LIS1_ASPFN
ID LIS1_ASPFN Reviewed; 455 AA.
AC B8N9H4;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Nuclear distribution protein nudF {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};
GN Name=nudF {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=lis1 {ECO:0000255|HAMAP-Rule:MF_03141}; ORFNames=AFLA_111200;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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 -!- SEQUENCE CAUTION:
CC Sequence=EED53743.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EQ963475; EED53743.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002376989.1; XM_002376948.1.
DR AlphaFoldDB; B8N9H4; -.
DR SMR; B8N9H4; -.
DR STRING; 5059.CADAFLAP00004854; -.
DR EnsemblFungi; EED53743; EED53743; AFLA_111200.
DR eggNOG; KOG0295; Eukaryota.
DR Proteomes; UP000001875; 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; Repeat; Transport; WD repeat.
FT CHAIN 1..455
FT /note="Nuclear distribution protein nudF"
FT /id="PRO_0000405068"
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..239
FT /note="WD 3"
FT REPEAT 242..281
FT /note="WD 4"
FT REPEAT 287..347
FT /note="WD 5"
FT REPEAT 349..388
FT /note="WD 6"
FT REPEAT 392..438
FT /note="WD 7"
FT REPEAT 440..455
FT /note="WD 8"
FT REGION 408..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 61..88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 455 AA; 50557 MW; FA338E21ECDD82C5 CRC64;
MPPLLTNRQA EELHKSMIAY LVASDLPDTA AALRREVNLS EDVFDPTTAK RYEGMLEKKW
TSIARLQKKI MDLESRNATL QSELDNSTPA SRLKRNQDPA SWLPSTVRYS LESHRDKVNC
VAFHPTFSSI ASGSDDCTIK IWDWELGELE RTLKGHTRAV RDVDYGGPRD NVLLASCSSD
LSIKLWKPTD NYKNIRTLQG HDHIVSAVRF IPSRNLLVSA SRDNDMRIWD VTTGYCVKTI
NGHTDWVRDV SISFDGRFLF STGQDMTARL WDISTVSNIE HKRTMLGHEN FIECCAFAPP
TSYQFLAPLA GLGKRPSSTN GADFMATGSR DNTIKIWDSR GTCLMTLVGH DSWVQALVFH
PGGKYLLSVS DDKTLRCWDL NQQGKCVKTL DAHESFVTSL RWAPGVAKNV PGGDGAAEGE
GNDKNGAGSE NPANIQMRCV VATGGWDQKL KIFAG
