LIS1_TALSN
ID LIS1_TALSN Reviewed; 459 AA.
AC B8M0Q1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=TSTA_086670;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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 ---------------------------------------------------------------------------
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; EQ962653; EED21434.1; -; Genomic_DNA.
DR RefSeq; XP_002478397.1; XM_002478352.1.
DR AlphaFoldDB; B8M0Q1; -.
DR SMR; B8M0Q1; -.
DR STRING; 441959.B8M0Q1; -.
DR EnsemblFungi; EED21434; EED21434; TSTA_086670.
DR GeneID; 8110073; -.
DR VEuPathDB; FungiDB:TSTA_086670; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; B8M0Q1; -.
DR OMA; LTHWPSG; -.
DR OrthoDB; 995692at2759; -.
DR PhylomeDB; B8M0Q1; -.
DR Proteomes; UP000001745; 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; 2.
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..459
FT /note="Nuclear distribution protein nudF"
FT /id="PRO_0000405108"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 114..155
FT /note="WD 1"
FT REPEAT 157..197
FT /note="WD 2"
FT REPEAT 201..240
FT /note="WD 3"
FT REPEAT 243..282
FT /note="WD 4"
FT REPEAT 288..349
FT /note="WD 5"
FT REPEAT 351..390
FT /note="WD 6"
FT REPEAT 395..434
FT /note="WD 7"
FT REPEAT 436..459
FT /note="WD 8"
FT COILED 63..88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 459 AA; 50460 MW; ABA63C402DF9F87C CRC64;
MSRLLTIRQA EELHKSIIAY LSANNLTNAA AALRAELGLS EEVFDTGTMV KYETLLEKKW
TSIVRLQKKI MDLEARTVAL QTELNNATPT SLSKRNQDPA SWLPKVPARY SLESHRSTVN
CVAFHPKFSS IASGSDDSMI KIWDWELGEL EATLKGHTRS VLGVDYGTAQ SGVLLASCSS
DLSIKIWNPS DDYKNIRTLL GHEHSVSAVR FIPGRNLLVS ASRDKDLRIW DVTTGFCVKT
IQGHSGWVRD VCPSFDGNYL LSAGDDITAR LWDITNISNP EAKLTMVGHD HVIECCAVAP
QTSYQYLAPM AGVKKEAVSK LGAVEFIATG SRDKTIKVWD RRGSCLMTLV GHDNWIRAIV
FHPGGKYLLS SSDDRSIRCW DLSQDGKCVK TLSEAHGHFI SSLRWAPNVV KEVANNADSG
NGKTDSNGLL KGKDNPPNVQ IRCVVASAGV DCKLNIYAN
