TPM2_DROME
ID TPM2_DROME Reviewed; 284 AA.
AC P09491; A0AVW5; A4V2Y6; P09490; Q24408; Q24427; Q24428; Q8SZ65; Q9VF95;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Tropomyosin-2;
DE AltName: Full=Tropomyosin I;
GN Name=Tm2; Synonyms=TmI; ORFNames=CG4843;
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, Larva, and Pupae;
RX PubMed=6202423; DOI=10.1016/0092-8674(84)90377-5;
RA Karlik C.C., Mahaffey J.W., Coutu M.D., Fyrberg E.A.;
RT "Organization of contractile protein genes within the 88F subdivision of
RT the D. melanogaster third chromosome.";
RL Cell 37:469-481(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=3079761; DOI=10.1016/s0021-9258(17)36169-0;
RA Basi G.S., Storti R.V.;
RT "Structure and DNA sequence of the tropomyosin I gene from Drosophila
RT melanogaster.";
RL J. Biol. Chem. 261:817-827(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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EMBRYONIC).
RC STRAIN=Berkeley; TISSUE=Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS EMBRYONIC AND THORACIC).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Booth B., Frise E., Park S., Kapadia B.,
RA Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 258-284.
RX PubMed=4000944; DOI=10.1093/nar/13.5.1763;
RA Boardman M., Basi G.S., Storti R.V.;
RT "Multiple polyadenylation sites in a Drosophila tropomyosin gene are used
RT to generate functional mRNAs.";
RL Nucleic Acids Res. 13:1763-1776(1985).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19567471; DOI=10.1242/jcs.050880;
RA Sahota V.K., Grau B.F., Mansilla A., Ferrus A.;
RT "Troponin I and Tropomyosin regulate chromosomal stability and cell
RT polarity.";
RL J. Cell Sci. 122:2623-2631(2009).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex, plays
CC a central role in the calcium dependent regulation of muscle
CC contraction. May also regulate motor systems required to maintain
CC nuclear integrity and apico-basal polarity during embryogenesis.
CC {ECO:0000269|PubMed:19567471}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Thoracic; Synonyms=127, C, t;
CC IsoId=P09491-1; Sequence=Displayed;
CC Name=Embryonic; Synonyms=129, A, B, e;
CC IsoId=P09491-2; Sequence=VSP_006616;
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 -!- DISRUPTION PHENOTYPE: Pre-cellular embryos exhibit abnormal nuclear
CC divisions with frequent loss of chromosome fragments. During
CC cellularization, apico-basal polarity is also disrupted.
CC {ECO:0000269|PubMed:19567471}.
CC -!- SIMILARITY: Belongs to the tropomyosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK30920.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA26142.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; K02622; AAA28970.1; -; Genomic_DNA.
DR EMBL; K02623; AAA28971.1; -; Genomic_DNA.
DR EMBL; K02622; AAA28971.1; JOINED; Genomic_DNA.
DR EMBL; K03277; AAA28973.1; -; Genomic_DNA.
DR EMBL; K03277; AAA28974.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13652.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13653.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13654.2; -; Genomic_DNA.
DR EMBL; AY071087; AAL48709.1; -; mRNA.
DR EMBL; BT029283; ABK30920.1; ALT_FRAME; mRNA.
DR EMBL; BT044580; ACI16542.1; -; mRNA.
DR EMBL; X02220; CAA26142.1; ALT_SEQ; Genomic_DNA.
DR PIR; A25624; A25624.
DR PIR; B25624; B25624.
DR RefSeq; NP_001262592.1; NM_001275663.1. [P09491-2]
DR RefSeq; NP_001262593.1; NM_001275664.1. [P09491-2]
DR RefSeq; NP_001287337.1; NM_001300408.1. [P09491-2]
DR RefSeq; NP_524361.4; NM_079637.5. [P09491-2]
DR RefSeq; NP_732012.1; NM_169644.2. [P09491-2]
DR RefSeq; NP_732013.2; NM_169645.4. [P09491-1]
DR AlphaFoldDB; P09491; -.
DR SMR; P09491; -.
DR BioGRID; 66917; 76.
DR DIP; DIP-21556N; -.
DR IntAct; P09491; 3.
DR STRING; 7227.FBpp0082535; -.
DR Allergome; 1517; Dro m 7.
DR Allergome; 4080; Dro m 7.0102.
DR Allergome; 4174; Dro m 7.0104.
DR Allergome; 4175; Dro m 7.0105.
DR PaxDb; P09491; -.
DR PRIDE; P09491; -.
DR DNASU; 41853; -.
DR EnsemblMetazoa; FBtr0083078; FBpp0082535; FBgn0004117. [P09491-2]
DR EnsemblMetazoa; FBtr0083079; FBpp0082536; FBgn0004117. [P09491-2]
DR EnsemblMetazoa; FBtr0083080; FBpp0089270; FBgn0004117. [P09491-1]
DR EnsemblMetazoa; FBtr0333920; FBpp0306048; FBgn0004117. [P09491-2]
DR EnsemblMetazoa; FBtr0339530; FBpp0308613; FBgn0004117. [P09491-2]
DR EnsemblMetazoa; FBtr0345212; FBpp0311407; FBgn0004117. [P09491-2]
DR GeneID; 41853; -.
DR KEGG; dme:Dmel_CG4843; -.
DR UCSC; CG4843-RB; d. melanogaster.
DR CTD; 41853; -.
DR FlyBase; FBgn0004117; Tm2.
DR VEuPathDB; VectorBase:FBgn0004117; -.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR HOGENOM; CLU_055027_0_2_1; -.
DR InParanoid; P09491; -.
DR OMA; EDKCKQM; -.
DR PhylomeDB; P09491; -.
DR Reactome; R-DME-9013424; RHOV GTPase cycle.
DR SignaLink; P09491; -.
DR BioGRID-ORCS; 41853; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41853; -.
DR PRO; PR:P09491; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004117; Expressed in crop (Drosophila) and 34 other tissues.
DR ExpressionAtlas; P09491; baseline and differential.
DR Genevisible; P09491; DM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IGI: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 Alternative splicing; Coiled coil; Muscle protein; Reference proteome;
KW Repeat.
FT CHAIN 1..284
FT /note="Tropomyosin-2"
FT /id="PRO_0000205686"
FT REGION 82..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..284
FT /evidence="ECO:0000250"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 259..284
FT /note="RLFNEKEKYKAICDDLDQTFAELTGY -> ELGINKDRYKSLADEMDSTFAE
FT LAGY (in isoform Embryonic)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.6"
FT /id="VSP_006616"
FT CONFLICT 11
FT /note="M -> V (in Ref. 1; AAA28970/AAA28971)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="Q -> L (in Ref. 1; AAA28970/AAA28971)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="I -> T (in Ref. 1; AAA28970/AAA28971)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="R -> D (in Ref. 1; AAA28970/AAA28971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32981 MW; 07AD03FDD304EA5F CRC64;
MDAIKKKMQA MKLEKDNAID KADTCENQAK DANSRADKLN EEVRDLEKKF VQVEIDLVTA
KEQLEKANTE LEEKEKLLTA TESEVATQNR KVQQIEEDLE KSEERSTTAQ QKLLEATQSA
DENNRMCKVL ENRSQQDEER MDQLTNQLKE ARMLAEDADT KSDEVSRKLA FVEDELEVAE
DRVRSGESKI MELEEELKVV GNSLKSLEVS EEKANQRVEE FKREMKTLSI KLKEAEQRAE
HAEKQVKRLQ KEVDRLEDRL FNEKEKYKAI CDDLDQTFAE LTGY
