90250; Troponin coil-coiled subunits; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Alternative splicing; Methylation;
KW Muscle protein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..269
FT /note="Troponin I"
FT /id="PRO_0000186159"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..171
FT /note="Troponin T-interaction"
FT /evidence="ECO:0000250"
FT REGION 189..202
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 239..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 6..66
FT /note="Missing (in isoform 1, isoform 2, isoform 3, isoform
FT 4, isoform 5, isoform 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1908472"
FT /id="VSP_006626"
FT VAR_SEQ 151..183
FT /note="GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> DTLKSLIKQHYDRIN
FT KLEDQKYDLEYVVKRKDV (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006627"
FT VAR_SEQ 151..183
FT /note="GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> DTIQSVCKDYHSKIL
FT KLESEKYDFEYDVARKDY (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006628"
FT VAR_SEQ 151..183
FT /note="GELQEICEEYYERMYICEGQKWDLEYEVRKKDW -> AELQTICKQYWQRVY
FT SLEGDKFDLEHVQKVKAQ (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_006629"
FT VAR_SEQ 249..269
FT /note="PDWSKGKPGDAKVKEEVEAEA -> IKDAAVLNKAKK (in isoform 1,
FT isoform 3, isoform 5, isoform 7 and isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_006630"
SQ 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
//
