LIS1_CANGA
ID LIS1_CANGA Reviewed; 467 AA.
AC Q6FWT9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 118.
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=CAGL0C02937g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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 {ECO:0000255|HAMAP-
CC Rule:MF_03141}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus ends of
CC microtubules and the mitotic spindle poles. {ECO:0000255|HAMAP-
CC 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; CR380949; CAG58211.1; -; Genomic_DNA.
DR RefSeq; XP_445305.1; XM_445305.1.
DR AlphaFoldDB; Q6FWT9; -.
DR SMR; Q6FWT9; -.
DR STRING; 5478.XP_445305.1; -.
DR EnsemblFungi; CAG58211; CAG58211; CAGL0C02937g.
DR GeneID; 2886739; -.
DR KEGG; cgr:CAGL0C02937g; -.
DR CGD; CAL0127484; CAGL0C02937g.
DR VEuPathDB; FungiDB:CAGL0C02937g; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q6FWT9; -.
DR OMA; LTHWPSG; -.
DR Proteomes; UP000002428; Chromosome C.
DR GO; GO:0005881; C:cytoplasmic microtubule; IEA:EnsemblFungi.
DR GO; GO:0005875; C:microtubule associated complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0070840; F:dynein complex binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:EnsemblFungi.
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 GO; GO:0030473; P:nuclear migration along microtubule; IEA:EnsemblFungi.
DR GO; GO:1903033; P:positive regulation of microtubule plus-end binding; IEA:EnsemblFungi.
DR Gene3D; 2.130.10.10; -; 2.
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; 3.
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; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
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..467
FT /note="Nuclear distribution protein PAC1"
FT /id="PRO_0000405074"
FT REPEAT 121..160
FT /note="WD 1"
FT REPEAT 164..212
FT /note="WD 2"
FT REPEAT 219..262
FT /note="WD 3"
FT REPEAT 264..302
FT /note="WD 4"
FT REPEAT 325..365
FT /note="WD 5"
FT REPEAT 385..424
FT /note="WD 6"
FT REPEAT 426..466
FT /note="WD 7"
FT COILED 62..96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 467 AA; 52501 MW; D5C956FA256BFFAB CRC64;
MSSLTDSQVN DLHCSIYRYV QWVSQNNGSS DLLNKLQSVL DIDELQLSLD DGDQMLLPKK
WGSIIRLQRA ITKLEQKCDA LQQELDDKTK QLETIVPKDT QIATTTDVNW LPPDHIYASI
QNESPVTAIK LHPSLAIVYV GTDTGRLIAY DILNYTIPLA VTTAHSKAIT SIEVIEAHNF
EEFIDSTTLV STTSKDAQIN VYDHSSNTGE LKLIRSFNAH DSTVSSQKTW QKDNDVLLAS
SSRDATVKVW RVNDSRCLQS FSPHSEWVKS IDVLDEYILS GSLDSTLRLT HWPSGNGLSV
GTGHEFPIER VLIIPFSDSK ICTSPYRDQN EHSAFAPLRF KYCASAARDN TIKIWEVPLP
QLKPNSAPVP STTNTTFKCV MTLRGHTSWV KDLKLRGDHL FSCSDDETIK CWDLNTGNCV
KTWSSIHNNF INCIDIDREA TIEQFSPSLQ REILVSGDMD NKVKIIR
