MYO7A_DROME
ID MYO7A_DROME Reviewed; 2167 AA.
AC Q9V3Z6; Q6NNF6; Q8T0A9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Myosin-VIIa;
DE Short=DmVIIa;
DE AltName: Full=Protein crinkled;
GN Name=ck {ECO:0000312|EMBL:AAF53435.1}; ORFNames=CG7595;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Berkeley {ECO:0000269|PubMed:15579689};
RC TISSUE=Embryo {ECO:0000269|PubMed:15579689};
RX PubMed=15579689; DOI=10.1534/genetics.104.026369;
RA Kiehart D.P., Franke J.D., Chee M.K., Montague R.A., Chen T.-L., Roote J.,
RA Ashburner M.;
RT "Drosophila crinkled, mutations of which disrupt morphogenesis and cause
RT lethality, encodes fly myosin VIIA.";
RL Genetics 168:1337-1352(2004).
RN [2] {ECO:0000312|EMBL:AAF53435.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF53435.1}
RP GENOME REANNOTATION.
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 [4] {ECO:0000312|EMBL:AAR96124.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15886106; DOI=10.1016/j.cub.2005.03.050;
RA Todi S.V., Franke J.D., Kiehart D.P., Eberl D.F.;
RT "Myosin VIIA defects, which underlie the Usher 1B syndrome in humans, lead
RT to deafness in Drosophila.";
RL Curr. Biol. 15:862-868(2005).
RN [6] {ECO:0000305}
RP FUNCTION, AND SUBUNIT.
RX PubMed=16585515; DOI=10.1073/pnas.0509935103;
RA Yang Y., Kovacs M., Sakamoto T., Zhang F., Kiehart D.P., Sellers J.R.;
RT "Dimerized Drosophila myosin VIIa: a processive motor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5746-5751(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1651; SER-1654 AND THR-2045,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION, INTERACTION WITH CAD99C, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=25236597; DOI=10.1242/jcs.099242;
RA Glowinski C., Liu R.H., Chen X., Darabie A., Godt D.;
RT "Myosin VIIA regulates microvillus morphogenesis and interacts with
RT cadherin Cad99C in Drosophila oogenesis.";
RL J. Cell Sci. 127:4821-4832(2014).
RN [9]
RP FUNCTION, INTERACTION WITH CAD99C; SANS AND ZIP, AND DISRUPTION PHENOTYPE.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity
CC (PubMed:16585515). Unconventional myosins serve in intracellular
CC movements: can function in cells as a single-molecule cargo transporter
CC (PubMed:16585515). A very slow and high-duty-ratio motor, may be
CC suitable for tension maintenance of actin filaments (PubMed:16585515).
CC Their highly divergent tails are presumed to bind to membranous
CC compartments, which would be moved relative to actin filaments
CC (PubMed:15579689). Plays a key role in the formation of cellular
CC projections and other actin-based functions required for embryonic and
CC larval viability (PubMed:15579689, PubMed:16585515). Necessary for
CC auditory transduction: plays a role in Johnston's organ organization by
CC functioning in scolopidial apical attachment and therefore to acoustic
CC stimulus propagation from the antenna a2/a3 joint to transducing
CC elements (PubMed:15886106, PubMed:27331610). Interaction with the
CC myosin zip may be important for its function in scolopidial apical
CC attachment (PubMed:27331610). During oogenesis it has Cad99c-dependent
CC and Cad99c-independent roles in regulating the shape and spacing of the
CC follicle cell microvilli which secrete eggshell material such as the
CC vitelline membrane (PubMed:25236597). May be required for the normal
CC expression of Cad99c in the follicle cell microvilli (PubMed:25236597).
CC {ECO:0000269|PubMed:15579689, ECO:0000269|PubMed:15886106,
CC ECO:0000269|PubMed:16585515, ECO:0000269|PubMed:25236597,
CC ECO:0000269|PubMed:27331610}.
CC -!- SUBUNIT: Homodimerizes in a two headed molecule through the formation
CC of a coiled-coil rod (PubMed:16585515). Homodimers motility is
CC approximately 8-10 times slower than that of myosin V, and its step
CC size is 30 nm, which is consistent with the presence of five IQ motifs
CC in its neck region (PubMed:16585515). Interacts with Cad99C (via the
CC cytoplasmic domain) (PubMed:25236597, PubMed:27331610). Interacts with
CC zip and Sans (PubMed:27331610). {ECO:0000269|PubMed:16585515,
CC ECO:0000269|PubMed:25236597, ECO:0000269|PubMed:27331610}.
CC -!- INTERACTION:
CC Q9V3Z6; P62152: Cam; NbExp=3; IntAct=EBI-15762145, EBI-182924;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15886106,
CC ECO:0000269|PubMed:25236597}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:25236597}. Cell projection, microvillus
CC {ECO:0000269|PubMed:25236597}. Note=In scolopale cells (radially
CC organized units in the Johnston's organ), protein is concentrated along
CC actin-rich scolopale rods and more apically near scolopale cell-cap
CC cell junctions (PubMed:15886106). In neurons, protein is concentrated
CC near the basal body where neurons are tethered to the scolopale cell
CC (PubMed:15886106). In germline and associated somatic cells of the
CC ovary, it has a punctate distribution and associates with specific F-
CC actin cell structures (PubMed:25236597). In germline cells, expressed
CC in the F-actin-rich cytocortex of the oocyte (from stage 3, peaking at
CC stages 9 to 10a) and in the cortex of nurse cells (from stage 6)
CC (PubMed:25236597). Expressed in the microvilli and terminal web of
CC follicle cells (PubMed:25236597). High expression at the base of the
CC follicle cell microvilli in the brush border (PubMed:25236597).
CC {ECO:0000269|PubMed:15886106, ECO:0000269|PubMed:25236597}.
CC -!- TISSUE SPECIFICITY: Expressed in the setae, micro- and macrochaetae on
CC the head, thorax and wing. {ECO:0000269|PubMed:15579689}.
CC -!- DEVELOPMENTAL STAGE: Throughout oogenesis expressed in the germline and
CC associated somatic cells (at protein level) (PubMed:25236597). In
CC germline cells of the germarium, expression levels peak during follicle
CC formation and again from mid-oogenesis until late oogenesis (at protein
CC level). Expressed both maternally and zygotically (PubMed:15579689).
CC Expression peaks in 12-18 hour embryos, and continues at a constant low
CC level of expression through to adults (PubMed:15579689).
CC {ECO:0000269|PubMed:15579689, ECO:0000269|PubMed:25236597}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit altered morphology of setae,
CC micro- and macrochaetae on the head, thorax and wing (PubMed:15579689).
CC The number and distribution of setae on the thorax is altered, as is
CC the morphology of the aristae (PubMed:15579689). Mutants also exhibit
CC scolopidial apical detachment and overall Johnston's organ (JO)
CC disorganization (PubMed:15579689). RNAi-mediated knockdown in
CC Johnston's organs, disrupts the filamentous structure of the
CC glycoprotein NompA at the apical junction (PubMed:27331610). NompA
CC occurs as puncta and scolopidia detatch from the hinge of the second
CC and third antennal segment (PubMed:27331610).
CC {ECO:0000269|PubMed:15579689, ECO:0000269|PubMed:27331610}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; AE014134; AAF53435.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10886.1; -; Genomic_DNA.
DR EMBL; AY069438; AAL39583.2; -; mRNA.
DR EMBL; BT011332; AAR96124.1; -; mRNA.
DR RefSeq; NP_001285949.1; NM_001299020.1.
DR RefSeq; NP_001285950.1; NM_001299021.1.
DR RefSeq; NP_523571.1; NM_078847.4.
DR RefSeq; NP_723895.1; NM_165099.3.
DR AlphaFoldDB; Q9V3Z6; -.
DR SMR; Q9V3Z6; -.
DR BioGRID; 60900; 14.
DR DIP; DIP-48747N; -.
DR IntAct; Q9V3Z6; 2.
DR STRING; 7227.FBpp0080282; -.
DR iPTMnet; Q9V3Z6; -.
DR PaxDb; Q9V3Z6; -.
DR PRIDE; Q9V3Z6; -.
DR EnsemblMetazoa; FBtr0080723; FBpp0080282; FBgn0000317.
DR EnsemblMetazoa; FBtr0080724; FBpp0080283; FBgn0000317.
DR EnsemblMetazoa; FBtr0343686; FBpp0310274; FBgn0000317.
DR EnsemblMetazoa; FBtr0343687; FBpp0310275; FBgn0000317.
DR GeneID; 34882; -.
DR KEGG; dme:Dmel_CG7595; -.
DR CTD; 34882; -.
DR FlyBase; FBgn0000317; ck.
DR VEuPathDB; VectorBase:FBgn0000317; -.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000155350; -.
DR HOGENOM; CLU_000192_14_1_1; -.
DR InParanoid; Q9V3Z6; -.
DR OMA; LHRGNKH; -.
DR OrthoDB; 527681at2759; -.
DR PhylomeDB; Q9V3Z6; -.
DR Reactome; R-DME-2453902; The canonical retinoid cycle in rods (twilight vision).
DR SignaLink; Q9V3Z6; -.
DR BioGRID-ORCS; 34882; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34882; -.
DR PRO; PR:Q9V3Z6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000317; Expressed in second segment of antenna (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q9V3Z6; baseline and differential.
DR Genevisible; Q9V3Z6; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0045180; C:basal cortex; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0035182; C:female germline ring canal outer rim; IDA:FlyBase.
DR GO; GO:0070825; C:micropyle; IDA:FlyBase.
DR GO; GO:0005902; C:microvillus; IDA:FlyBase.
DR GO; GO:0031477; C:myosin VII complex; IPI:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:FlyBase.
DR GO; GO:0045296; F:cadherin binding; IPI:FlyBase.
DR GO; GO:0000146; F:microfilament motor activity; IDA:FlyBase.
DR GO; GO:0032027; F:myosin light chain binding; IPI:FlyBase.
DR GO; GO:0060002; F:plus-end directed microfilament motor activity; IDA:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0030048; P:actin filament-based movement; IDA:FlyBase.
DR GO; GO:0007469; P:antennal development; IMP:FlyBase.
DR GO; GO:0048800; P:antennal morphogenesis; IMP:FlyBase.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0035293; P:chitin-based larval cuticle pattern formation; IGI:FlyBase.
DR GO; GO:0046847; P:filopodium assembly; IGI:FlyBase.
DR GO; GO:0032529; P:follicle cell microvillus organization; IMP:FlyBase.
DR GO; GO:0035317; P:imaginal disc-derived wing hair organization; IGI:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IGI:FlyBase.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd13198; FERM_C1_MyoVII; 1.
DR CDD; cd13199; FERM_C2_MyoVII; 1.
DR CDD; cd01381; MYSc_Myo7; 1.
DR Gene3D; 1.20.80.10; -; 2.
DR Gene3D; 1.25.40.530; -; 2.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR041793; MyoVII_FERM_C1.
DR InterPro; IPR041794; MyoVII_FERM_C2.
DR InterPro; IPR036106; MYSc_Myo7.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47031; SSF47031; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2167
FT /note="Myosin-VIIa"
FT /id="PRO_0000306376"
FT DOMAIN 63..733
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 736..758
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 759..788
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 805..827
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 828..857
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1008..1245
FT /note="MyTH4 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1250..1560
FT /note="FERM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 1558..1627
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1701..1849
FT /note="MyTH4 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 1855..2158
FT /note="FERM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 612..634
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT REGION 712..726
FT /note="Actin-binding"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT COILED 886..919
FT /evidence="ECO:0000255"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P08799"
FT MOD_RES 1651
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1654
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2045
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 2024
FT /note="I -> M (in Ref. 4; AAR96124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2167 AA; 250309 MW; 3C57E34ADDD89A42 CRC64;
MVIVTRGDYI WIEPASGREF DVAIGARVVS AEGRRIQVRD DDGDEVWLAP ERRIKAMHAS
SVQGVEDMIS LGDLHEAGIL RNLLIRYKEN LIYTYTGSIL VAVNPYQILP IYTGDQIKLY
KERKIGELPP HIFAIGDNAY AHMKRYRQDQ CIVISGESGA GKTESTKLIL QYLAAISGKH
SWIEQQILEA NPILEAFGNA KTIRNDNSSR FGKYIDIHFS ANGVIEGAKI EQYLLEKSRI
VSQNHSERNY HVFYCILAGL SADEKSRLDL GMAADYKYLT GGNSITCEGR DDAAEFSDIR
SAMKVLLFSD QEIWEIIKLL AALLHCGNIK YKATVVDNLD ATEIPEHINV ERVAGLLGLP
IQPLIDALTR RTLFAHGETV VSTLSRDQSV DVRDAFVKGI YGRMFVHIVR KINTAIFKPR
GTSRNAIGVL DIFGFENFDQ NSFEQFCINY ANENLQQFFV QHIFKLEQEE YNHEAINWQH
IEFVDNQDAL DLIAIKQLNI MALIDEEARF PKGTDQTMLA KLHKTHGSHK NYLKPKSDIN
TSFGLNHFAG VVFYDTRGFL DKNRDTFSPD LLHLVSQSTN KFLRQIFAQD IEMGAETRKR
TPTLSTQFRK SLDALMKTLS SCQPFFIRCI KPNELKKPMM FDRGLCCRQL RYSGMMETIR
IRRAGYPIRH GFREFVERYR FLIPGVPPAH RTDCQAATSR ICAVVLGKSD YQLGHTKVFL
KDAHDLFLEQ ERDRVLTRKI LILQRSIRGW VYRRRFLRLR AAAITVQRFW KGYAQRKRYR
NMRVGYMRLQ ALIRSRVLSH RFRHLRGHIV GLQAHARGYL VRREYGHKMW AVIKIQSHVR
RMIAMRRYRK LRLEHKQFAE VLQLRKLEEQ ELLHRGNKHA REIAEQHYRD RLHELERREI
QEQLENRRRV EVNMNIINDA ARKQEEPVDD GKLVEAMFDF LPDSSSDAPT PHGGRETSVF
NDLPHAQNVN QDDIIAPIHI SEDEEDLSEF KFQKFAATYF QGNVNHQYAK KALKHPLLPL
HTQGDQLAAQ ALWITILRFT GDMPEPKYHT MDRMDTTSVM SKVTATLGRN FIRSKEFQEA
QLMGLDPDAF LKQKPRSIRH KLVSLTLKRK NKLGEDVRRR LQDDEYTADS YQSWLQSRPT
SNLEKLHFII GHGILRAELR DEIYCQICKQ LTNNPLKSSH ARGWILLSLC VGCFAPSEKF
VNYLRAFIRE GPPGYAPYCE ERLKRTFNNG TRNQPPSWLE LQATKSKKPI MLPITFMDGN
TKTLLADSAT TARELCNQLS DKISLKDQFG FSLYIALFDK VSSLGSGGDH VMDAISQCEQ
YAKEQGAQER NAPWRLFFRK EIFAPWHEPT HDQVATNLIY QQVVRGVKFG EYRCDKEEDL
AMIAAQQYFI EYSTDMSMER LFTLLPNFIP DFCLSGVDKA IERWAALVLQ AYKKSYYVKD
KIAPLKIKED IVSYAKYKWP LLFSRFYEAY RNSGPNLPKN DVIIAVNWTG VYVVDDQEQV
LLELSFPEIT AVSSQKTNKV FTQTFSLSTV RGEEFTFQSP NAEDIRDLVV YFLDGLKKRS
KYVIALQDYR APSDGTSFLS FFKGDLIILE DESCGESVLN NGWCIGRCDR SQERGDFPAE
TVYVLPTLSK PPQDILALFN IEEAHHGRRL SMASNGGAVE PRDRPHTLME YALDHFRLPP
KRTMSKTLTL SSKRSEELWR YSRDPIKAPL LRKLQSKEEF AEEACFAFAA ILKYMGDLPS
KRPRMGNEIT DHIFDGPLKH EILRDEIYCQ LMKQLTDNRN RMSEERGWEL MWLATGLFAC
SQGLLKELLL FLRTRRHPIS QDSMHRLQKT IRHGQRKYPP HQVEVEAIQH KTTQIFHKVY
FPDDTDEAFE VDSSTRAKDF CNNISQRLSL RTSEGFSLFV KIADKVISVP EGDFFFDFVR
HLTDWIKKAR PIRDGANPQF TYQVFFMKKL WTNTVPGKDR NADLIFHYHQ ELPKLLRGYH
KCSREEAAKL AALVFRVRFG ENKQELQAIP QMLRELIPSD IMKIQSTSEW KRSIVASYNQ
DGGMTSEDAK VAFLKIVYRW PTFGSAFFEV KQTTEPNYPE MLLIAINKHG VSLIHPVTKD
ILVTHPFTRI SNWSSGNTYF HMTIGNLVRG SKLLCETSLG YKMDDLLTSY ISLMLTNMNK
NRTIRAN
