ID   LIS1_POLPP              Reviewed;         417 AA.
AC   D3BUN1;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN   ORFNames=PPL_11852;
OS   Polysphondylium pallidum (strain ATCC 26659 / Pp 5 / PN500) (Heterostelium
OS   pallidum).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Acytosteliales;
OC   Acytosteliaceae; Heterostelium.
OX   NCBI_TaxID=670386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26659 / Pp 5 / PN500;
RX   PubMed=21757610; DOI=10.1101/gr.121137.111;
RA   Heidel A.J., Lawal H.M., Felder M., Schilde C., Helps N.R., Tunggal B.,
RA   Rivero F., John U., Schleicher M., Eichinger L., Platzer M., Noegel A.A.,
RA   Schaap P., Gloeckner G.;
RT   "Phylogeny-wide analysis of social amoeba genomes highlights ancient
RT   origins for complex intercellular communication.";
RL   Genome Res. 21:1882-1891(2011).
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; ADBJ01000060; EFA74819.1; -; Genomic_DNA.
DR   AlphaFoldDB; D3BUN1; -.
DR   SMR; D3BUN1; -.
DR   STRING; 670386.D3BUN1; -.
DR   OMA; TQECKCV; -.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000001396; 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; 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..417
FT                   /note="Lissencephaly-1 homolog"
FT                   /id="PRO_0000405056"
FT   DOMAIN          7..39
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          102..143
FT                   /note="WD 1"
FT   REPEAT          144..185
FT                   /note="WD 2"
FT   REPEAT          186..225
FT                   /note="WD 3"
FT   REPEAT          228..267
FT                   /note="WD 4"
FT   REPEAT          270..339
FT                   /note="WD 5"
FT   REPEAT          342..383
FT                   /note="WD 6"
FT   REPEAT          385..417
FT                   /note="WD 7"
FT   REGION          72..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          52..80
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   COMPBIAS        78..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   417 AA;  46327 MW;  174D575C69C83140 CRC64;
     MVLTNKQKEE LNGAILDYFD SSGYKLTSTE FTKETNIELD PKLKGLLEKK WTSVIRLQKK
     VMDLEAKVSQ LEEELNNGGR GPARRGKEDA LPRQPEKHVL TGHRNCINAV RFHPLFSVIV
     SASEDATMRI WDFDSGDFER TLKGHTNAVQ DIDFDKSGNL LASCSADLTI KLWDFQSFDC
     IKTLHGHDHN VSCVRFLPSG DQLVSSSRDK SIKVWETATG YCTKTLTGHE DWVRKVIVSE
     DGTTLASCSN DQTARVWNLA KGECLLTFRE HSHVVECLAY SPANIVEVPG SLLSTPEGKA
     KAKAGAGGTS FGQAGYLATG SRDKTIKIWE LATGRCLQTY IGHDNWVRSI KFHPCGKYLI
     SVGDDKSIRV WDIAQGRCIK TINEAHSHFI SCLDFCSHNP HIATGGVDDI IKIWKLG