ID LIS12_PENRW Reviewed; 464 AA.
AC B6GZD3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, 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=Pc12g01900;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(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; AM920427; CAP79817.1; -; Genomic_DNA.
DR RefSeq; XP_002557085.1; XM_002557039.1.
DR AlphaFoldDB; B6GZD3; -.
DR SMR; B6GZD3; -.
DR STRING; 500485.B6GZD3; -.
DR GeneID; 8315018; -.
DR KEGG; pcs:Pc12g01900; -.
DR VEuPathDB; FungiDB:PCH_Pc12g01900; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR OMA; RGTCLMT; -.
DR OrthoDB; 1798470at2759; -.
DR BioCyc; PCHR:PC12G01900-MONOMER; -.
DR Proteomes; UP000000724; Contig Pc00c12.
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 CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.960.30; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22847:SF637; WD REPEAT DOMAIN 5; 1.
DR PANTHER; PTHR22847; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF00400; WD40; 6.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
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..464
FT /note="Nuclear distribution protein nudF 2"
FT /id="PRO_0000405089"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 112..151
FT /note="WD 1"
FT REPEAT 154..195
FT /note="WD 2"
FT REPEAT 199..238
FT /note="WD 3"
FT REPEAT 241..280
FT /note="WD 4"
FT REPEAT 285..343
FT /note="WD 5"
FT REPEAT 344..383
FT /note="WD 6"
FT REPEAT 388..424
FT /note="WD 7"
FT REPEAT 426..464
FT /note="WD 8"
FT COILED 63..88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 464 AA; 51634 MW; EFC3AC49071039DD CRC64;
MPSSLTPQQA AELNKSIIAY LSAHGLAETL AAFRKESDFP DNMFDATAAK QYENLLERKW
TSNSTLMKKL LALESHNKAL RNELNSTRPS FLNRNADVND WLPQHPIRSL ESHRDSINCI
AFHPKYSLIA SGSGDLTIRI WDWEDSTLER TLKGHTMAVC DVDYGDTSSG ILLASCSSDF
TIKLWDTTDD YKNVKTLRGH DHIVSAVRFI PSGNLLASAS RDMKVILWNV INGYRVKTIE
DHTGWVRDIS PSFDGQFLLS TGDDMTVRLW EISASQPICK FTATGHENRI LCCAVAPATS
FRYLASFLES RGSTIAAEIT ATGSRDKSIK LWDSHGRCIM TLTGHASWVR AIAFHPGGKY
LLSVSDDKTM RCWDLSQQGR CVKSISNAHD GFITCLKWVP GIAKDTRNGT MTISYQRKGS
AELPRSKLDE VGQPGVQIRC VLATGGEDQK IRVFALQAND RSHK
//
