MY31D_DROME
ID MY31D_DROME Reviewed; 1011 AA.
AC Q23978; A4V0K5; M9MRS7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Unconventional myosin ID {ECO:0000303|PubMed:16598259, ECO:0000303|PubMed:22491943};
DE Short=MyoID {ECO:0000303|PubMed:22491943};
DE AltName: Full=Brush border myosin IA;
DE Short=BBMIA;
DE AltName: Full=Myosin 1D {ECO:0000303|PubMed:30467170};
DE Short=Myo1D {ECO:0000303|PubMed:30467170};
DE AltName: Full=Myosin-IA {ECO:0000303|PubMed:16598259, ECO:0000303|PubMed:8201616};
DE Short=MIA {ECO:0000303|PubMed:7589814};
DE Short=MyoIA {ECO:0000303|PubMed:16598258};
GN Name=Myo31DF {ECO:0000303|PubMed:16598259};
GN Synonyms=Myo1D {ECO:0000303|PubMed:30467170}; ORFNames=CG7438;
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], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=8201616; DOI=10.1006/jmbi.1994.1376;
RA Morgan N.S., Skovronsky D.M., Artavanis-Tsakonas S., Mooseker M.S.;
RT "The molecular cloning and characterization of Drosophila melanogaster
RT myosin-IA and myosin-IB.";
RL J. Mol. Biol. 239:347-356(1994).
RN [2]
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 [3]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP ACTIN-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=7589814; DOI=10.1006/dbio.1995.0005;
RA Morgan N.S., Heintzelman M.B., Mooseker M.S.;
RT "Characterization of myosin-IA and myosin-IB, two unconventional myosins
RT associated with the Drosophila brush border cytoskeleton.";
RL Dev. Biol. 172:51-71(1995).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF 331-GLN--VAL-1011.
RX PubMed=16598258; DOI=10.1038/nature04625;
RA Hozumi S., Maeda R., Taniguchi K., Kanai M., Shirakabe S., Sasamura T.,
RA Speder P., Noselli S., Aigaki T., Murakami R., Matsuno K.;
RT "An unconventional myosin in Drosophila reverses the default handedness in
RT visceral organs.";
RL Nature 440:798-802(2006).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INTERACTION WITH ARM,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 695-HIS--GLN-736.
RX PubMed=16598259; DOI=10.1038/nature04623;
RA Speder P., Adam G., Noselli S.;
RT "Type ID unconventional myosin controls left-right asymmetry in
RT Drosophila.";
RL Nature 440:803-807(2006).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF
RP 103-GLY--THR-107; LYS-106; ASN-156; PHE-382; 579-PRO--ASP-589;
RP 692-MET--GLU-737 AND 738-LEU--VAL-1011.
RX PubMed=18521948; DOI=10.1002/dvdy.21583;
RA Hozumi S., Maeda R., Taniguchi-Kanai M., Okumura T., Taniguchi K.,
RA Kawakatsu Y., Nakazawa N., Hatori R., Matsuno K.;
RT "Head region of unconventional myosin I family members is responsible for
RT the organ-specificity of their roles in left-right polarity in
RT Drosophila.";
RL Dev. Dyn. 237:3528-3537(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SHG AND ARM, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=22491943; DOI=10.1242/dev.047589;
RA Petzoldt A.G., Coutelis J.B., Geminard C., Speder P., Suzanne M.,
RA Cerezo D., Noselli S.;
RT "DE-Cadherin regulates unconventional Myosin ID and Myosin IC in Drosophila
RT left-right asymmetry establishment.";
RL Development 139:1874-1884(2012).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH DS,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=26073018; DOI=10.1016/j.devcel.2015.04.026;
RA Gonzalez-Morales N., Geminard C., Lebreton G., Cerezo D., Coutelis J.B.,
RA Noselli S.;
RT "The Atypical Cadherin Dachsous Controls Left-Right Asymmetry in
RT Drosophila.";
RL Dev. Cell 33:675-689(2015).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 331-GLN--VAL-1011.
RX PubMed=25659376; DOI=10.1534/genetics.115.174698;
RA Okumura T., Sasamura T., Inatomi M., Hozumi S., Nakamura M., Hatori R.,
RA Taniguchi K., Nakazawa N., Suzuki E., Maeda R., Yamakawa T., Matsuno K.;
RT "Class I myosins have overlapping and specialized functions in left-right
RT asymmetric development in Drosophila.";
RL Genetics 199:1183-1199(2015).
RN [12]
RP FUNCTION, LIPID-BINDING, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=30467170; DOI=10.1126/science.aat8642;
RA Lebreton G., Geminard C., Lapraz F., Pyrpassopoulos S., Cerezo D.,
RA Speder P., Ostap E.M., Noselli S.;
RT "Molecular to organismal chirality is induced by the conserved myosin 1D.";
RL Science 362:949-952(2018).
CC -!- FUNCTION: Unconventional myosin that functions as actin-based motor
CC protein with ATPase activity (PubMed:30467170). Binds to membranes
CC enriched in phosphatidylinositol 4-5-bisphosphate, and can glide along
CC actin filaments when anchored to a lipid bilayer (PubMed:30467170).
CC Generates left-right asymmetry at the level of single cells, organs and
CC the whole body via its interaction with the actin cytoskeleton, both in
CC the embryo and the adult (PubMed:16598258, PubMed:16598259,
CC PubMed:18521948, PubMed:26073018, PubMed:25659376, PubMed:30467170).
CC Normal left-right asymmetry of the larval midgut and hindgut requires
CC expression in the embryonic hindgut epithelium during a critical time
CC period, 10 to 12.75 hours after egg laying (PubMed:18521948). This
CC period corresponds to a late stage of germband retraction, and precedes
CC left-right asymmetric morphogenesis (PubMed:18521948). Expression in
CC segment H1 of the imaginal ring is required at 0 to 24 hours after
CC pupation for changes of cell shape and orientation in the H2 segment,
CC which then gives rise to normal, dextral looping of the adult hindgut
CC (PubMed:16598258, PubMed:26073018). Required during a critical period,
CC 126-132 hours after egg laying, for normal, dextral rotation of the
CC adult male genitalia (PubMed:16598258, PubMed:16598259,
CC PubMed:22491943, PubMed:26073018, PubMed:25659376). Has a double role
CC by promoting dextral rotation in the posterior compartment of segment
CC A8 of the male genital disk, and in repressing sinistral looping in the
CC anterior compartment (PubMed:16598259). {ECO:0000269|PubMed:16598258,
CC ECO:0000269|PubMed:16598259, ECO:0000269|PubMed:18521948,
CC ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:25659376,
CC ECO:0000269|PubMed:26073018, ECO:0000269|PubMed:30467170}.
CC -!- SUBUNIT: Binds to F-actin (PubMed:7589814). Interacts with arm
CC (PubMed:16598259, PubMed:22491943). Interacts with shg
CC (PubMed:22491943). Interacts with ds (via intracellular region)
CC (PubMed:26073018). {ECO:0000269|PubMed:16598259,
CC ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:26073018,
CC ECO:0000269|PubMed:7589814}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16598258,
CC ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:7589814}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:16598258, ECO:0000269|PubMed:22491943,
CC ECO:0000269|PubMed:25659376, ECO:0000269|PubMed:7589814}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:16598258, ECO:0000269|PubMed:16598259,
CC ECO:0000269|PubMed:7589814}. Cell membrane
CC {ECO:0000269|PubMed:26073018, ECO:0000269|PubMed:30467170}; Peripheral
CC membrane protein {ECO:0000269|PubMed:26073018,
CC ECO:0000269|PubMed:30467170}; Cytoplasmic side. Cell junction
CC {ECO:0000269|PubMed:26073018}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:16598259}. Cell projection
CC {ECO:0000269|PubMed:16598258}. Note=Detected throughout the cytoplasm.
CC Detected primarily in the basolateral cytoplasmic region of immature
CC enterocytes. Detected also in the apical cytoplasmic region in midgut
CC enterocytes and follicle cells (PubMed:7589814). Colocalizes with the
CC actin cytoskeleton (PubMed:7589814, PubMed:16598258, PubMed:16598259,
CC PubMed:25659376). Colocalizes with arm at adherens junctions
CC (PubMed:16598259). Colocalizes with ds at cell junctions
CC (PubMed:26073018). {ECO:0000269|PubMed:16598258,
CC ECO:0000269|PubMed:16598259, ECO:0000269|PubMed:25659376,
CC ECO:0000269|PubMed:26073018, ECO:0000269|PubMed:7589814}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in gastric caeca, midgut
CC cells of the proventriculus, and in the mid and hindgut. In the larval
CC gut brush border, expression is in the terminal web domain. In the
CC adult gut brush border, expression remains in the web domain and has
CC also moved into the microvilli. Also expressed at low levels in
CC follicle cells during oogenesis. {ECO:0000269|PubMed:7589814}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development to adulthood with highest levels at the end of
CC larval development. Expression in embryogenesis is correlated with the
CC formation of a brush border within the alimentary canal. Detected in
CC the developing hindgut and midgut in stage 12 and stage 14 embryos (at
CC protein level) (PubMed:16598258). In third instar larvae, detected in a
CC symmetrical, double chevron-like pattern in the ventral section of
CC segment A8 of the male genital disk, with one chevron in the anterior
CC and the other in the posterior part of this segment (PubMed:16598259,
CC PubMed:22491943). Detected in the H1 domain of the larval imaginal disk
CC (PubMed:26073018). Detected in embryonic anterior and posterior midgut,
CC hindgut, and in salivary gland (PubMed:25659376).
CC {ECO:0000269|PubMed:16598258, ECO:0000269|PubMed:16598259,
CC ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:25659376,
CC ECO:0000269|PubMed:26073018, ECO:0000269|PubMed:7589814,
CC ECO:0000269|PubMed:8201616}.
CC -!- DOMAIN: The myosin motor domain contains the derminants for dextral
CC twisting. {ECO:0000269|PubMed:30467170}.
CC -!- DOMAIN: The two IQ domains are essential for activity in determining
CC left-right asymmetry. {ECO:0000269|PubMed:16598259,
CC ECO:0000269|PubMed:18521948}.
CC -!- DOMAIN: The actin-binding domain is essential for activity in
CC determining left-right asymmetry. {ECO:0000269|PubMed:18521948}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:16598258). Mutant
CC embryos and adults display normal foregut left-right asymmetry, but
CC inverted left-right asymmetry of the midgut and hindgut
CC (PubMed:16598258, PubMed:18521948). RNAi-mediated knockdown in the
CC hindgut at 0 to 24 hours after pupation leads to inverted left-right
CC asymmetry of the adult hindgut, but knockdown at later stages has
CC little or no effect (PubMed:16598258, PubMed:26073018). Adults display
CC inverted left-right asymmetry of the male genitalia (PubMed:16598258).
CC RNAi-mediated knockdown in the anterior and the posterior part of
CC segment A8 of the male genital disk causes loss of the normal dextral
CC rotation of the genital plate and inverted, sinistral spermiduct
CC looping (PubMed:16598259, PubMed:26073018). Selective RNAi-mediated
CC down-regulation in the anterior part of segment A8 of the male genital
CC disk leads to partial dextral rotation of the genitalia, while RNAi-
CC mediated down-regulation in the posterior part of segment A8 leads to
CC non-rotated genitalia (PubMed:16598259). Combined RNAi-mediated
CC knockdown of both ds and Myo31DF in the H1 segment of the imaginal ring
CC causes mislooping of the adult hindgut (PubMed:26073018).
CC {ECO:0000269|PubMed:16598258, ECO:0000269|PubMed:16598259,
CC ECO:0000269|PubMed:18521948, ECO:0000269|PubMed:26073018}.
CC -!- MISCELLANEOUS: Overexpression throughout the embryo reverses the normal
CC left-right asymmetry of the embryonic gut, giving rise to a gut that is
CC a mirror-image of the wild-type (PubMed:16598258). Ectopic expression
CC in the larval epidermis causes dextral twisting of the entire larval
CC body. Ectopic expression in tracheal precursor cells causes dextral
CC spiraling of tracheal branches, giving rise to a spiraling ribbon shape
CC instead of the normal smooth tube. Ectopic expression in epithelial
CC cells causes increased elongation and a clear shift of the membrane
CC orientation toward one side, so that the membrane is no longer
CC perpendicular to the anterior-posterior axis (PubMed:30467170).
CC {ECO:0000269|PubMed:16598258, ECO:0000269|PubMed:30467170}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin that should not be
CC confused with the conventional myosin-1. {ECO:0000305}.
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DR EMBL; U07595; AAA19590.1; -; mRNA.
DR EMBL; AE014134; AAF52966.1; -; Genomic_DNA.
DR EMBL; AE014134; ADV37034.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10756.1; -; Genomic_DNA.
DR EMBL; AY075567; AAL68374.1; -; mRNA.
DR PIR; S45573; S45573.
DR RefSeq; NP_001188784.1; NM_001201855.2.
DR RefSeq; NP_523538.1; NM_078814.4.
DR RefSeq; NP_723596.1; NM_164933.3.
DR AlphaFoldDB; Q23978; -.
DR SMR; Q23978; -.
DR BioGRID; 60525; 12.
DR IntAct; Q23978; 7.
DR STRING; 7227.FBpp0079625; -.
DR PaxDb; Q23978; -.
DR PRIDE; Q23978; -.
DR DNASU; 34445; -.
DR EnsemblMetazoa; FBtr0080035; FBpp0079625; FBgn0086347.
DR EnsemblMetazoa; FBtr0080036; FBpp0079626; FBgn0086347.
DR EnsemblMetazoa; FBtr0304138; FBpp0293078; FBgn0086347.
DR GeneID; 34445; -.
DR KEGG; dme:Dmel_CG7438; -.
DR CTD; 34445; -.
DR FlyBase; FBgn0086347; Myo31DF.
DR VEuPathDB; VectorBase:FBgn0086347; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000158053; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q23978; -.
DR OMA; QDVKYGH; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; Q23978; -.
DR SignaLink; Q23978; -.
DR BioGRID-ORCS; 34445; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 34445; -.
DR PRO; PR:Q23978; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0086347; Expressed in embryonic/larval hemocyte (Drosophila) and 52 other tissues.
DR Genevisible; Q23978; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:FlyBase.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:UniProtKB.
DR GO; GO:0061525; P:hindgut development; IMP:FlyBase.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 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; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Cell junction;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW Developmental protein; Lipid-binding; Membrane; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1011
FT /note="Unconventional myosin ID"
FT /id="PRO_0000123454"
FT DOMAIN 7..690
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 694..714
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 716..736
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 806..1007
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 567..589
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MUTAGEN 103..107
FT /note="Missing: Loss of function in specification of gut
FT left-right asymmetry."
FT /evidence="ECO:0000269|PubMed:18521948"
FT MUTAGEN 106
FT /note="K->A: Loss of function in specification of gut left-
FT right asymmetry; when associated with A-155 and A-382."
FT /evidence="ECO:0000269|PubMed:18521948"
FT MUTAGEN 156
FT /note="N->A: Loss of function in specification of gut left-
FT right asymmetry; when associated with A-106 and A-382."
FT /evidence="ECO:0000269|PubMed:18521948"
FT MUTAGEN 331..1011
FT /note="Missing: Causes inverted left-right asymmetry of the
FT midgut and hindgut in embryos and adults. Flies are viable
FT and fertile, but display mildly reduced hatching rate and
FT reduced life span."
FT /evidence="ECO:0000269|PubMed:16598258,
FT ECO:0000269|PubMed:26073018"
FT MUTAGEN 382
FT /note="F->A: Loss of function in specification of gut left-
FT right asymmetry; when associated with A-106 and A-156."
FT /evidence="ECO:0000269|PubMed:18521948"
FT MUTAGEN 579..589
FT /note="Missing: Loss of function in specification of gut
FT left-right asymmetry."
FT /evidence="ECO:0000269|PubMed:18521948"
FT MUTAGEN 692..737
FT /note="Missing: Loss of function in specification of gut
FT left-right asymmetry."
FT /evidence="ECO:0000269|PubMed:18521948"
FT MUTAGEN 695..736
FT /note="Missing: Loss of the ability to promote the normal
FT dextral looping of the spermiduct."
FT /evidence="ECO:0000269|PubMed:16598259"
FT MUTAGEN 738..1011
FT /note="Missing: Loss of function in specification of gut
FT left-right asymmetry."
FT /evidence="ECO:0000269|PubMed:18521948"
SQ SEQUENCE 1011 AA; 117095 MW; 31206C065B5D5DFA CRC64;
MAMQREAGVQ DFVLLDQVSM EKFMDNLRKR FQNGSIYTYI GEVCVSMNPY RQMNIYGPET
IRKYKGRELF ENAPHLFAIA DSAYRVLKQR QQDTCILISG ESGAGKTEAS KIIMKYIAAV
TNAQGQNEIE RVKNVLIQSN AILETFGNAK TNRNDNSSRF GKYMDIEFDY KADPVGGIIT
NYLLEKSRVV QQQPGERNFH SFYQLLRGAN DNELRQYELQ KETGKYHYLN QGSMDILTEK
SDYKGTCNAF KTLGFSTDEV QTIWRTIAAV LHLGNVEFQT IEDELVISNK QHLKSTAKLL
QVTETELSTA LTKRVIAAGG NVMQKDHNAT QAEYGKDALA KAIYDRLFTW IISRINRAIL
FRGSKTQARF NSVIGVLDIY GFEIFDSNSF EQFCINYCNE KLQQLFIELV LKQEQEEYQR
EGIEWTNIEY FNNKIICDLV EQPHKGIIAI MDEACLSVGK VTDDTLLGAM DKNLSKHPHY
TSRQLKPTDK ELKHREDFRI THYAGDVIYN INGFIEKNKD TLYQDFKRLL HNSKDANLSE
MWPEGAQDIK KTTKRPLTAG TLFQRSMADL VVTLLKKEPF YVRCIKPNDL KSSTVFDEER
VEHQVRYLGL LENLRVRRAG FVHRQRYDKF LLRYKMISQY TWPNFRAGSD RDGVRVLIEE
KKFAQDVKYG HTKIFIRSPR TLFALEHQRN EMIPHIVTLL QKRVRGWIVR RNFKKMKAAI
TIVRAYKAYK LRSYVQELAN RLRKAKQMRD YGKSIQWPQP PLAGRKVEAK LHRMFDFWRA
NMILHKYPRS EWPQLRLQII AATALAGRRP YWGQARRWVG DYLANSQENS GYEAYNGSIK
NIRNHPADGE TFQQVLFSSF VKKFNHFNKQ ANRAFIVSDS TIHKLDGIKN KFKDMKRTIK
IRELTSISVS PGRDQLIVFH SSKNKDLVFS LESEYTPLKE DRIGEVVGIV CKKYHDLTGT
ELRVNVTTNI SCRLDGKARI ITVEAASNVE VPNFRPKEGN IIFEVPAAYC V
