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-APR-2013, entry version 117.
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;
OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; 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;
RA Karlik C.C., Fyrberg E.A.;
RT "Two Drosophila melanogaster tropomyosin genes: structural and
RT functional 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;
RA Hanke P.D., Lepinske H.M., Storti R.V.;
RT "Characterization of a Drosophila cDNA clone that encodes a 252-amino
RT acid 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.,
RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA 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.,
RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA 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.,
RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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;
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.,
RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a
RT systematic 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;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA Rubin G.M., Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Tropomyosin, in association with the troponin complex,
CC plays a central role in the calcium dependent regulation of muscle
CC contraction.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- INTERACTION:
CC Self; NbExp=1; IntAct=EBI-176070, EBI-176070;
CC Q9VPP2:CG4213; NbExp=1; IntAct=EBI-176070, EBI-195064;
CC Q9VCZ7:CG5376; NbExp=1; IntAct=EBI-176070, EBI-99019;
CC Q7KS38:RpS19b; NbExp=1; IntAct=EBI-176070, EBI-522741;
CC Q8T414:SIP3; NbExp=1; IntAct=EBI-176070, EBI-95177;
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 Note=No experimental confirmation available;
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 Note=No experimental confirmation available;
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
CC isoform is expressed at late embryogenesis through to adulthood,
CC highest expression level being late embryo and early larval
CC stages.
CC -!- DOMAIN: The molecule is in a coiled coil structure that is formed
CC by 2 polypeptide chains. The sequence exhibits a prominent seven-
CC residues periodicity.
CC -!- SIMILARITY: Belongs to the tropomyosin family.
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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.
DR RefSeq; NP_732001.3; NM_169633.5.
DR RefSeq; NP_732002.1; NM_169634.3.
DR RefSeq; NP_732003.1; NM_169635.3.
DR RefSeq; NP_732004.1; NM_169636.3.
DR RefSeq; NP_996216.1; NM_206494.3.
DR UniGene; Dm.19116; -.
DR ProteinModelPortal; P06754; -.
DR SMR; P06754; 1-337.
DR IntAct; P06754; 6.
DR MINT; MINT-1009663; -.
DR Allergome; 1517; Dro m 7.
DR Allergome; 4079; Dro m 7.0101.
DR Allergome; 4182; Dro m 7.0112.
DR PaxDb; P06754; -.
DR GeneID; 41852; -.
DR KEGG; dme:Dmel_CG4898; -.
DR CTD; 41852; -.
DR FlyBase; FBgn0003721; Tm1.
DR eggNOG; NOG304012; -.
DR InParanoid; P06754; -.
DR KO; K10373; -.
DR OMA; ANTRADE; -.
DR OrthoDB; EOG4GMSD4; -.
DR ChiTaRS; Tm1; drosophila.
DR GenomeRNAi; 41852; -.
DR NextBio; 825903; -.
DR GermOnline; CG4898; Drosophila melanogaster.
DR GO; GO:0070865; C:investment cone; IDA:FlyBase.
DR GO; GO:0030017; C:sarcomere; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IDA:FlyBase.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; 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 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; Complete proteome;
KW Cytoplasm; Cytoskeleton; Muscle protein; Reference proteome.
FT CHAIN 1 339 Tropomyosin-1, isoforms 9A/A/B.
FT /FTId=PRO_0000205684.
FT COILED 14 285 By similarity.
FT VAR_SEQ 1 86 Missing (in isoform A).
FT /FTId=VSP_006617.
FT VAR_SEQ 81 134 Missing (in isoform D, isoform L and
FT isoform 9A).
FT /FTId=VSP_015697.
FT VAR_SEQ 180 242 ARKILENRALADEERMDALENQLKEARFLAEEADKKYDEVA
FT RKLAMVEADLERAEERAEQGEN -> IRKALENRTNMEDDK
FT VALLENQLAQAKLIAEEADKKYEEVARKLVLMEQDLERSEE
FT KVELSES (in isoform L and isoform A).
FT /FTId=VSP_006619.
FT VAR_SEQ 269 285 NQREEEYKNQIKTLNTR -> TQKEETFETQIKVLDHS
FT (in isoform L and isoform A).
FT /FTId=VSP_006621.
FT VAR_SEQ 315 339 VLEKERYKDIGDDLDTAFVELILKE -> LNVRGKNKLLQE
FT EMEATLHDIQNM (in isoform L, isoform A and
FT isoform 9A).
FT /FTId=VSP_006622.
FT CONFLICT 90 91 SI -> RL (in Ref. 3).
FT CONFLICT 160 168 LGSATAKLS -> SASAIQLAA (in Ref. 2;
FT AAA28966).
FT CONFLICT 173 173 A -> S (in Ref. 2; AAA28966/AAA28969).
FT CONFLICT 237 237 A -> AMVEADLERAEERA (in Ref. 2).
FT CONFLICT 253 253 V -> L (in Ref. 2; AAA28966/AAA28969).
FT CONFLICT 268 268 A -> S (in Ref. 1; AAA28975).
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
//
