LIS1_KLULA
ID LIS1_KLULA Reviewed; 439 AA.
AC Q6CU55;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=KLLA0C07513g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382123; CAH01385.1; -; Genomic_DNA.
DR RefSeq; XP_452534.1; XM_452534.1.
DR AlphaFoldDB; Q6CU55; -.
DR SMR; Q6CU55; -.
DR STRING; 28985.XP_452534.1; -.
DR EnsemblFungi; CAH01385; CAH01385; KLLA0_C07513g.
DR GeneID; 2892206; -.
DR KEGG; kla:KLLA0_C07513g; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q6CU55; -.
DR OMA; LTHWPSG; -.
DR Proteomes; UP000000598; 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; -; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
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; 2.
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..439
FT /note="Nuclear distribution protein PAC1"
FT /id="PRO_0000405080"
FT REPEAT 106..145
FT /note="WD 1"
FT REPEAT 149..193
FT /note="WD 2"
FT REPEAT 199..240
FT /note="WD 3"
FT REPEAT 243..282
FT /note="WD 4"
FT REPEAT 295..335
FT /note="WD 5"
FT REPEAT 355..392
FT /note="WD 6"
FT REPEAT 402..438
FT /note="WD 7"
FT COILED 55..90
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 439 AA; 49514 MW; 0CA83D26C7734E44 CRC64;
MLTYKQRQSL NHAICDYVRQ NEGSDELLVQ LESVLLPNGS DVIPQDPNLL ERKWNSIVRL
QSKIMELEKN CEELQKSIDE QQSSTNQISN ASSDWCPRDT PSFQITLDAS ITALCLHPSL
PIIFIGLDSG KLLRYDILNV ELPLQSTMAH MDGITSISIS LPNENGRPAY LATTSKDLNT
KIWELELDST LSHIKTLAGH EHTVSDCQFF ERGADLLLAT CSRDLYLKIW DISNGWCIKS
FQPHTQWIRS LHVHGEFVLT GSNDSAIRLT HWPSGNGLSM GIGHDFPVEK VLILIPDPQH
LQPQYQPLGF QHVASASRDG TIRLWKVSLP KFIPHRPPRP NPLDTTFKVI AVLTDHNSWV
RDLRQFNDML FSCSDDGSVK CWSLDWTNLS TTTCKKSWDL SNKGFQNCLT LDNIAFTGLP
SRKLLFSGSS EGTLTSFMR