ID   LIS11_PARTE             Reviewed;         403 AA.
AC   A0DB19;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Lissencephaly-1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN   ORFNames=GSPATT00015130001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA   Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA   Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA   Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA   Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E.,
RA   Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
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; CT868363; CAK80236.1; -; Genomic_DNA.
DR   RefSeq; XP_001447633.1; XM_001447596.1.
DR   AlphaFoldDB; A0DB19; -.
DR   SMR; A0DB19; -.
DR   STRING; 5888.CAK80236; -.
DR   EnsemblProtists; CAK80236; CAK80236; GSPATT00015130001.
DR   GeneID; 5033432; -.
DR   KEGG; ptm:GSPATT00015130001; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   InParanoid; A0DB19; -.
DR   OMA; TQECKCV; -.
DR   Proteomes; UP000000600; Partially assembled 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; 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; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
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..403
FT                   /note="Lissencephaly-1 homolog 1"
FT                   /id="PRO_0000405057"
FT   DOMAIN          7..38
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          103..142
FT                   /note="WD 1"
FT   REPEAT          145..184
FT                   /note="WD 2"
FT   REPEAT          187..226
FT                   /note="WD 3"
FT   REPEAT          229..270
FT                   /note="WD 4"
FT   REPEAT          271..327
FT                   /note="WD 5"
FT   REPEAT          330..369
FT                   /note="WD 6"
FT   REPEAT          373..403
FT                   /note="WD 7"
FT   COILED          51..87
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   403 AA;  46072 MW;  F588E527C96D644A CRC64;
     MVLTARQRDE LNQAIHQYLL ISYQQSAQLF KTEAAVKDGQ IEADLLEKKW NSIVRLSKRV
     ITLEQQVEQL NEQLAQAQAG KIQFNKSDDE QRLTPIEKFK LEGHRAGVNC VAFHPQYQIL
     GSASDDGSIK LWDYESGHFE KTLKGHTSNV NCLAFDPTGK YICSASSDLS IKIWELKNHT
     CVKTLIGHEH SVSTVQFSDH GDFILSASRD KNIKLWEVAT GFCKKTFSEH QEWVRCAVFS
     NDEKQIASCS QDQMIYIWVI DSGQVLHQLS GHEHVVEQVK YIPEHGAKQI LTQQQQQNIQ
     TINLLVSVSR DKEIKIWNTI LGTNLFTLSG HDNWVNGVSF HPDGVHMLSV SDDKTIRVWN
     LKEQKQKKKI ENAHDKFILK CEINKFIFAT CSVDQTIKLW LLS