MY61F_DROME
ID MY61F_DROME Reviewed; 1035 AA.
AC Q23979; A4V191; Q7KVC1; Q8T0U8; Q9W0H0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Unconventional myosin IC {ECO:0000303|PubMed:22491943};
DE Short=MyoIC {ECO:0000303|PubMed:22491943};
DE AltName: Full=Brush border myosin IB;
DE Short=BBMIB;
DE AltName: Full=Myosin-IB {ECO:0000303|PubMed:7589814, ECO:0000303|PubMed:8201616};
DE Short=MIB {ECO:0000303|PubMed:7589814};
DE AltName: Full=Unconventional myosin 1C {ECO:0000303|PubMed:22491943, ECO:0000303|PubMed:30467170};
DE Short=Myo1C {ECO:0000303|PubMed:22491943, ECO:0000303|PubMed:30467170};
GN Name=Myo61F;
GN Synonyms=Myo1C {ECO:0000303|PubMed:22491943, ECO:0000303|PubMed:30467170};
GN ORFNames=CG9155;
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 B), AND DEVELOPMENTAL STAGE.
RC TISSUE=Head;
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, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 347-706.
RX PubMed=8216259; DOI=10.1006/bbrc.1993.2182;
RA Cheney C.M., Kravit N.G., Verbsky J.W.;
RT "A new myosin I gene in Drosophila.";
RL Biochem. Biophys. Res. Commun. 195:1280-1288(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 639-1035.
RA Caggese C.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND THR-310, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [10]
RP FUNCTION, AND MUTAGENESIS OF 114-GLY--THR-121; LYS-120; ASN-166; PHE-395;
RP 590-PRO--ASP-600; 705-LYS--ASN-774 AND 775-GLY--GLN-1035.
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
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 [13]
RP FUNCTION, LIPID-BINDING, SUBCELLULAR LOCATION, ACTIN-BINDING, AND DOMAIN.
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 Functions as antagonist for Myo31DF, an unconventional myosin with an
CC essential role in the establishment of body left-right asymmetry
CC (PubMed:16598258, PubMed:18521948, PubMed:22491943, PubMed:25659376,
CC PubMed:30467170). {ECO:0000269|PubMed:16598258,
CC ECO:0000269|PubMed:18521948, ECO:0000269|PubMed:22491943,
CC ECO:0000269|PubMed:25659376, ECO:0000269|PubMed:30467170}.
CC -!- SUBUNIT: Binds F-actin. {ECO:0000269|PubMed:30467170,
CC ECO:0000269|PubMed:7589814}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22491943,
CC ECO:0000269|PubMed:25659376, ECO:0000269|PubMed:7589814}. Cytoplasm,
CC cell cortex {ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:25659376,
CC ECO:0000269|PubMed:7589814}. Cell membrane
CC {ECO:0000269|PubMed:22491943}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22491943}; Cytoplasmic side
CC {ECO:0000269|PubMed:22491943}. Note=Protein shifts from the basolateral
CC to apical domain in enterocytes and follicle cells (PubMed:7589814).
CC Colocalizes with the actin cytoskeleton (PubMed:22491943,
CC PubMed:25659376). {ECO:0000269|PubMed:22491943,
CC ECO:0000269|PubMed:25659376, ECO:0000269|PubMed:7589814}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q23979-1; Sequence=Displayed;
CC Name=B; Synonyms=C;
CC IsoId=Q23979-2; Sequence=VSP_009274;
CC Name=D;
CC IsoId=Q23979-3; Sequence=VSP_035432;
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 and adult gut brush border, expressed in the microvilli. Also expressed
CC at high levels in follicle cells during oogenesis.
CC {ECO:0000269|PubMed:25659376, ECO:0000269|PubMed:7589814}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 8-12 hours embryonic
CC development, continues to increase until third larval instar,
CC disappears in pupae and is present at a low level in adults. Expression
CC in embryogenesis is correlated with the formation of a brush border
CC within the alimentary canal. In third instar larvae, detected in
CC segment A8 of the male genital disk (PubMed:22491943). First detected
CC at stage 12 in the embryonic anterior and posterior midgut, and in the
CC stomatogastric nervous system. Detected in trachea at stage 14. Widely
CC expressed in stage 16 in embryos (PubMed:25659376).
CC {ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:25659376,
CC ECO:0000269|PubMed:7589814, ECO:0000269|PubMed:8201616}.
CC -!- DOMAIN: The myosin motor domain contains the derminants for the
CC direction of left-right body asymmetry. {ECO:0000269|PubMed:30467170}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile, but adults have a shortened
CC lifespan. Flies deficient in both Myo31DF and Myo61F are viable and
CC fertile, but adults have a shorter lifespan than single mutants. Flies
CC deficient in Myo61F show normal left-right asymmetry of the embryonic
CC gut and normal, dextral rotation of male genitalia, and the same is
CC observed in mutants deficient in both Myo61F and Myo95E. Mutants
CC deficient in Myo31DF and Myo61F display stronger sinistral rotation of
CC the male genitalia than mutants deficient for Myo31DF
CC (PubMed:25659376). RNAi-mediated knockdown causes defects in embryonic
CC midgut laterality, but only with low-frequency (PubMed:16598258). RNAi-
CC mediated knockdown has no effect on normal, dextral rotation of male
CC genitalia (PubMed:22491943). Combined RNAi-mediated knockdown of
CC Myo31DF and Myo61F gives rise to the same phenotype as knockdown of
CC Myo31DF alone, i.e sinistral rotation of the male genitalia
CC (PubMed:22491943). {ECO:0000269|PubMed:16598258,
CC ECO:0000269|PubMed:22491943, ECO:0000269|PubMed:25659376}.
CC -!- MISCELLANEOUS: Overexpression in larval epidermis causes sinistral
CC twisting of the whole larval body. Ectopic expression in tracheal
CC precursor cells causes sinistral spiraling of tracheal branches, giving
CC rise to a spiraling ribbon shape instead of the normal smooth tube.
CC Ectopic expression in epithelial cells causes increased elongation and
CC a clear shift of the membrane orientation toward one side, so that the
CC membrane is no longer perpendicular to the anterior-posterior axis
CC (PubMed:30467170). Overexpression causes reversal of the normal left-
CC right laterality of the embryonic midgut and hindgut (PubMed:16598258,
CC PubMed:18521948). Overexpression causes loss of the normal dextral
CC rotation of the male genitalia, and leads to sinistral rotation in some
CC cases (PubMed:22491943). {ECO:0000269|PubMed:16598258,
CC ECO:0000269|PubMed:18521948, ECO:0000269|PubMed:22491943,
CC ECO:0000269|PubMed:30467170}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; U07596; AAA19591.1; -; mRNA.
DR EMBL; AE014296; AAF47477.3; -; Genomic_DNA.
DR EMBL; AE014296; AAF47478.3; -; Genomic_DNA.
DR EMBL; AE014296; AAN11472.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11473.1; -; Genomic_DNA.
DR EMBL; AY069044; AAL39189.1; -; mRNA.
DR EMBL; L13070; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ000879; CAA04367.1; -; Genomic_DNA.
DR PIR; S45574; S45574.
DR RefSeq; NP_476934.2; NM_057586.4. [Q23979-3]
DR RefSeq; NP_728594.2; NM_167870.2. [Q23979-1]
DR RefSeq; NP_728595.1; NM_167871.2. [Q23979-2]
DR RefSeq; NP_728596.1; NM_167872.2. [Q23979-2]
DR AlphaFoldDB; Q23979; -.
DR SMR; Q23979; -.
DR BioGRID; 63696; 11.
DR IntAct; Q23979; 9.
DR STRING; 7227.FBpp0072567; -.
DR iPTMnet; Q23979; -.
DR PaxDb; Q23979; -.
DR PRIDE; Q23979; -.
DR DNASU; 38153; -.
DR EnsemblMetazoa; FBtr0072672; FBpp0072565; FBgn0010246. [Q23979-2]
DR EnsemblMetazoa; FBtr0072673; FBpp0072566; FBgn0010246. [Q23979-2]
DR EnsemblMetazoa; FBtr0072674; FBpp0072567; FBgn0010246. [Q23979-3]
DR EnsemblMetazoa; FBtr0072675; FBpp0072568; FBgn0010246. [Q23979-1]
DR GeneID; 38153; -.
DR KEGG; dme:Dmel_CG9155; -.
DR UCSC; CG9155-RC; d. melanogaster.
DR UCSC; CG9155-RD; d. melanogaster.
DR CTD; 38153; -.
DR FlyBase; FBgn0010246; Myo61F.
DR VEuPathDB; VectorBase:FBgn0010246; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000170976; -.
DR InParanoid; Q23979; -.
DR PhylomeDB; Q23979; -.
DR SignaLink; Q23979; -.
DR BioGRID-ORCS; 38153; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38153; -.
DR PRO; PR:Q23979; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0010246; Expressed in adult midgut (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q23979; baseline and differential.
DR Genevisible; Q23979; DM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; IDA:FlyBase.
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; IBA:GO_Central.
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:0042742; P:defense response to bacterium; IMP:FlyBase.
DR GO; GO:0007368; P:determination of left/right symmetry; 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:0032528; P:microvillus organization; IMP: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; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
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; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cytoplasm; Lipid-binding; Membrane; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1035
FT /note="Unconventional myosin IC"
FT /id="PRO_0000123455"
FT DOMAIN 21..703
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 696..728
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 729..751
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 752..779
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 857..1035
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 578..600
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8201616"
FT /id="VSP_009274"
FT VAR_SEQ 2..3
FT /note="AS -> YIEIKSLIFAIMDTKDYID (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_035432"
FT MUTAGEN 114..121
FT /note="Missing: Abolishes the ability to cause laterality
FT defects upon overexpression."
FT /evidence="ECO:0000269|PubMed:22491943"
FT MUTAGEN 120
FT /note="K->A: Abolishes the ability to cause laterality
FT defects upon overexpression; when associated with A-166 and
FT A-395."
FT /evidence="ECO:0000269|PubMed:22491943"
FT MUTAGEN 166
FT /note="N->A: Abolishes the ability to cause laterality
FT defects upon overexpression; when associated with A-120 and
FT A-395."
FT /evidence="ECO:0000269|PubMed:22491943"
FT MUTAGEN 395
FT /note="F->A: Abolishes the ability to cause laterality
FT defects upon overexpression; when associated with A-120 and
FT A-166."
FT /evidence="ECO:0000269|PubMed:22491943"
FT MUTAGEN 590..600
FT /note="Missing: Abolishes the ability to cause laterality
FT defects upon overexpression."
FT /evidence="ECO:0000269|PubMed:22491943"
FT MUTAGEN 705..774
FT /note="Missing: No effect on the ability to cause
FT laterality defects upon overexpression."
FT /evidence="ECO:0000269|PubMed:22491943"
FT MUTAGEN 775..1035
FT /note="Missing: Abolishes the ability to cause laterality
FT defects upon overexpression."
FT /evidence="ECO:0000269|PubMed:22491943"
FT CONFLICT 73
FT /note="D -> N (in Ref. 1; AAA19591)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="R -> G (in Ref. 1; AAA19591)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="R -> S (in Ref. 1; AAA19591)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="T -> G (in Ref. 1; AAA19591)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="N -> S (in Ref. 1; AAA19591 and 5; L13070)"
FT /evidence="ECO:0000305"
FT CONFLICT 560..561
FT /note="EL -> DV (in Ref. 5; L13070)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="E -> Y (in Ref. 4; AAL39189)"
FT /evidence="ECO:0000305"
FT CONFLICT 697
FT /note="D -> AI (in Ref. 5; L13070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1035 AA; 118990 MW; E7B153700A31D818 CRC64;
MASFNSQLKM ETGLHERDRA GVQDFVLLEN YQSEEAFIGN LKKRFQEDLI YTYIGQVLIS
VNPYKQLPIY TDDHVKAYRN KHFYEMPPHI FAVTDNAFRS LIEENRGQCV LISGESGSGK
TEASKKVLQF IAACSGNQTT VEGVKDKLLK SNPVLEAFGN AKTNRNDNSS RFGKYMDIQF
DFKGAPIGGN ILNYLLEKSR VVAQMGGERN FHIFYQLLAG ADEALLQELR LERALDTYSY
LTDGLNGTVT RINDADSFKQ VQQALTVIDF TKEEQREIFG IVASILHLGN VGFTEVEGNA
KVNSRDLVVT AARLLGVNAS ELEAALTHRT IDARGDVVTS PLNQELAIYA RDALAKAVYD
RLFSWLVQRL NISLQAKETR ASRNNVMGIL DIYGFEIFQK NSFEQFCINF CNEKLQQLFI
ELTLKSEQDE YRREGIEWIP VEYFDNKVIC NLIEEKHKGI ISILDEECLR PGEPTDKTFL
EKLTQKLAQH HHYVCHEKAP AHIKKIMLRD EFRLVHYAGE VTYSVNGFLD KNNDLLFRDL
KETLSKAGNG IVRNCFPEKE LRSLKRPETA ITQFRASLNN LMDILMCKEP SYIRCIKPND
LQTANVFNDE LVLHQVKYLG LMENLRVRRA GFAYRRTYEL FLERYKSLSK STWPNYKGPG
GPKAGVQQLV KDLGWDEEKY RVGETKLFIR WPRTLFDTED AYQEKKHEIA AIIQAHWKGL
MQRRKYLKLR AQVIIMQSYC RRKLAQQAAK KRREAADKIR AFIKGFITRN DAPNGFNEEF
IANAKRMWLL RLAKELPTKV LDKSWPHAPG HCEEASGILH RLHRLHLARI YRLKLTPQQK
RQFELKVLAE KVFKGKKNNY ASSVSTWFQE DRIPKEHIQR VNDFVASTFG SEQLKYQSFC
TKFDRHGYKS RDRFILLSNK AIYVLDGKTY KQKHRLPLDK IDFTLTNHND DLMVIRIPLD
LKKDKGDLIL IIPRIIEFST YIIDTVGTAS IVSIVDRNSL EHNVVKGKGG VIDIQTGAEP
GVVRDKGHLV IIGTQ
