TPM1_DROME
ID TPM1_DROME Reviewed; 339 AA.
AC P06754; A4V2Y4; P09492; Q7KSH8; Q7KSI1; Q95SZ3; Q9VF96; Q9VF97;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Tropomyosin-1, isoforms 9A/A/B;
DE AltName: Full=Cytoskeletal tropomyosin;
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 [MRNA] (ISOFORM D).
RX PubMed=3803921; DOI=10.1016/0378-1119(86)90256-8;
RA Hanke P.D., Storti R.V.;
RT "Nucleotide sequence of a cDNA clone encoding a Drosophila muscle
RT tropomyosin II isoform.";
RL Gene 45:211-214(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [MRNA] (ISOFORM A).
RC TISSUE=Embryo, and Pupae;
RX PubMed=3693358; DOI=10.1016/s0021-9258(18)45387-2;
RA Hanke P.D., Lepinske H.M., Storti R.V.;
RT "Characterization of a Drosophila cDNA clone that encodes a 252-amino acid
RT non-muscle tropomyosin isoform.";
RL J. Biol. Chem. 262:17370-17373(1987).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
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 [7]
RP INTERACTION WITH UNC-89.
RX PubMed=26251439; DOI=10.1242/jcs.170639;
RA Katzemich A., West R.J., Fukuzawa A., Sweeney S.T., Gautel M., Sparrow J.,
RA Bullard B.;
RT "Binding partners of the kinase domains in Drosophila obscurin and their
RT effect on the structure of the flight muscle.";
RL J. Cell Sci. 128:3386-3397(2015).
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 (Probable). May interact with Unc-89 (via protein
CC kinase domain 2) (PubMed:26251439). {ECO:0000269|PubMed:26251439,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 9A]: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=B;
CC IsoId=P06754-4; Sequence=Displayed;
CC Name=9A;
CC IsoId=P06754-3; Sequence=VSP_015697, VSP_006622;
CC Name=A; Synonyms=Cytoskeletal, Non-muscle;
CC IsoId=P06754-2; Sequence=VSP_006617, VSP_006619, VSP_006621,
CC VSP_006622;
CC Name=D; Synonyms=9D, G, J, Muscle;
CC IsoId=P06754-1; Sequence=VSP_015697;
CC Name=L;
CC IsoId=P06754-5; Sequence=VSP_015697, VSP_006619, VSP_006621,
CC VSP_006622;
CC Name=33; Synonyms=9C, K;
CC IsoId=P49455-1; Sequence=External;
CC Name=34; Synonyms=9B, F;
CC IsoId=P49455-2; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Isoform 9A is expressed both maternally and
CC zygotically during embryogenesis and mid pupal stages. Muscle isoform
CC is expressed at late embryogenesis through to adulthood, highest
CC expression level being late embryo and early larval 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; M15466; AAA28975.1; -; mRNA.
DR EMBL; L00363; AAA28966.1; -; Genomic_DNA.
DR EMBL; M12840; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; L00355; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; L00356; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; L00357; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; L00358; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; L00359; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; L00360; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; L00362; AAA28966.1; JOINED; Genomic_DNA.
DR EMBL; M13023; AAA28969.1; -; Genomic_DNA.
DR EMBL; M12840; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; L00355; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; L00356; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; L00357; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; L00358; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; L00359; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; L00360; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; L00362; AAA28969.1; JOINED; Genomic_DNA.
DR EMBL; J03502; AAA28972.1; -; mRNA.
DR EMBL; AE014297; AAF55163.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF55164.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13644.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13645.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13646.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65156.1; -; Genomic_DNA.
DR EMBL; AY060414; AAL25453.1; -; mRNA.
DR PIR; A25561; A25561.
DR PIR; A28449; A28449.
DR PIR; C25242; C25242.
DR RefSeq; NP_524360.2; NM_079636.4. [P06754-2]
DR RefSeq; NP_732001.3; NM_169633.5. [P06754-1]
DR RefSeq; NP_732002.1; NM_169634.3. [P06754-1]
DR RefSeq; NP_732003.1; NM_169635.3. [P06754-1]
DR RefSeq; NP_732004.1; NM_169636.3. [P06754-1]
DR RefSeq; NP_996216.1; NM_206494.3. [P06754-5]
DR AlphaFoldDB; P06754; -.
DR SMR; P06754; -.
DR BioGRID; 66916; 29.
DR IntAct; P06754; 8.
DR STRING; 7227.FBpp0088904; -.
DR Allergome; 1517; Dro m 7.
DR Allergome; 4079; Dro m 7.0101.
DR Allergome; 4182; Dro m 7.0112.
DR PeptideAtlas; P06754; -.
DR PRIDE; P06754; -.
DR DNASU; 41852; -.
DR EnsemblMetazoa; FBtr0089960; FBpp0088899; FBgn0003721. [P06754-2]
DR EnsemblMetazoa; FBtr0089964; FBpp0088903; FBgn0003721. [P06754-1]
DR EnsemblMetazoa; FBtr0089967; FBpp0088906; FBgn0003721. [P06754-1]
DR EnsemblMetazoa; FBtr0089968; FBpp0089024; FBgn0003721. [P06754-5]
DR EnsemblMetazoa; FBtr0301959; FBpp0291171; FBgn0003721. [P06754-1]
DR EnsemblMetazoa; FBtr0305654; FBpp0296934; FBgn0003721. [P06754-1]
DR GeneID; 41852; -.
DR UCSC; CG4898-RG; d. melanogaster.
DR CTD; 41852; -.
DR FlyBase; FBgn0003721; Tm1.
DR VEuPathDB; VectorBase:FBgn0003721; -.
DR eggNOG; KOG1003; Eukaryota.
DR GeneTree; ENSGT01030000234542; -.
DR SignaLink; P06754; -.
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; P06754; baseline and differential.
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: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:0019901; F:protein kinase binding; IPI:UniProtKB.
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 InterPro; IPR000533; Tropomyosin.
DR Pfam; PF00261; Tropomyosin; 1.
DR Pfam; PF12718; Tropomyosin_1; 1.
DR PRINTS; PR00194; TROPOMYOSIN.
DR PROSITE; PS00326; TROPOMYOSIN; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Muscle protein; Reference proteome.
FT CHAIN 1..339
FT /note="Tropomyosin-1, isoforms 9A/A/B"
FT /id="PRO_0000205684"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..285
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..86
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:3693358"
FT /id="VSP_006617"
FT VAR_SEQ 81..134
FT /note="Missing (in isoform D, isoform L and isoform 9A)"
FT /evidence="ECO:0000303|PubMed:3803921"
FT /id="VSP_015697"
FT VAR_SEQ 180..242
FT /note="ARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVARKLAMVEADLE
FT RAEERAEQGEN -> IRKALENRTNMEDDKVALLENQLAQAKLIAEEADKKYEEVARKL
FT VLMEQDLERSEEKVELSES (in isoform L and isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:3693358"
FT /id="VSP_006619"
FT VAR_SEQ 269..285
FT /note="NQREEEYKNQIKTLNTR -> TQKEETFETQIKVLDHS (in isoform L
FT and isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:3693358"
FT /id="VSP_006621"
FT VAR_SEQ 315..339
FT /note="VLEKERYKDIGDDLDTAFVELILKE -> LNVRGKNKLLQEEMEATLHDIQN
FT M (in isoform L, isoform A and isoform 9A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:3693358"
FT /id="VSP_006622"
FT CONFLICT 90..91
FT /note="SI -> RL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 160..168
FT /note="LGSATAKLS -> SASAIQLAA (in Ref. 2; AAA28966)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="A -> S (in Ref. 2; AAA28966/AAA28969)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="A -> AMVEADLERAEERA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="V -> L (in Ref. 2; AAA28966/AAA28969)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="A -> S (in Ref. 1; AAA28975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 39325 MW; FDF05A09D3696E04 CRC64;
MDAIKKKMQA MKVDKDGALE RALVCEQEAR DANTRAEKAE EEARQLQKKI QTVENELDQT
QEALTLVTGK LEEKNKALQN KKKTTKMTTS IPQGTLLDVL KKKMRQTKEE MEKYKDECEE
FHKRLQLEVV RREEAESEVA ALNRRIQLLE EDLERSEERL GSATAKLSEA SQAADESERA
RKILENRALA DEERMDALEN QLKEARFLAE EADKKYDEVA RKLAMVEADL ERAEERAEQG
ENKIVELEEE LRVVGNNLKS LEVSEEKANQ REEEYKNQIK TLNTRLKEAE ARAEFAERSV
QKLQKEVDRL EDDLVLEKER YKDIGDDLDT AFVELILKE
