LIS1_DROME
ID LIS1_DROME Reviewed; 411 AA.
AC Q7KNS3; A4UZJ3; O96698; Q5BI20; Q8SXJ6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=DLis-1;
DE Short=Dlis1;
DE Short=Lissencephaly1;
GN Name=Lis-1 {ECO:0000255|HAMAP-Rule:MF_03141}; Synonyms=Lis1;
GN ORFNames=CG8440;
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], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF GLU-128.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=10498683; DOI=10.1242/dev.126.20.4477;
RA Liu Z., Xie T., Steward R.;
RT "Lis1, the Drosophila homolog of a human lissencephaly disease gene, is
RT required for germline cell division and oocyte differentiation.";
RL Development 126:4477-4488(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10559989; DOI=10.1038/15680;
RA Swan A., Nguyen T., Suter B.;
RT "Drosophila Lissencephaly-1 functions with Bic-D and dynein in oocyte
RT determination and nuclear positioning.";
RL Nat. Cell Biol. 1:444-449(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND LACK OF INTERACTION WITH PAF-AH-ALPHA.
RX PubMed=10737922;
RX DOI=10.1002/(sici)1097-0134(20000401)39:1<1::aid-prot1>3.0.co;2-n;
RA Sheffield P.J., Garrard S., Caspi M., Aoki J., Arai H., Derewenda U.,
RA Inoue K., Suter B., Reiner O., Derewenda Z.S.;
RT "Homologs of the alpha- and beta-subunits of mammalian brain platelet-
RT activating factor acetylhydrolase Ib in the Drosophila melanogaster
RT genome.";
RL Proteins 39:1-8(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., 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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP SER-167.
RX PubMed=10993674; DOI=10.1006/dbio.2000.9848;
RA Lei Y., Warrior R.;
RT "The Drosophila Lissencephaly1 (DLis1) gene is required for nuclear
RT migration.";
RL Dev. Biol. 226:57-72(2000).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11056531; DOI=10.1038/35041011;
RA Liu Z., Steward R., Luo L.;
RT "Drosophila Lis1 is required for neuroblast proliferation, dendritic
RT elaboration and axonal transport.";
RL Nat. Cell Biol. 2:776-783(2000).
RN [10]
RP FUNCTION.
RX PubMed=16105886; DOI=10.1242/jcs.02504;
RA Dzhindzhev N.S., Rogers S.L., Vale R.D., Ohkura H.;
RT "Distinct mechanisms govern the localisation of Drosophila CLIP-190 to
RT unattached kinetochores and microtubule plus-ends.";
RL J. Cell Sci. 118:3781-3790(2005).
RN [11]
RP FUNCTION, INTERACTION WITH DYNEIN AND DYNACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=16107559; DOI=10.1091/mbc.e05-04-0338;
RA Siller K.H., Serr M., Steward R., Hays T.S., Doe C.Q.;
RT "Live imaging of Drosophila brain neuroblasts reveals a role for
RT Lis1/dynactin in spindle assembly and mitotic checkpoint control.";
RL Mol. Biol. Cell 16:5127-5140(2005).
CC -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC microtubule motor protein dynein. May enhance dynein-mediated
CC microtubule sliding by targeting dynein to the microtubule plus end.
CC Required for several dynein- and microtubule-dependent processes such
CC as nuclear migration during cell division, mitotic spindle formation
CC and the removal of mitotic checkpoint proteins from kinetochores at the
CC metaphase to anaphase transition. Required for several aspects of
CC neurogenesis including neuroblast proliferation, neuronal cell
CC differentiation, dendritic growth, branching and maturation and axonal
CC transport. Required for synchronized cell divisions in the germline,
CC fusome integrity and oocyte differentiation. Acts together with BicD,
CC Egl, dynein and microtubules to determine oocyte identity during
CC oogenesis. Also required for nurse cell to oocyte transport during
CC oocyte growth and for the positioning of the nucleus in the oocyte.
CC {ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:10498683,
CC ECO:0000269|PubMed:10559989, ECO:0000269|PubMed:10993674,
CC ECO:0000269|PubMed:11056531, ECO:0000269|PubMed:16105886,
CC ECO:0000269|PubMed:16107559}.
CC -!- SUBUNIT: Interacts with dynein and dynactin. Does not interact with
CC Paf-A-Halpha. {ECO:0000269|PubMed:16107559}.
CC -!- INTERACTION:
CC Q7KNS3; P42003: Mad; NbExp=2; IntAct=EBI-156005, EBI-162238;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000255|HAMAP-
CC Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle pole. Chromosome,
CC centromere, kinetochore. Note=Localizes to the plus end of
CC microtubules. Also localizes to the mitotic spindle poles from late
CC prophase through to telophase and to kinetochore microtubules in
CC metaphase. Localization to kinetochore microtubules is reduced in
CC anaphase and telophase. In oocytes, it concentrates in the cortex from
CC stage 5 of oogenesis.
CC -!- TISSUE SPECIFICITY: Expressed primarily in germline cells during
CC oogenesis. Low levels are detected in the germarium in regions 1 and 2
CC and in both nurse cells and the oocyte in stage 2-4 egg chambers.
CC Enriched in the oocyte during stages 5-7 and in nurse cells in stage 8-
CC 10 egg chambers. Ubiquitously distributed in early embryos. Expressed
CC throughout cell bodies, dendrites and axons of the mushroom-body
CC neurons. {ECO:0000269|PubMed:10498683, ECO:0000269|PubMed:10993674,
CC ECO:0000269|PubMed:11056531}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout all developmental stages but is most abundant at
CC precellular blastoderm stages; expression declines after gastrulation.
CC Expressed at higher level in adult females. Following germ-band
CC retraction it is enriched in the developing central nervous system. In
CC third-instar larvae, low levels are detected in the brain hemispheres
CC and imaginal disks. {ECO:0000269|PubMed:10993674}.
CC -!- DOMAIN: Dimerization mediated by the LisH domain may be required to
CC activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC83821.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL90338.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF152419; AAD38390.1; -; mRNA.
DR EMBL; AF117606; AAD13113.1; -; mRNA.
DR EMBL; AF098070; AAC83821.1; ALT_INIT; mRNA.
DR EMBL; AE013599; AAO41380.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64845.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58050.1; -; Genomic_DNA.
DR EMBL; AY089600; AAL90338.1; ALT_FRAME; mRNA.
DR EMBL; BT021404; AAX33552.1; -; mRNA.
DR RefSeq; NP_001246361.1; NM_001259432.2.
DR RefSeq; NP_477160.1; NM_057812.5.
DR RefSeq; NP_788370.1; NM_176190.2.
DR RefSeq; NP_995852.1; NM_206130.2.
DR AlphaFoldDB; Q7KNS3; -.
DR SMR; Q7KNS3; -.
DR BioGRID; 62511; 26.
DR DIP; DIP-59474N; -.
DR IntAct; Q7KNS3; 2.
DR STRING; 7227.FBpp0086375; -.
DR PaxDb; Q7KNS3; -.
DR PRIDE; Q7KNS3; -.
DR DNASU; 36791; -.
DR EnsemblMetazoa; FBtr0087236; FBpp0086375; FBgn0015754.
DR EnsemblMetazoa; FBtr0087240; FBpp0086379; FBgn0015754.
DR EnsemblMetazoa; FBtr0087241; FBpp0089100; FBgn0015754.
DR EnsemblMetazoa; FBtr0304747; FBpp0293289; FBgn0015754.
DR GeneID; 36791; -.
DR KEGG; dme:Dmel_CG8440; -.
DR UCSC; CG8440-RB; d. melanogaster.
DR CTD; 36791; -.
DR FlyBase; FBgn0015754; Lis-1.
DR VEuPathDB; VectorBase:FBgn0015754; -.
DR eggNOG; KOG0295; Eukaryota.
DR GeneTree; ENSGT00940000155039; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q7KNS3; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR PhylomeDB; Q7KNS3; -.
DR Reactome; R-DME-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SignaLink; Q7KNS3; -.
DR BioGRID-ORCS; 36791; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36791; -.
DR PRO; PR:Q7KNS3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0015754; Expressed in antenna and 55 other tissues.
DR ExpressionAtlas; Q7KNS3; baseline and differential.
DR Genevisible; Q7KNS3; DM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005869; C:dynactin complex; IDA:FlyBase.
DR GO; GO:0030286; C:dynein complex; IDA:FlyBase.
DR GO; GO:0030426; C:growth cone; IDA:FlyBase.
DR GO; GO:0000776; C:kinetochore; IDA:FlyBase.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IDA:FlyBase.
DR GO; GO:0070840; F:dynein complex binding; IPI:FlyBase.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0008088; P:axo-dendritic transport; IMP:FlyBase.
DR GO; GO:0098930; P:axonal transport; IMP:UniProtKB.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0048854; P:brain morphogenesis; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0051299; P:centrosome separation; IMP:FlyBase.
DR GO; GO:0030381; P:chorion-containing eggshell pattern formation; IMP:FlyBase.
DR GO; GO:0061883; P:clathrin-dependent endocytosis involved in vitellogenesis; IDA:FlyBase.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
DR GO; GO:0016358; P:dendrite development; IMP:UniProtKB.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0048135; P:female germ-line cyst formation; IMP:FlyBase.
DR GO; GO:0045478; P:fusome organization; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0048142; P:germarium-derived cystoblast division; IMP:UniProtKB.
DR GO; GO:0030706; P:germarium-derived oocyte differentiation; IMP:UniProtKB.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:UniProtKB.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:FlyBase.
DR GO; GO:0051383; P:kinetochore organization; IMP:FlyBase.
DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:FlyBase.
DR GO; GO:0016319; P:mushroom body development; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IMP:UniProtKB.
DR GO; GO:0030473; P:nuclear migration along microtubule; IGI:FlyBase.
DR GO; GO:0051647; P:nucleus localization; IMP:FlyBase.
DR GO; GO:0030716; P:oocyte fate determination; IGI:FlyBase.
DR GO; GO:0007312; P:oocyte nucleus migration involved in oocyte dorsal/ventral axis specification; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:UniProtKB.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:FlyBase.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IDA:FlyBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:FlyBase.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:FlyBase.
DR GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IMP:FlyBase.
DR GO; GO:0019827; P:stem cell population maintenance; IDA:FlyBase.
DR GO; GO:0010970; P:transport along microtubule; IMP:FlyBase.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03141; lis1; 1.
DR InterPro; IPR017252; Dynein_regulator_LIS1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR037190; LIS1_N.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF109925; SSF109925; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 6.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Kinetochore;
KW Microtubule; Mitosis; Neurogenesis; Oogenesis; Reference proteome; Repeat;
KW Transport; WD repeat.
FT CHAIN 1..411
FT /note="Lissencephaly-1 homolog"
FT /id="PRO_0000051067"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 106..147
FT /note="WD 1"
FT REPEAT 148..187
FT /note="WD 2"
FT REPEAT 191..230
FT /note="WD 3"
FT REPEAT 233..272
FT /note="WD 4"
FT REPEAT 275..334
FT /note="WD 5"
FT REPEAT 337..376
FT /note="WD 6"
FT REPEAT 379..411
FT /note="WD 7"
FT COILED 56..83
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT MUTAGEN 128
FT /note="E->K: In Lis1-23F2; induces lethality in second
FT instar larvae."
FT /evidence="ECO:0000269|PubMed:10498683"
FT MUTAGEN 167
FT /note="S->F: In DLis8.25.3; induces defects in nuclear
FT migration."
FT /evidence="ECO:0000269|PubMed:10993674"
FT CONFLICT 2
FT /note="K -> T (in Ref. 3; AAC83821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46460 MW; 867D06C958B2D97F CRC64;
MKMVLSQRQR EELNQAIADY LGSNGYADSL ETFRKEADLS TEVEKKFGGL LEKKWTSVIR
LQKKVMELEA KLTEAEKEVI EGAPTKNKRT PGEWIPRPPE KFSLTGHRAS ITRVIFHPIF
ALMVSASEDA TIRIWDFETG EYERSLKGHT DSVQDVAFDA QGKLLASCSA DLSIKLWDFQ
QSYECIKTMH GHDHNVSSVA FVPAGDYVLS ASRDRTIKMW EVATGYCVKT YTGHREWVRM
VRVHIEGSIF ATCSNDQTIR VWLTNSKDCK VELRDHEHTV ECIAWAPEAA ASAINEAAGA
DNKKGHHQGP FLASGSRDKT IRIWDVSVGL CLLTLSGHDN WVRGLAFHPG GKYLVSASDD
KTIRVWDLRN KRCMKTLYAH QHFCTSIDFH KAHPYVISGS VDQTVKVWEC R
