ID   LIS1_DROWI              Reviewed;         409 AA.
AC   B4MY65;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN   Name=Lis-1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=GK22131;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH963894; EDW77054.1; -; Genomic_DNA.
DR   RefSeq; XP_002066068.2; XM_002066032.2.
DR   AlphaFoldDB; B4MY65; -.
DR   SMR; B4MY65; -.
DR   STRING; 7260.FBpp0251274; -.
DR   EnsemblMetazoa; FBtr0252782; FBpp0251274; FBgn0224116.
DR   GeneID; 6643350; -.
DR   KEGG; dwi:6643350; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   InParanoid; B4MY65; -.
DR   OMA; TQECKCV; -.
DR   OrthoDB; 995692at2759; -.
DR   PhylomeDB; B4MY65; -.
DR   Proteomes; UP000007798; 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..409
FT                   /note="Lissencephaly-1 homolog"
FT                   /id="PRO_0000405049"
FT   DOMAIN          7..39
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          104..145
FT                   /note="WD 1"
FT   REPEAT          146..185
FT                   /note="WD 2"
FT   REPEAT          189..228
FT                   /note="WD 3"
FT   REPEAT          231..270
FT                   /note="WD 4"
FT   REPEAT          273..332
FT                   /note="WD 5"
FT   REPEAT          335..374
FT                   /note="WD 6"
FT   REPEAT          377..409
FT                   /note="WD 7"
FT   COILED          54..81
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   409 AA;  46122 MW;  B4D65B04ED31D85A CRC64;
     MVLSQRQREE LNQAIADYLG TNGYADSLEA FRKEADLSTE AEKKFGGLLE KKWTSVIRLQ
     KKVMELEAKL TEAEKEVIEG APTKNKRTPG EWIPRPPEKY SLTGHRASIT RVIFHPIFGL
     MVSASEDATI KIWDFETGEY ERSLKGHTDS VQDVAFDAQG KLLVSCSADL SIKLWDFQQS
     YACVKTMHGH DHNVSSVAFV PAGDYVLSAS RDRTIKMWEV ATGYCVKTYT GHREWVRMVR
     VHIEGSLFAT CSNDHTIRVW LTNSKDCKVE LRDHEHTVEC IAWAPEAAAS AINEAAGADN
     KKGHHQGPFL ASGSRDKTIR IWDVSVGLCL LTLNGHDNWV RGLAFHPGGK YLVSASDDKT
     IRVWDLRNKR CMKTLYAHQH FCTSIDFHKA HPYVISGSVD QTVKVWECR