LIS1_ASHGO
ID LIS1_ASHGO Reviewed; 461 AA.
AC Q759U7;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-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}; OrderedLocusNames=ADR176W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52096.1; -; Genomic_DNA.
DR RefSeq; NP_984272.1; NM_209625.2.
DR AlphaFoldDB; Q759U7; -.
DR SMR; Q759U7; -.
DR STRING; 33169.AAS52096; -.
DR EnsemblFungi; AAS52096; AAS52096; AGOS_ADR176W.
DR GeneID; 4620434; -.
DR KEGG; ago:AGOS_ADR176W; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q759U7; -.
DR OMA; LTHWPSG; -.
DR Proteomes; UP000000591; Chromosome IV.
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; 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; 3.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
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; 2.
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..461
FT /note="Nuclear distribution protein PAC1"
FT /id="PRO_0000405065"
FT REPEAT 118..157
FT /note="WD 1"
FT REPEAT 161..203
FT /note="WD 2"
FT REPEAT 209..252
FT /note="WD 3"
FT REPEAT 254..292
FT /note="WD 4"
FT REPEAT 318..362
FT /note="WD 5"
FT REPEAT 382..421
FT /note="WD 6"
FT REPEAT 423..461
FT /note="WD 7"
FT COILED 64..93
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 461 AA; 52250 MW; 0724D538DE642AC6 CRC64;
MSQHHILPQH QRADLNRSIC DYVQRCGAEE SLVVGLRQLF GLSAEECDAT RNGRDPDLLL
KKWNSIIRLH RKILDLEQKC QQLTEELEAV PTEAYGKAGR GVSHVLWTPR SNPTFQLDVG
ASVTDIKLHP SLPIAFLATD QGKVVAYDLF NRSMPLHSTQ AHMKGVTSLA VMEAENGSLL
ISTTSKDLQC KIWSFTDNAA FQLLRTLSSH EHIVSQSCFL RSGSDLLLAT CSRDLTVKVW
DTKSGWCIKS FQPHNQWVRT LELHGDYVIT GSNDATIRLS HWPSGNGLSM AVMHEFPIER
VLIIPMRANT AQKTEADDDQ VELEYRKYDP DYSPLGFKYC ISCSRDNLIV LWKIPLPKFI
PHRPPQPNLL QTNFEKVHVF KGHTSWVRDI KVRGRHLFSC SDDRSIRCWD LVTGQCLKVW
PEASHGFINC LSVDSDVSND KLLRELFLSG SIDGKCNVFM R
