LIS12_SORMK
ID LIS12_SORMK Reviewed; 486 AA.
AC D1ZEM6; F7W444;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 63.
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}; ORFNames=SMAC_05575;
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; CABT02000026; CCC12398.1; -; Genomic_DNA.
DR RefSeq; XP_003349292.1; XM_003349244.1.
DR AlphaFoldDB; D1ZEM6; -.
DR SMR; D1ZEM6; -.
DR STRING; 771870.D1ZEM6; -.
DR EnsemblFungi; CCC12398; CCC12398; SMAC_05575.
DR GeneID; 10806775; -.
DR KEGG; smp:SMAC_05575; -.
DR VEuPathDB; FungiDB:SMAC_05575; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; D1ZEM6; -.
DR OMA; GHENYNL; -.
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..486
FT /note="Nuclear distribution protein PAC1-2"
FT /id="PRO_0000405107"
FT DOMAIN 15..47
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 121..162
FT /note="WD 1"
FT REPEAT 164..204
FT /note="WD 2"
FT REPEAT 208..255
FT /note="WD 3"
FT REPEAT 258..297
FT /note="WD 4"
FT REPEAT 303..363
FT /note="WD 5"
FT REPEAT 365..404
FT /note="WD 6"
FT REPEAT 446..485
FT /note="WD 7"
FT COILED 70..95
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ SEQUENCE 486 AA; 52883 MW; 0F1077404A0AAF14 CRC64;
MAQAQIGTPL LTTRQAEELH KSILAYLSSK NLASTAATLR DELPDLAEVT FDTEKAKKYE
GLLEKKWTSV VRLQKKILDL ESRNTLLQSE IDNATPSSLS RRTQDPTNWL PKAPPRYVLE
SHRLPVTCVA FHPVFTSLAS GSEDYTIKIW DWELGELERT IKGHTKAVLD VDFGGPRGGT
LLASCSSDLT IKLWDPSDEY KNIRTLPGHD HIVSSVRFIP SGAAGAPASG NLLVSASKDN
SLKIWDVTTG YCVKTILGHV DWPRAVCPSH DGRYLLSTGS DKSVRLWDLA GGRDAECRLV
MFGHENYNLC CAFAPPTAYA YLAKLAGLDR PPPLGASAEF MATGSRDKQI RLWDGRGNCV
KVLVGHDNWV RGLVFHPGGK YLLSVADDRT MRCWDLSQEG KCVQTLTGVY EGFVSCIRWA
PPVVKDADAM AANTKSGGTG PLADTVVAAR RRAATVGSVN ASVQIRCVVA TGSVDGTEGK
VRIFAN
