LIS12_ASPCL
ID LIS12_ASPCL Reviewed; 435 AA.
AC A1CF18;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Nuclear distribution protein nudF 2 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 homolog 2 {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=nudF-2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=lis1-2 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=ACLA_091650;
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; DS027052; EAW11467.1; -; Genomic_DNA.
DR RefSeq; XP_001272893.1; XM_001272892.1.
DR AlphaFoldDB; A1CF18; -.
DR SMR; A1CF18; -.
DR STRING; 5057.CADACLAP00008295; -.
DR EnsemblFungi; EAW11467; EAW11467; ACLA_091650.
DR GeneID; 4705134; -.
DR KEGG; act:ACLA_091650; -.
DR VEuPathDB; FungiDB:ACLA_091650; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR OMA; LTHWPSG; -.
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; 3.
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..435
FT /note="Nuclear distribution protein nudF 2"
FT /id="PRO_0000405067"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 86..125
FT /note="WD 1"
FT REPEAT 128..171
FT /note="WD 2"
FT REPEAT 175..214
FT /note="WD 3"
FT REPEAT 217..256
FT /note="WD 4"
FT REPEAT 280..320
FT /note="WD 5"
FT REPEAT 322..361
FT /note="WD 6"
FT REPEAT 366..396
FT /note="WD 7"
FT REPEAT 397..434
FT /note="WD 8"
SQ SEQUENCE 435 AA; 48261 MW; 7373A884CAAE83ED CRC64;
MARLLTNSQA EELHKSIIAY LSANGLPETT AILRKELGVT EHDFNATAVK KYETLLEKNG
PLLFAYRESR DSKAWLPQRP RYSLHSHRDT INCIAFHPKY SSIASGSDDC TIKIWDWELG
ELEVTLKGHT RAVRDLDYGS PPGAVGVLLA SCSSDLTIKL WDPADGYKNI RTLQGHDHIV
SAVRFIPNGS LLASASRDMD VRLWDVTNGY CVKTIQGHTG WVRDVCASLD GRFILSTGDD
MTVRLWDISA KPENKLTMVG HENFNECCAI APPTSYQYLA PLARLAKVSR AGSTAEFMAT
GSRDKTIKLW DARGTCLMTL TGHDNWVRAI VFHPGGRYLL SVSDDKTLRC WDLSQEGKCV
KTIRDTHGGF ITCLRWAPAI LKDTPTDAAR ALVRQIPDVA EIMKNATFEE SFSDVQIRCV
VATGSVDKKL QIFAG
