LIS11_SORMK
ID LIS11_SORMK Reviewed; 460 AA.
AC D1ZEB4; F7W614;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 66.
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}; ORFNames=SMAC_06094;
OS Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=771870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT Sordaria macrospora, a model organism for fungal morphogenesis.";
RL PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000032; CCC12952.1; -; Genomic_DNA.
DR RefSeq; XP_003349399.1; XM_003349351.1.
DR AlphaFoldDB; D1ZEB4; -.
DR SMR; D1ZEB4; -.
DR STRING; 771870.D1ZEB4; -.
DR EnsemblFungi; CCC12952; CCC12952; SMAC_06094.
DR GeneID; 10806916; -.
DR KEGG; smp:SMAC_06094; -.
DR VEuPathDB; FungiDB:SMAC_06094; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; D1ZEB4; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000001881; 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; 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..460
FT /note="Nuclear distribution protein PAC1-1"
FT /id="PRO_0000405106"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 120..161
FT /note="WD 1"
FT REPEAT 163..203
FT /note="WD 2"
FT REPEAT 207..247
FT /note="WD 3"
FT REPEAT 250..289
FT /note="WD 4"
FT REPEAT 294..354
FT /note="WD 5"
FT REPEAT 355..394
FT /note="WD 6"
FT REPEAT 399..439
FT /note="WD 7"
FT REPEAT 441..460
FT /note="WD 8"
FT REGION 90..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 74..96
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 460 AA; 50602 MW; F7B9A475A1E101E8 CRC64;
MSQILTSRQA DELHRALIAY LTAANLPNTA AALREELNLG EDVFDPATAK KYEGLLEKKW
TSVVRLQKKS LTPLVTQIMD LESRNHILQS ELDNATPTSR QNKDPVAWLP RAPPRHTLQS
HRDPITCVAF HPVFSSLASG SEDQTIKIWD WELGELERTI KGHTKAVLDV DYGGPRGNTL
LASCSSDLTI KLWDPLDSYK NIRTLPGHDH SVSAVRFIPG SGNLLVSASR DKTLRIWDVS
TGYCVKTLRG HAEWVRDVCP SFDGKYILST SDDYTSRLWD VTVTNPEPRV TLIGHEHVVL
CCAIAPPAAY QNLAAMAGIK KPPATSSAEF MATGSRDKSI RLWDARGTCI KTLAGHDNWV
RGLVFHPGGK YLLSVSDDKT LRCWDLTQEG KCVKTIGDAH GHFVQCIRWA PSVIKDVSVN
GDNGEPNGTP KKGAAVTPDS QIRCVIATGS VDLNVRIFAN
