MYSA_DROME
ID MYSA_DROME Reviewed; 1962 AA.
AC P05661; O18392; O18393; Q24412; Q7JN62; Q7JN63; Q7JQ08; Q7JQ09; Q7M4K4;
AC Q8INZ9; Q8IP00; Q8IP01; Q8IP02; Q8IP03; Q8IP04; Q8IP05; Q8IP06; Q8IP07;
AC Q8IP08; Q8IP09; Q8IP10; Q9TY21; Q9TY22; Q9TYD7; Q9VJI3;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 4.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Myosin heavy chain, muscle;
GN Name=Mhc; ORFNames=CG17927;
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 (ISOFORMS BDBBA
RP AND BABDB).
RC STRAIN=Canton-S; TISSUE=Pupae;
RX PubMed=2506434; DOI=10.1128/mcb.9.7.2957-2974.1989;
RA George E.L., Ober M.B., Emerson C.P. Jr.;
RT "Functional domains of the Drosophila melanogaster muscle myosin heavy-
RT chain gene are encoded by alternatively spliced exons.";
RL Mol. Cell. Biol. 9:2957-2974(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM M), NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 762-1962, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=2116987; DOI=10.1101/gad.4.6.885;
RA Collier V.L., Kronert W.A., O'Donnell P.T., Edwards K.A., Bernstein S.I.;
RT "Alternative myosin hinge regions are utilized in a tissue-specific fashion
RT that correlates with muscle contraction speed.";
RL Genes Dev. 4:885-895(1990).
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 [GENOMIC DNA] OF 1-264.
RX PubMed=3038896; DOI=10.1016/s0021-9258(18)61026-9;
RA Wassenberg D.R. II, Kronert W.A., O'Donnell P.T., Bernstein S.I.;
RT "Analysis of the 5' end of the Drosophila muscle myosin heavy chain gene.
RT Alternatively spliced transcripts initiate at a single site and intron
RT locations are conserved compared to myosin genes of other organisms.";
RL J. Biol. Chem. 262:10741-10747(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-614.
RC STRAIN=Canton-S; TISSUE=Embryonic muscle;
RX PubMed=1907912; DOI=10.1002/j.1460-2075.1991.tb07787.x;
RA Kronert W.A., Edwards K.A., Roche E.S., Wells L., Bernstein S.I.;
RT "Muscle-specific accumulation of Drosophila myosin heavy chains: a splicing
RT mutation in an alternative exon results in an isoform substitution.";
RL EMBO J. 10:2479-2488(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1774-1962.
RX PubMed=2431291; DOI=10.1128/mcb.6.7.2511-2519.1986;
RA Bernstein S.I., Hansen C.J., Becker K.D., Wassenberg D.R. II, Roche E.S.,
RA Donady J.J., Emerson C.P. Jr.;
RT "Alternative RNA splicing generates transcripts encoding a thorax-specific
RT isoform of Drosophila melanogaster myosin heavy chain.";
RL Mol. Cell. Biol. 6:2511-2519(1986).
RN [8]
RP PROTEIN SEQUENCE OF 1778-1938.
RA Bernstein S.I.;
RL Unpublished observations (JAN-1982).
CC -!- FUNCTION: Muscle contraction.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the
CC myofibrils.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=26;
CC Comment=Additional isoforms seem to exist. Exons 3, 7, 9, 11 and 15
CC are mutually exclusive splicing exons and exon 18 is included or
CC excluded.;
CC Name=AAAAA;
CC IsoId=P05661-1; Sequence=Displayed;
CC Name=BDBBA; Synonyms=B;
CC IsoId=P05661-2; Sequence=VSP_003329, VSP_003332, VSP_003333,
CC VSP_003335;
CC Name=BABDB; Synonyms=A;
CC IsoId=P05661-3; Sequence=VSP_003329, VSP_003333, VSP_003337,
CC VSP_003339;
CC Name=3b;
CC IsoId=P05661-4; Sequence=VSP_003329;
CC Name=7b;
CC IsoId=P05661-5; Sequence=VSP_003330;
CC Name=7c;
CC IsoId=P05661-6; Sequence=VSP_003331;
CC Name=7d;
CC IsoId=P05661-7; Sequence=VSP_003332;
CC Name=9b;
CC IsoId=P05661-8; Sequence=VSP_003333;
CC Name=9c;
CC IsoId=P05661-9; Sequence=VSP_003334;
CC Name=11b;
CC IsoId=P05661-10; Sequence=VSP_003335;
CC Name=11c;
CC IsoId=P05661-11; Sequence=VSP_003336;
CC Name=11d;
CC IsoId=P05661-12; Sequence=VSP_003337;
CC Name=11e;
CC IsoId=P05661-13; Sequence=VSP_003338;
CC Name=15b;
CC IsoId=P05661-14; Sequence=VSP_003339;
CC Name=18;
CC IsoId=P05661-15; Sequence=VSP_003340, VSP_003341;
CC Name=C;
CC IsoId=P05661-16; Sequence=VSP_003333, VSP_003336, VSP_003339;
CC Name=D;
CC IsoId=P05661-17; Sequence=VSP_003329, VSP_003333, VSP_003336,
CC VSP_003339;
CC Name=E;
CC IsoId=P05661-18; Sequence=VSP_003334, VSP_003337, VSP_003339;
CC Name=F;
CC IsoId=P05661-19; Sequence=VSP_003329, VSP_003333, VSP_003339;
CC Name=G;
CC IsoId=P05661-20; Sequence=VSP_003333, VSP_003337, VSP_003339;
CC Name=H;
CC IsoId=P05661-21; Sequence=VSP_003329, VSP_003334, VSP_003337,
CC VSP_003339;
CC Name=I;
CC IsoId=P05661-22; Sequence=VSP_003329, VSP_003334, VSP_003336,
CC VSP_003339;
CC Name=Q;
CC IsoId=P05661-23; Sequence=VSP_003330, VSP_003333, VSP_003337,
CC VSP_003339;
CC Name=K;
CC IsoId=P05661-24; Sequence=VSP_003329, VSP_003332, VSP_003338,
CC VSP_003340, VSP_003341;
CC Name=L;
CC IsoId=P05661-25; Sequence=VSP_003329, VSP_003332, VSP_003335,
CC VSP_003340, VSP_003341;
CC Name=M;
CC IsoId=P05661-26; Sequence=VSP_003329, VSP_003332, VSP_003333,
CC VSP_003335, VSP_003340, VSP_003341;
CC -!- TISSUE SPECIFICITY: Expressed in larval and adult muscles. Isoforms
CC containing exon 9a are expressed in indirect flight muscles, exons 9a
CC and 9b are expressed in jump muscles, exons 9b and 9c are expressed in
CC other larval and adult muscles. {ECO:0000269|PubMed:2116987}.
CC -!- DOMAIN: Alternative splicing exons contribute to the specialized
CC contractile activities of different muscle types. Exon 3 encodes the
CC hydrophobic pocket adjacent to the ATP-binding site, exon 9 is adjacent
CC to the actin-binding domain, exon 11 is involved in actin-binding, exon
CC 15 in the S2 hinge and exons 18 and 19 the non-coiled tail region.
CC -!- DOMAIN: Limited proteolysis of myosin heavy chain produces 1 light
CC meromyosin (LMM) and 1 heavy meromyosin (HMM). HMM can be further
CC cleaved into 2 globular subfragments (S1) and 1 rod-shaped subfragment
CC (S2). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; M61229; AAA28686.1; -; Genomic_DNA.
DR EMBL; M61229; AAA28687.1; -; Genomic_DNA.
DR EMBL; X53155; CAA37308.1; -; Genomic_DNA.
DR EMBL; X53155; CAA37309.1; -; Genomic_DNA.
DR EMBL; X53155; CAA37310.1; -; Genomic_DNA.
DR EMBL; X53155; CAA37311.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53566.4; -; Genomic_DNA.
DR EMBL; AE014134; AAN10959.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10960.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10961.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10962.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10963.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10964.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10965.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10966.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10967.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10968.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10969.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10970.1; -; Genomic_DNA.
DR EMBL; J02788; AAA28706.1; -; Genomic_DNA.
DR EMBL; J02788; AAA28707.1; -; Genomic_DNA.
DR EMBL; X60196; CAA42752.1; -; Genomic_DNA.
DR EMBL; X60196; CAA42753.1; -; Genomic_DNA.
DR EMBL; X60196; CAA42754.1; -; Genomic_DNA.
DR EMBL; M13360; AAA28708.1; -; Genomic_DNA.
DR EMBL; M13360; AAA28709.1; -; Genomic_DNA.
DR PIR; A18942; A18942.
DR PIR; A25380; A25380.
DR PIR; A28492; A28492.
DR PIR; A32491; A32491.
DR PIR; A35815; A35815.
DR PIR; B25380; B25380.
DR PIR; B32491; B32491.
DR PIR; B35815; B35815.
DR PIR; C35815; C35815.
DR PIR; D35815; D35815.
DR PIR; S16600; S16600.
DR PIR; S16601; S16601.
DR PIR; S16602; S16602.
DR RefSeq; NP_001162991.1; NM_001169520.3. [P05661-20]
DR RefSeq; NP_523587.4; NM_078863.6. [P05661-21]
DR RefSeq; NP_723999.1; NM_165181.3. [P05661-16]
DR RefSeq; NP_724000.1; NM_165182.3. [P05661-20]
DR RefSeq; NP_724001.1; NM_165183.3. [P05661-18]
DR RefSeq; NP_724002.2; NM_165184.3. [P05661-23]
DR RefSeq; NP_724003.1; NM_165185.3. [P05661-19]
DR RefSeq; NP_724004.1; NM_165186.3. [P05661-17]
DR RefSeq; NP_724005.1; NM_165187.3. [P05661-3]
DR RefSeq; NP_724006.1; NM_165188.3. [P05661-22]
DR RefSeq; NP_724007.1; NM_165189.3. [P05661-2]
DR RefSeq; NP_724008.1; NM_165190.4. [P05661-24]
DR RefSeq; NP_724009.1; NM_165191.3. [P05661-25]
DR RefSeq; NP_724010.1; NM_165192.4. [P05661-26]
DR PDB; 5W1A; X-ray; 2.23 A; A/C=1-810, A/C=2-805.
DR PDBsum; 5W1A; -.
DR AlphaFoldDB; P05661; -.
DR SMR; P05661; -.
DR BioGRID; 61014; 59.
DR IntAct; P05661; 8.
DR MINT; P05661; -.
DR STRING; 7227.FBpp0080452; -.
DR PaxDb; P05661; -.
DR PeptideAtlas; P05661; -.
DR PRIDE; P05661; -.
DR EnsemblMetazoa; FBtr0080895; FBpp0080452; FBgn0264695. [P05661-20]
DR EnsemblMetazoa; FBtr0080896; FBpp0080453; FBgn0264695. [P05661-3]
DR EnsemblMetazoa; FBtr0080897; FBpp0080454; FBgn0264695. [P05661-2]
DR EnsemblMetazoa; FBtr0080898; FBpp0080455; FBgn0264695. [P05661-16]
DR EnsemblMetazoa; FBtr0080899; FBpp0080456; FBgn0264695. [P05661-18]
DR EnsemblMetazoa; FBtr0080900; FBpp0080457; FBgn0264695. [P05661-17]
DR EnsemblMetazoa; FBtr0080901; FBpp0080458; FBgn0264695. [P05661-19]
DR EnsemblMetazoa; FBtr0080902; FBpp0080459; FBgn0264695. [P05661-21]
DR EnsemblMetazoa; FBtr0080903; FBpp0080460; FBgn0264695. [P05661-22]
DR EnsemblMetazoa; FBtr0080905; FBpp0080462; FBgn0264695. [P05661-25]
DR EnsemblMetazoa; FBtr0080906; FBpp0080463; FBgn0264695. [P05661-24]
DR EnsemblMetazoa; FBtr0080907; FBpp0080464; FBgn0264695. [P05661-26]
DR EnsemblMetazoa; FBtr0301828; FBpp0291042; FBgn0264695. [P05661-20]
DR EnsemblMetazoa; FBtr0307492; FBpp0298827; FBgn0264695. [P05661-23]
DR GeneID; 35007; -.
DR KEGG; dme:Dmel_CG17927; -.
DR CTD; 35007; -.
DR FlyBase; FBgn0264695; Mhc.
DR VEuPathDB; VectorBase:FBgn0264695; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000175738; -.
DR InParanoid; P05661; -.
DR OMA; YFVSQGK; -.
DR PhylomeDB; P05661; -.
DR SignaLink; P05661; -.
DR BioGRID-ORCS; 35007; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Mhc; fly.
DR GenomeRNAi; 35007; -.
DR PRO; PR:P05661; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0264695; Expressed in crop (Drosophila) and 37 other tissues.
DR ExpressionAtlas; P05661; baseline and differential.
DR Genevisible; P05661; DM.
DR GO; GO:0031672; C:A band; IDA:FlyBase.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:0030017; C:sarcomere; IDA:FlyBase.
DR GO; GO:0005863; C:striated muscle myosin thick filament; HDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:FlyBase.
DR GO; GO:0007527; P:adult somatic muscle development; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007427; P:epithelial cell migration, open tracheal system; IMP:FlyBase.
DR GO; GO:0060361; P:flight; IMP:FlyBase.
DR GO; GO:0040011; P:locomotion; IMP:FlyBase.
DR GO; GO:0042692; P:muscle cell differentiation; IMP:FlyBase.
DR GO; GO:0006936; P:muscle contraction; IMP:FlyBase.
DR GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
DR GO; GO:0071689; P:muscle thin filament assembly; IMP:FlyBase.
DR GO; GO:0030239; P:myofibril assembly; IMP:FlyBase.
DR GO; GO:0031033; P:myosin filament organization; IMP:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR GO; GO:0043520; P:regulation of myosin II filament assembly; IDA:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IMP:FlyBase.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Motor protein; Muscle protein; Myosin; Nucleotide-binding;
KW Reference proteome; Thick filament.
FT CHAIN 1..1962
FT /note="Myosin heavy chain, muscle"
FT /id="PRO_0000123387"
FT DOMAIN 33..82
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 86..777
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 780..809
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 656..678
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1822..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1922..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 802..1927
FT /evidence="ECO:0000255"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 69..116
FT /note="VRDIKSEKVEKVNPPKFEKIEDMADMTVLNTPCVLHNLRQRYYAKLIY ->
FT TRDLKKDLLQQVNPPKYEKAEDMSNLTYLNDASVLHNLRQRYYNKLIY (in
FT isoform 3b, isoform BDBBA, isoform BABDB, isoform D,
FT isoform F, isoform H, isoform I, isoform K, isoform L and
FT isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_003329"
FT VAR_SEQ 298..332
FT /note="DICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTD -> EYCLLSNNIYDYR
FT IVSQGKTTIPSVNDGEEWVAVD (in isoform 7b and isoform Q)"
FT /evidence="ECO:0000305"
FT /id="VSP_003330"
FT VAR_SEQ 298..332
FT /note="DICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTD -> EMVFLGQHIGDYP
FT GICQGKTRIPGVNDGEEFELTD (in isoform 7c)"
FT /evidence="ECO:0000305"
FT /id="VSP_003331"
FT VAR_SEQ 298..332
FT /note="DICLLTDNIYDYHIVSQGKVTVASIDDAEEFSLTD -> EMCFLSDNIYDYY
FT NVSQGKVTVPNMDDGEEFQLAD (in isoform 7d, isoform BDBBA,
FT isoform K, isoform L and isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_003332"
FT VAR_SEQ 469..525
FT /note="YNGFEQLCINFTNEKLQQFFNHIMFVMEQEEYKKEGINWDFIDFGMDLLACI
FT DLIEK -> YNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLA
FT CIDLIEK (in isoform 9b, isoform BDBBA, isoform BABDB,
FT isoform C, isoform D, isoform F, isoform G, isoform Q and
FT isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_003333"
FT VAR_SEQ 469..525
FT /note="YNGFEQLCINFTNEKLQQFFNHIMFVMEQEEYKKEGINWDFIDFGMDLLACI
FT DLIEK -> YNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYQREGIEWTFIDFGMDLQL
FT CIDLIEK (in isoform 9c, isoform E, isoform H and isoform
FT I)"
FT /evidence="ECO:0000305"
FT /id="VSP_003334"
FT VAR_SEQ 723..761
FT /note="YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK -> YQILNPAGI
FT VGVDDPKKCGSIILESTALDPDMYRIGHTK (in isoform 11b, isoform
FT BDBBA, isoform L and isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_003335"
FT VAR_SEQ 723..761
FT /note="YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK -> YQILNPKGI
FT KGIEDPKKCTKVLIESTELNDDQYRLGNTK (in isoform 11c, isoform C,
FT isoform D and isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_003336"
FT VAR_SEQ 723..761
FT /note="YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK -> YKIMCPKLL
FT QGVEKDKKATEIIIKFIDLPEDQYRLGNTK (in isoform 11d, isoform
FT BABDB, isoform E, isoform G, isoform H and isoform Q)"
FT /evidence="ECO:0000305"
FT /id="VSP_003337"
FT VAR_SEQ 723..761
FT /note="YQILNPRGIKDLDCPKKASKVLIESTELNEDLYRLGHTK -> YMILAPAIM
FT AAEKVAKNAAGKCLEAVGLDPDMYRIGHTK (in isoform 11e and isoform
FT K)"
FT /evidence="ECO:0000305"
FT /id="VSP_003338"
FT VAR_SEQ 1216..1241
FT /note="AEHDRQTCHNELNQTRTACDQLGRDK -> AEKEKNEYYGQLNDLRAGVDHI
FT TNEK (in isoform 15b, isoform BABDB, isoform C, isoform D,
FT isoform E, isoform F, isoform G, isoform H, isoform I and
FT isoform Q)"
FT /evidence="ECO:0000305"
FT /id="VSP_003339"
FT VAR_SEQ 1936
FT /note="P -> I (in isoform 18, isoform K, isoform L and
FT isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_003340"
FT VAR_SEQ 1937..1962
FT /note="Missing (in isoform 18, isoform K, isoform L and
FT isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_003341"
FT CONFLICT 43..44
FT /note="EK -> RE (in Ref. 5; AAA28706/AAA28707)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="E -> K (in Ref. 5; AAA28706/AAA28707)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> M (in Ref. 5; AAA28706/AAA28707)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="S -> C (in Ref. 1; AAA28686/AAA28687)"
FT /evidence="ECO:0000305"
FT CONFLICT 1922
FT /note="K -> KFRAK (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1933..1938
FT /note="SPAPRA -> GPAVSY (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 243..251
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 342..359
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 391..399
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 416..446
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 454..460
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 472..503
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 512..516
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 517..524
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 544..555
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 603..610
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 615..620
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 648..664
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 666..674
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 687..696
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 699..706
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 716..723
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 724..726
FT /evidence="ECO:0007829|PDB:5W1A"
FT TURN 728..733
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 737..746
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 755..757
FT /evidence="ECO:0007829|PDB:5W1A"
FT STRAND 759..764
FT /evidence="ECO:0007829|PDB:5W1A"
FT HELIX 768..806
FT /evidence="ECO:0007829|PDB:5W1A"
SQ SEQUENCE 1962 AA; 224465 MW; C8010B7971BB9576 CRC64;
MPKPVANQED EDPTPYLFVS LEQRRIDQSK PYDSKKSCWI PDEKEGYLLG EIKATKGDIV
SVGLQGGEVR DIKSEKVEKV NPPKFEKIED MADMTVLNTP CVLHNLRQRY YAKLIYTYSG
LFCVAINPYK RYPVYTNRCA KMYRGKRRNE VPPHIFAISD GAYVDMLTNH VNQSMLITGE
SGAGKTENTK KVIAYFATVG ASKKTDEAAK SKGSLEDQVV QTNPVLEAFG NAKTVRNDNS
SRFGKFIRIH FGPTGKLAGA DIETYLLEKA RVISQQSLER SYHIFYQIMS GSVPGVKDIC
LLTDNIYDYH IVSQGKVTVA SIDDAEEFSL TDQAFDILGF TKQEKEDVYR ITAAVMHMGG
MKFKQRGREE QAEQDGEEEG GRVSKLFGCD TAELYKNLLK PRIKVGNEFV TQGRNVQQVT
NSIGALCKGV FDRLFKWLVK KCNETLDTQQ KRQHFIGVLD IAGFEIFEYN GFEQLCINFT
NEKLQQFFNH IMFVMEQEEY KKEGINWDFI DFGMDLLACI DLIEKPMGIL SILEEESMFP
KATDQTFSEK LTNTHLGKSA PFQKPKPPKP GQQAAHFAIA HYAGCVSYNI TGWLEKNKDP
LNDTVVDQFK KSQNKLLIEI FADHAGQSGG GEQAKGGRGK KGGGFATVSS AYKEQLNSLM
TTLRSTQPHF VRCIIPNEMK QPGVVDAHLV MHQLTCNGVL EGIRICRKGF PNRMMYPDFK
MRYQILNPRG IKDLDCPKKA SKVLIESTEL NEDLYRLGHT KVFFRAGVLG QMEEFRDERL
GKIMSWMQAW ARGYLSRKGF KKLQEQRVAL KVVQRNLRKY LQLRTWPWYK LWQKVKPLLN
VSRIEDEIAR LEEKAKKAEE LHAAEVKVRK ELEALNAKLL AEKTALLDSL SGEKGALQDY
QERNAKLTAQ KNDLENQLRD IQERLTQEED ARNQLFQQKK KADQEISGLK KDIEDLELNV
QKAEQDKATK DHQIRNLNDE IAHQDELINK LNKEKKMQGE TNQKTGEELQ AAEDKINHLN
KVKAKLEQTL DELEDSLERE KKVRGDVEKS KRKVEGDLKL TQEAVADLER NKKELEQTIQ
RKDKELSSIT AKLEDEQVVV LKHQRQIKEL QARIEELEEE VEAERQARAK AEKQRADLAR
ELEELGERLE EAGGATSAQI ELNKKREAEL SKLRRDLEEA NIQHESTLAN LRKKHNDAVA
EMAEQVDQLN KLKAKAEHDR QTCHNELNQT RTACDQLGRD KAAQEKIAKQ LQHTLNEVQS
KLDETNRTLN DFDASKKKLS IENSDLLRQL EEAESQVSQL SKIKISLTTQ LEDTKRLADE
ESRERATLLG KFRNLEHDLD NLREQVEEEA EGKADLQRQL SKANAEAQVW RSKYESDGVA
RSEELEEAKR KLQARLAEAE ETIESLNQKC IGLEKTKQRL STEVEDLQLE VDRANAIANA
AEKKQKAFDK IIGEWKLKVD DLAAELDASQ KECRNYSTEL FRLKGAYEEG QEQLEAVRRE
NKNLADEVKD LLDQIGEGGR NIHEIEKARK RLEAEKDELQ AALEEAEAAL EQEENKVLRA
QLELSQVRQE IDRRIQEKEE EFENTRKNHQ RALDSMQASL EAEAKGKAEA LRMKKKLEAD
INELEIALDH ANKANAEAQK NIKRYQQQLK DIQTALEEEQ RARDDAREQL GISERRANAL
QNELEESRTL LEQADRGRRQ AEQELADAHE QLNEVSAQNA SISAAKRKLE SELQTLHSDL
DELLNEAKNS EEKAKKAMVD AARLADELRA EQDHAQTQEK LRKALEQQIK ELQVRLDEAE
ANALKGGKKA IQKLEQRVRE LENELDGEQR RHADAQKNLR KSERRVKELS FQSEEDRKNH
ERMQDLVDKL QQKIKTYKRQ IEEAEEIAAL NLAKFRKAQQ ELEEAEERAD LAEQAISKFR
AKGRAGSVGR GASPAPRATS VRPQFDGLAF PPRFDLAPEN EF
