LIS1_YEAS1
ID LIS1_YEAS1 Reviewed; 494 AA.
AC B3LJT5;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
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}; ORFNames=SCRG_01651;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408045; EDV10838.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LJT5; -.
DR SMR; B3LJT5; -.
DR TopDownProteomics; B3LJT5; -.
DR EnsemblFungi; EDV10838; EDV10838; SCRG_01651.
DR HOGENOM; CLU_000288_57_15_1; -.
DR Proteomes; UP000008335; Unassembled 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:0000922; C:spindle pole; 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; 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; Repeat; Transport; WD repeat.
FT CHAIN 1..494
FT /note="Nuclear distribution protein PAC1"
FT /id="PRO_0000405103"
FT DOMAIN 14..46
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 153..192
FT /note="WD 1"
FT REPEAT 196..244
FT /note="WD 2"
FT REPEAT 251..292
FT /note="WD 3"
FT REPEAT 295..334
FT /note="WD 4"
FT REPEAT 347..395
FT /note="WD 5"
FT REPEAT 415..454
FT /note="WD 6"
FT REPEAT 457..492
FT /note="WD 7"
FT COILED 90..123
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 494 AA; 56841 MW; 9B4B16870969E327 CRC64;
MTNWQQQLPL TDTQKNELDK SVLRYLNWNY KQTVRHEHAQ DYESVRHAIV TLSGFLLQES
VDRQEFISNN DTSNESMVDI DELLLPKKWN SIVRLQKKII ELEQNTETLV SQIKDLNTQV
SELAQFKPTT SNGASAHNVL KWIPRNLPSC LINVESSVTS VKLHPNLPIV FVATDHGKLY
AFDLFNYTIP LASLQSHTKA ITSMDVLFTN FTNSSKKNYL VVVTASKDLQ IHVFKWVSEE
CKFQQIRSLL GHEHIVSAVK IWQKNNDVHI ASCSRDQTVK IWDFHNGWSL KTFQPHSQWV
RSIDVLGDYI ISGSHDTTLR LTHWPSGNGL SVGTGHEFPI EKVKFIHFIE DSPEIRFRTP
STDRYKNWGM QYCVSASRDR TIKIWEIPLP TLMAHRAPIP NPTDSNFRCV LTLKGHLSWV
RDISIRGQYL FSCADDKSVR CWDLNTGQCL HVWEKLHTGF VNCLDLDVDF DSNVTPRQMM
VTGGLDCKSN VFMR
