LIS12_PODAN
ID LIS12_PODAN Reviewed; 468 AA.
AC B2B766; A0A090CK24;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Nuclear distribution protein PAC1-2 {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};
DE AltName: Full=nudF homolog 2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=PAC1-2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1-2 {ECO:0000255|HAMAP-Rule:MF_03141};
GN OrderedLocusNames=Pa_2_10070; ORFNames=PODANS_2_10070;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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 NDL1 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; CU640366; CAP73644.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP26047.1; -; Genomic_DNA.
DR RefSeq; XP_001911816.1; XM_001911781.1.
DR AlphaFoldDB; B2B766; -.
DR SMR; B2B766; -.
DR STRING; 5145.XP_001911816.1; -.
DR EnsemblFungi; CAP73644; CAP73644; PODANS_2_10070.
DR GeneID; 6195508; -.
DR KEGG; pan:PODANSg8861; -.
DR VEuPathDB; FungiDB:PODANS_2_10070; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000001197; Chromosome 2.
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; 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..468
FT /note="Nuclear distribution protein PAC1-2"
FT /id="PRO_0000405097"
FT DOMAIN 13..45
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 118..159
FT /note="WD 1"
FT REPEAT 161..201
FT /note="WD 2"
FT REPEAT 205..251
FT /note="WD 3"
FT REPEAT 254..293
FT /note="WD 4"
FT REPEAT 298..358
FT /note="WD 5"
FT REPEAT 360..399
FT /note="WD 6"
FT REPEAT 404..429
FT /note="WD 7"
FT REPEAT 430..468
FT /note="WD 8"
FT COILED 66..92
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 468 AA; 51164 MW; 9F04A42DA3353016 CRC64;
MTMASRSFLT DRQAEELHKS IIAYLTSLNL ATTANTLRAE LNLPEETFDL AKAKQYEGLL
EKKWTSVIRL QKKVLDLQAE NAHLKNEIEN AGPLALSRKN QDPANWLPKG PPRYTLEGHR
LPITSVAFHP VFSSLASASE DNTIKIWDWE LGELERTLKG HTKAVLDVDF GGPRGNTLLA
SCSSDMSIKL WDPADQYKNI RTLHGHDHIV SSVRFVPANG TAGAGGNLLV SASKDNTLKL
WDVTTGYCVK TIEGHNDWPR AVAPSADGRW LLSTGSDKAA RLWDIGGTEP ECRVVMFGHE
NFNLCCEFAP STSYPHLARL AGHEKVPPAN SAAEFMATGS RDKQIRLWDR RGQCIKVLEG
HDNWVRGLAF HPAGKFLISV ADDRTMRCWD LSQDGKCVQT LSGMFDGFVS CVRWAPGITK
DGLAGGDAGD GTPKKKTGAE ANGGVQMRCV VATGSVDGTE GKVRIFAN
