LIS1_YARLI
ID LIS1_YARLI Reviewed; 437 AA.
AC Q6CG48;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Nuclear distribution protein PAC1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=nudF homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=PAC1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN OrderedLocusNames=YALI0B00902g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC microtubule motor protein dynein. Plays a central role in positioning
CC the mitotic spindle at the bud neck during cell division. Targets
CC cytoplasmic dynein to microtubule plus ends, thereby promoting dynein-
CC mediated microtubule sliding along the bud cortex and consequently the
CC movement of the mitotic spindle to the bud neck. {ECO:0000255|HAMAP-
CC Rule:MF_03141}.
CC -!- SUBUNIT: Self-associates. Interacts with NDL1 and dynein.
CC {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC spindle pole {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the
CC plus ends of microtubules and the mitotic spindle poles.
CC {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; CR382128; CAG82578.1; -; Genomic_DNA.
DR RefSeq; XP_500364.1; XM_500364.1.
DR AlphaFoldDB; Q6CG48; -.
DR SMR; Q6CG48; -.
DR STRING; 4952.CAG82578; -.
DR EnsemblFungi; CAG82578; CAG82578; YALI0_B00902g.
DR GeneID; 2906884; -.
DR KEGG; yli:YALI0B00902g; -.
DR VEuPathDB; FungiDB:YALI0_B00902g; -.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q6CG48; -.
DR OMA; TQECKCV; -.
DR Proteomes; UP000001300; Chromosome B.
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:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 5.
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; 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..437
FT /note="Nuclear distribution protein PAC1"
FT /id="PRO_0000240430"
FT REPEAT 114..153
FT /note="WD 1"
FT REPEAT 156..217
FT /note="WD 2"
FT REPEAT 221..260
FT /note="WD 3"
FT REPEAT 263..301
FT /note="WD 4"
FT REPEAT 304..356
FT /note="WD 5"
FT REPEAT 358..397
FT /note="WD 6"
FT REPEAT 401..437
FT /note="WD 7"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..94
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COMPBIAS 170..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 48180 MW; B6F73C53D6E785DA CRC64;
MESLLTDKQR SDLETSIFGY VSRLTNDEAL LSQLAAVLSQ PSGSEPVPAD TLKANALLLE
KKWLSVIRLQ RKVMDLETRL EAAEREASST HKANGLGAGD PKTWLPKTSR FSLLHKQPVN
AVSFHPFHST LASACEDGNI RIWDYELGEI ETTIKAHTRG VLDVDFSQPD TGASRDKSHD
KPRADVSHAQ PRALLVSCSS DLTIRIWDPQ NEYANVKTLT GHDHTISAVK FTASGNHVIS
ASRDKTVRVW SVQSGYCVRT VHGHTDWVKS CAALNEEFIF SAGIDHVTRV SEFVSGDGKM
TLLGHEHVIE GVAVYPKSAA GCLAKLDKTS SYFVVSWSRD KTIRVWSSRG DPLLILRGHD
NWVRGVVLHP AGRYLVSVSD DKTMRCWDLE QGGRCIRVVD AHGHFVTCVA WAPNDVNGRV
RCLVATGGVD GQVKVWQ
