ID   LIS1_DROVI              Reviewed;         411 AA.
AC   B4LQ21;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN   Name=Lis-1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=GJ21422;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_03141}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-
CC       Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC       centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the
CC       plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-
CC       Rule:MF_03141}.
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}.
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DR   EMBL; CH940648; EDW60344.1; -; Genomic_DNA.
DR   RefSeq; XP_002049151.1; XM_002049115.2.
DR   RefSeq; XP_015029696.1; XM_015174210.1.
DR   RefSeq; XP_015029697.1; XM_015174211.1.
DR   AlphaFoldDB; B4LQ21; -.
DR   SMR; B4LQ21; -.
DR   STRING; 7244.FBpp0235839; -.
DR   EnsemblMetazoa; FBtr0237347; FBpp0235839; FBgn0208548.
DR   EnsemblMetazoa; FBtr0435270; FBpp0392258; FBgn0208548.
DR   EnsemblMetazoa; FBtr0438362; FBpp0395123; FBgn0208548.
DR   GeneID; 6626875; -.
DR   KEGG; dvi:6626875; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   InParanoid; B4LQ21; -.
DR   OMA; TQECKCV; -.
DR   OrthoDB; 995692at2759; -.
DR   PhylomeDB; B4LQ21; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:UniProtKB-UniRule.
DR   GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..411
FT                   /note="Lissencephaly-1 homolog"
FT                   /id="PRO_0000405048"
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"
SQ   SEQUENCE   411 AA;  46413 MW;  862C0F92AEE93A31 CRC64;
     MKMVLSQRQR EELNQAIADY LGSNGYADSL EAFRKEADLS TEAEKKFGGL LEKKWTSVIR
     LQKKVMELEA KLTEAEKEVI EGAPTKNKRT PGEWIPRPPE KYSLTGHRAS ITRVIFHPIF
     GLMVSASEDA TIKIWDFETG EYERSLKGHT DSVQDVAFDA QGKLLASCSA DLSIKLWDFQ
     QSYECVKTMH GHDHNVSSVA FVPAGDYVLS ASRDRTIKMW EVATGYCVKT YTGHREWVRM
     VRVHIEGSIF ATCSNDHTIR VWLTNSKDCK VELRDHEHTV ECIAWAPEAA ASAINEAAGA
     DNKKGHHQGP FLASGSRDKT IRIWDVSVGQ CLLTLNGHDN WVRGLAFHPG GKYLVSASDD
     KTIRVWDLRN KRCMKTLYAH QHFCTSIDFH KAHPYVISGS VDQTVKVWEC R