LIS11_ASPCL
ID LIS11_ASPCL Reviewed; 467 AA.
AC A1CUD6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Nuclear distribution protein nudF 1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=nudF-1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=lis1-1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=ACLA_086220;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Positively regulates the activity of the minus-end directed
CC microtubule motor protein dynein. May enhance dynein-mediated
CC microtubule sliding by targeting dynein to the microtubule plus end.
CC Required for nuclear migration during vegetative growth as well as
CC development. Required for retrograde early endosome (EE) transport from
CC the hyphal tip. Required for localization of dynein to the mitotic
CC spindle poles. Recruits additional proteins to the dynein complex at
CC SPBs. {ECO:0000255|HAMAP-Rule:MF_03141}.
CC -!- SUBUNIT: Self-associates. Interacts with nudE 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 at the hyphal tip and the mitotic spindle poles.
CC {ECO:0000255|HAMAP-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; DS027060; EAW06923.1; -; Genomic_DNA.
DR RefSeq; XP_001268349.1; XM_001268348.1.
DR AlphaFoldDB; A1CUD6; -.
DR SMR; A1CUD6; -.
DR STRING; 5057.CADACLAP00007273; -.
DR EnsemblFungi; EAW06923; EAW06923; ACLA_086220.
DR GeneID; 4700403; -.
DR KEGG; act:ACLA_086220; -.
DR VEuPathDB; FungiDB:ACLA_086220; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000006701; 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; IPR006594; LisH.
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; 6.
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; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
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 nudF 1"
FT /id="PRO_0000405066"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 113..154
FT /note="WD 1"
FT REPEAT 156..196
FT /note="WD 2"
FT REPEAT 200..247
FT /note="WD 3"
FT REPEAT 250..289
FT /note="WD 4"
FT REPEAT 292..352
FT /note="WD 5"
FT REPEAT 354..393
FT /note="WD 6"
FT REPEAT 398..428
FT /note="WD 7"
FT REPEAT 429..466
FT /note="WD 8"
FT REGION 417..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..87
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COMPBIAS 425..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 50764 MW; D78D0C68D3E7563F CRC64;
MSQLLTTRQA EELHKSIIAY LASVNLSESA TTLRAELGDA VTIDDATIKK YEGLLEKKWT
SVVRLQKKIM DLESRCAALQ SELDSATPTS LLRKNQDPTA WLPRAPPRHT LESHRSPVTC
VAFHPVFSSL ASGSDDTTIK IWDWELGELE RTVKGHTKAV LDVDYGGPRG GTLLASCSSD
LTIKLWDPSD DYKNIRTLPG HDHSVSSVRF IPSGAAGSPM SGNLLVSASR DKTLRIWDVT
TGYCVKTLSG HVDWVRAVAP SIDGRFLFAA GDDRIPRLWD LSAAETRSTF LGHEHVIECV
AIAPAASYPH LAVLSGLKKP PSASSSAEFF ATGSRDKTIR LWDSRGNLIK TLVGHDNWVR
ALAFHPGGKY LLSVSDDKTI RCWDLTQECK CVRTIADTHE HFVTCLRWAP PLIKDSGANG
DAGANGTPAA TTTSNGARQD PNAANKISIR CVIATGSVDQ KVRVFAT
