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LIS1_ASPTN
ID   LIS1_ASPTN              Reviewed;         446 AA.
AC   Q0D0X6;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=ATEG_00408;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CH476594; EAU39054.1; -; Genomic_DNA.
DR   RefSeq; XP_001210494.1; XM_001210494.1.
DR   AlphaFoldDB; Q0D0X6; -.
DR   SMR; Q0D0X6; -.
DR   STRING; 341663.Q0D0X6; -.
DR   PRIDE; Q0D0X6; -.
DR   EnsemblFungi; EAU39054; EAU39054; ATEG_00408.
DR   GeneID; 4355162; -.
DR   VEuPathDB; FungiDB:ATEG_00408; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   OMA; TQECKCV; -.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000007963; 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; 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; 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..446
FT                   /note="Nuclear distribution protein nudF"
FT                   /id="PRO_0000405071"
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..240
FT                   /note="WD 3"
FT   REPEAT          243..282
FT                   /note="WD 4"
FT   REPEAT          285..345
FT                   /note="WD 5"
FT   REPEAT          347..386
FT                   /note="WD 6"
FT   REPEAT          391..430
FT                   /note="WD 7"
FT   REPEAT          432..446
FT                   /note="WD 8"
FT   COILED          60..86
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   446 AA;  48994 MW;  DDCEB614FB74B6F8 CRC64;
     MSQILTASQA EELHKSMVAY LSSIKASQSS NTLREELGIG DNFDEATCKK YEGLLEKKWT
     GIARLQRKIL DLESKITSLQ AELDSVPSMA RSKQHQDPDN WLPAQSSAHT FESHRDAITS
     IAFHPVFTSL ASGSEDCTIK IWDWELGELE RTLKGHMRGV SGLDFGGQKG HTLLASCSGD
     LTIKLWDPSK DYANIRTLHG HDHSVSAVRF LTSTENLLVS ASRDASIRIW DVSTGYCVRT
     ITSNSIWFLD VSPSFDGKWL VAGGRDQAVT VWEVSSAEPR AALLGHDNDV QCCVFAPPAS
     YEYLATLAGH KKAPLASSSS EFIATGSRDK TIKLWEARGR LIKTLVGHDN WIRGLVFHPS
     GKYLFSVSDD KTIRCWDLSQ EGRLVKTISN AHGHFISCIR WAPPPRNAAA EASETTNGVS
     KKAPTKPAFQ CVIATGSADS CVRVFK
 
 
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