LIS11_PODAN
ID LIS11_PODAN Reviewed; 464 AA.
AC B2AEZ5; A0A090D7C9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Nuclear distribution protein PAC1-1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=Lissencephaly-1 homolog 1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE Short=LIS-1 1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE AltName: Full=nudF homolog 1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Name=PAC1-1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=LIS1-1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN OrderedLocusNames=Pa_5_1030; ORFNames=PODANS_5_1030;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP62012.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU633457; CAP62012.1; ALT_SEQ; Genomic_DNA.
DR EMBL; FO904940; CDP29088.1; -; Genomic_DNA.
DR RefSeq; XP_001904234.1; XM_001904199.1.
DR AlphaFoldDB; B2AEZ5; -.
DR SMR; B2AEZ5; -.
DR STRING; 5145.XP_001904234.1; -.
DR PRIDE; B2AEZ5; -.
DR EnsemblFungi; CAP62012; CAP62012; PODANS_5_1030.
DR GeneID; 6188354; -.
DR KEGG; pan:PODANSg1252; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000001197; Chromosome 5.
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..464
FT /note="Nuclear distribution protein PAC1-1"
FT /id="PRO_0000405096"
FT DOMAIN 10..42
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..245
FT /note="WD 3"
FT REPEAT 248..287
FT /note="WD 4"
FT REPEAT 292..351
FT /note="WD 5"
FT REPEAT 353..392
FT /note="WD 6"
FT REPEAT 397..460
FT /note="WD 7"
FT REGION 78..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 62..89
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COMPBIAS 78..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 50462 MW; 1C0178C84F18E93E CRC64;
MNTNILTTRQ AEELHKAIIA YLTANNLSNT ASALRTELNL GEDVFDPATA KKYEGLLEKK
WTSVVRLQKK IMDLESRNST LQSELANSTP TSRQNKDPVA WLPKSPARHT LQSHRNPITC
VAFHPVFSSL ASGSEDQTIK IWDWELGELE RTIKGHTKAV LDVDFGGPRG NTLLASCSSD
LTIKLWDPSD DYKNIRTLPG HDHSVSAVRF IPSGVAGGTG NLLVSASRDK TLRIWDVSTG
YCVKTLRGHA EWVRDVCPSI DGRFILSTSD DYTGRLWDVS IPNPEPKTTL IGHEHVVLCC
AIAPAAAYPH LAAMAGIKKP PATSAVEFMA TGSRDKTIRL WDARGTCIKI LVGHDNWVRG
LVFHPGGQYL LSVADDYTLR CWDLTQEGRC VKTIGDAHGH FVQCIRWAPS IVKDVPAVNG
EGANGESNGT PRKAAGAAGA GGEAQIRCVI ATGSVDLNVR IFAN
