TPM4_DROME
ID TPM4_DROME Reviewed; 518 AA.
AC P49455; P49456; Q24425; Q24426; Q7KSH9; Q7KSI0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Tropomyosin-1, isoforms 33/34;
DE AltName: Full=Tropomyosin II;
GN Name=Tm1; Synonyms=TmII; ORFNames=CG4898;
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], AND ALTERNATIVE SPLICING.
RC TISSUE=Embryo, and Pupae;
RX PubMed=2851721; DOI=10.1128/mcb.8.9.3591-3602.1988;
RA Hanke P.D., Storti R.V.;
RT "The Drosophila melanogaster tropomyosin II gene produces multiple proteins
RT by use of alternative tissue-specific promoters and alternative splicing.";
RL Mol. Cell. Biol. 8:3591-3602(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R; TISSUE=Pupae;
RX PubMed=3097506; DOI=10.1128/mcb.6.6.1965-1973.1986;
RA Karlik C.C., Fyrberg E.A.;
RT "Two Drosophila melanogaster tropomyosin genes: structural and functional
RT aspects.";
RL Mol. Cell. Biol. 6:1965-1973(1986).
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).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC a central role in the calcium dependent regulation of muscle
CC contraction.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=33; Synonyms=9C, K;
CC IsoId=P49455-1; Sequence=Displayed;
CC Name=34; Synonyms=9B, F;
CC IsoId=P49455-2; Sequence=VSP_006623, VSP_006624, VSP_006625;
CC Name=9A;
CC IsoId=P06754-3; Sequence=External;
CC Name=A; Synonyms=Cytoskeletal, Non-muscle;
CC IsoId=P06754-2; Sequence=External;
CC Name=B;
CC IsoId=P06754-4; Sequence=External;
CC Name=D; Synonyms=9D, G, J, Muscle;
CC IsoId=P06754-1; Sequence=External;
CC Name=L;
CC IsoId=P06754-5; Sequence=External;
CC -!- TISSUE SPECIFICITY: Both isoforms are only expressed in indirect flight
CC muscles.
CC -!- DEVELOPMENTAL STAGE: Both isoforms are expressed during pupal and adult
CC stages.
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed by 2
CC polypeptide chains. The sequence exhibits a prominent seven-residues
CC periodicity.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
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DR EMBL; X76208; CAA53800.1; -; Genomic_DNA.
DR EMBL; X76208; CAA53801.1; -; Genomic_DNA.
DR EMBL; K02620; AAA28967.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L00355; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; L00356; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; L00357; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; L00358; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; L00359; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; L00360; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; L00362; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; M12840; AAA28967.1; JOINED; Genomic_DNA.
DR EMBL; K02621; AAA28968.1; -; Genomic_DNA.
DR EMBL; M12840; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; L00355; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; L00356; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; L00357; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; L00358; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; L00359; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; L00360; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; L00362; AAA28968.1; JOINED; Genomic_DNA.
DR EMBL; AE014297; AAN13647.2; -; Genomic_DNA.
DR EMBL; AE014297; AAS65155.1; -; Genomic_DNA.
DR PIR; B25242; B25242.
DR RefSeq; NP_732005.2; NM_169637.4. [P49455-2]
DR RefSeq; NP_996217.1; NM_206495.2. [P49455-1]
DR AlphaFoldDB; P49455; -.
DR SMR; P49455; -.
DR BioGRID; 66916; 29.
DR IntAct; P49455; 25.
DR Allergome; 1517; Dro m 7.
DR Allergome; 4081; Dro m 7.0103.
DR PaxDb; P49455; -.
DR PRIDE; P49455; -.
DR DNASU; 41852; -.
DR EnsemblMetazoa; FBtr0089957; FBpp0088896; FBgn0003721. [P49455-1]
DR EnsemblMetazoa; FBtr0089959; FBpp0088898; FBgn0003721. [P49455-2]
DR GeneID; 41852; -.
DR KEGG; dme:Dmel_CG4898; -.
DR CTD; 41852; -.
DR FlyBase; FBgn0003721; Tm1.
DR VEuPathDB; VectorBase:FBgn0003721; -.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_604422_0_0_1; -.
DR InParanoid; P49455; -.
DR PhylomeDB; P49455; -.
DR Reactome; R-DME-9013424; RHOV GTPase cycle.
DR SignaLink; P49455; -.
DR BioGRID-ORCS; 41852; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41852; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003721; Expressed in crop (Drosophila) and 67 other tissues.
DR ExpressionAtlas; P49455; baseline and differential.
DR Genevisible; P49455; DM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0070865; C:investment cone; IDA:FlyBase.
DR GO; GO:0043186; C:P granule; IDA:FlyBase.
DR GO; GO:0030017; C:sarcomere; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; TAS:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:FlyBase.
DR GO; GO:0019894; F:kinesin binding; IPI:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR GO; GO:0007315; P:pole plasm assembly; NAS:FlyBase.
DR GO; GO:0045451; P:pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0010591; P:regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0055093; P:response to hyperoxia; IMP:FlyBase.
DR GO; GO:0043149; P:stress fiber assembly; IMP:FlyBase.
DR InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Muscle protein; Reference proteome.
FT CHAIN 1..518
FT /note="Tropomyosin-1, isoforms 33/34"
FT /id="PRO_0000205685"
FT REGION 101..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..267
FT /evidence="ECO:0000250"
FT COMPBIAS 290..304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..378
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 259..293
FT /note="DLIVEKERYCMIGDSLDEAFVDLIKGLEPFWNPRN -> EMIKEIEHYALVG
FT DQLDWTFVEMMGMPPFYNERY (in isoform 34)"
FT /evidence="ECO:0000305"
FT /id="VSP_006623"
FT VAR_SEQ 300..367
FT /note="KLPTPTPEELAAMEEARAAAEAAAAAEAEAAEAAAAAGEAGPDGAPAAPGEE
FT KAPAKEPTPPKEPTPP -> ELTEEEKAALEAAAIAEAEAKARAEELAALGEEAGAEAG
FT EGGAPAEGAAPGEPGAATEPGVEAPPAEPERIPT (in isoform 34)"
FT /evidence="ECO:0000305"
FT /id="VSP_006624"
FT VAR_SEQ 391..518
FT /note="KNYEPPPPGSEPEPVPAAEGEAAPAAEGAAPPAEGAAPPAEGAVPPADGAAP
FT PAEGAAPAAEGAAPPADGAAPPAEAAAAPADAAAPAAEAAPAEAPAAEATAAEAPPAEA
FT APAEAAPAAAEGEAPPA -> RNAEPGDFAPPAEAAPAEGAPPAEGAPAAEGAAPAEGA
FT PAAEGAPPAEGAPAPAPAEGEAAPPAPAAEGDAAAAPPPPPAEGEAAPAPAEGEAPPAE
FT AAPAAEAPPA (in isoform 34)"
FT /evidence="ECO:0000305"
FT /id="VSP_006625"
FT CONFLICT 106..114
FT /note="LGSATAKLS -> SASAIQLAA (in Ref. 2; AAA28967)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="A -> S (in Ref. 2; AAA28967/AAA28968)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="A -> AMVEADLERAEERA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="V -> L (in Ref. 2; AAA28967/AAA28968)"
FT /evidence="ECO:0000305"
FT CONFLICT 298..299
FT /note="TP -> A (in Ref. 2; AAA28967)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="P -> A (in Ref. 1; CAA53800 and 2; AAA28968)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="P -> A (in Ref. 2; AAA28968)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 54585 MW; F431A313DE911D87 CRC64;
MDAIKKKMQA MKVDKDGALE RALVCEQEAR DANTRAEKAE EEARQLQKKI QTVENELDQT
QEALTLVTGK LEEKNKALQN AESEVAALNR RIQLLEEDLE RSEERLGSAT AKLSEASQAA
DESERARKIL ENRALADEER MDALENQLKE ARFLAEEADK KYDEVARKLA MVEADLERAE
ERAEQGENKI VELEEELRVV GNNLKSLEVS EEKANQREEE YKNQIKTLNT RLKEAEARAE
FAERSVQKLQ KEVDRLEDDL IVEKERYCMI GDSLDEAFVD LIKGLEPFWN PRNPKPPTPK
LPTPTPEELA AMEEARAAAE AAAAAEAEAA EAAAAAGEAG PDGAPAAPGE EKAPAKEPTP
PKEPTPPPPP PPPFEYSIDL PPEGAEVPYV KNYEPPPPGS EPEPVPAAEG EAAPAAEGAA
PPAEGAAPPA EGAVPPADGA APPAEGAAPA AEGAAPPADG AAPPAEAAAA PADAAAPAAE
AAPAEAPAAE ATAAEAPPAE AAPAEAAPAA AEGEAPPA
