ID   LIS1_MONBE              Reviewed;         410 AA.
AC   A9V790;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN   ORFNames=35260;
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154;
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
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; CH991565; EDQ86544.1; -; Genomic_DNA.
DR   RefSeq; XP_001748657.1; XM_001748605.1.
DR   AlphaFoldDB; A9V790; -.
DR   SMR; A9V790; -.
DR   STRING; 81824.XP_001748657.1; -.
DR   EnsemblProtists; EDQ86544; EDQ86544; MONBRDRAFT_35260.
DR   GeneID; 5893865; -.
DR   KEGG; mbr:MONBRDRAFT_35260; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   InParanoid; A9V790; -.
DR   OMA; LTHWPSG; -.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR   GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
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:0007097; P:nuclear migration; IBA:GO_Central.
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; PF00400; WD40; 6.
DR   PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
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; 5.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
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..410
FT                   /note="Lissencephaly-1 homolog"
FT                   /id="PRO_0000405115"
FT   DOMAIN          7..39
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          104..143
FT                   /note="WD 1"
FT   REPEAT          146..185
FT                   /note="WD 2"
FT   REPEAT          188..227
FT                   /note="WD 3"
FT   REPEAT          230..269
FT                   /note="WD 4"
FT   REPEAT          294..333
FT                   /note="WD 5"
FT   REPEAT          336..375
FT                   /note="WD 6"
FT   REPEAT          378..410
FT                   /note="WD 7"
FT   COILED          55..80
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   410 AA;  45189 MW;  72222FD5CEEEFE58 CRC64;
     MVLTARQQEE LQLAVHAYLV EAGHAEAAAA MAKSANLGDD AGDAKYTGLL EKKWTTITRL
     QKRNMELQAE VEELRSSARA PRSRTTTKME EWVPRPPATV AVDGHRLPIT AVAIHPSFAV
     MASASEDASI KLWDMESGNF ERSLKGHTNA VNDIAYDREG NRLVSCSTDM TIKVWNMDNF
     TCTKTLSGHD HTVSSVRFDH TGDRVFSASR DKTIKIWELA TGYCLQTLQG HSDWVRSIDV
     SADGAWICSA SSDHTVRVWS VASGECKHVW SDHEHVVEHA SFAPLVAHEA LNLMIFGSKP
     SAEAASKGPF VASASRDKSI CLFDVSTGQH LARLTGHDNW VRATAWSRGG RYLFSVADDK
     TMRVWDIATK RVSKTIPAHN HFVSCIAVHA KNTHVVTGSV DLKVKVWECN