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LIS1_SCLS1
ID   LIS1_SCLS1              Reviewed;         458 AA.
AC   A7EKM8;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Nuclear distribution protein PAC1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE   AltName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
DE            Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
DE   AltName: Full=nudF homolog {ECO:0000255|HAMAP-Rule:MF_03141};
GN   Name=pac1; Synonyms=lis1 {ECO:0000255|HAMAP-Rule:MF_03141};
GN   ORFNames=SS1G_05875;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476627; EDO03394.1; -; Genomic_DNA.
DR   RefSeq; XP_001592953.1; XM_001592903.1.
DR   AlphaFoldDB; A7EKM8; -.
DR   SMR; A7EKM8; -.
DR   STRING; 665079.A7EKM8; -.
DR   EnsemblFungi; EDO03394; EDO03394; SS1G_05875.
DR   GeneID; 5489425; -.
DR   KEGG; ssl:SS1G_05875; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   InParanoid; A7EKM8; -.
DR   OMA; TQECKCV; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR   GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR   GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR   GO; GO:0051012; P:microtubule sliding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
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; 6.
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..458
FT                   /note="Nuclear distribution protein PAC1"
FT                   /id="PRO_0000405105"
FT   DOMAIN          9..41
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          113..152
FT                   /note="WD 1"
FT   REPEAT          155..196
FT                   /note="WD 2"
FT   REPEAT          200..247
FT                   /note="WD 3"
FT   REPEAT          250..289
FT                   /note="WD 4"
FT   REPEAT          292..352
FT                   /note="WD 5"
FT   REPEAT          354..393
FT                   /note="WD 6"
FT   REPEAT          398..440
FT                   /note="WD 7"
FT   REGION          81..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          60..87
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   COMPBIAS        81..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  49778 MW;  85B8C8CF017F4B95 CRC64;
     MSQLLTSRQA EELHKSMIAY LNSANLLHSA ATLREELDIG ESFDSATSKK YEGLLEKKWT
     SVVRLQKKIM DLESRNAALQ SEIDNATPTS LSNRNTDPTA WLPKSPARHN LQSHREAITC
     VAFHPVFSSL ASGSEDCTIK IWDWELGELE LTVKGHTRAV LDVDFGGPRG GTLLASCSSD
     LTIKLWDPSD QYKNIRTLPG HDHSVSAVRF IPSGAAGSPS SGNLLVSASR DKTLRIWDVS
     TGYCVKTVRG HADWVRDVAP SYDGRWLLSA GVDQTARIWD ASSGEPKATL LGHENTIECC
     VFAPPASYPH LAAMAGLKKP PAASSSAEYI ATGARDKSIR IWDARGTLIK TLIGHDNWIR
     ALVFHPGGKY LLSVADDRTL RCWDLAQEGK CVKTISDAHG HFVSCMRWAP SVIKDAPLLN
     GENGVGTPIK NGNGATKKED AKGSDIDCTS LMPQIPSI
 
 
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