ID   LIS1_USTMA              Reviewed;         453 AA.
AC   Q4P9P9; A0A0D1C4P9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 109.
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 {ECO:0000255|HAMAP-Rule:MF_03141};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16688221; DOI=10.1038/sj.emboj.7601119;
RA   Lenz J.H., Schuchardt I., Straube A., Steinberg G.;
RT   "A dynein loading zone for retrograde endosome motility at microtubule
RT   plus-ends.";
RL   EMBO J. 25:2275-2286(2006).
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 localization of dynein to the mitotic spindle
CC       poles. Recruits additional proteins to the dynein complex at SPBs (By
CC       similarity). Required for retrograde early endosome (EE) transport from
CC       the hyphal tip. {ECO:0000250, ECO:0000269|PubMed:16688221}.
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, ECO:0000269|PubMed:16688221}. Cytoplasm, cytoskeleton,
CC       spindle pole {ECO:0000255|HAMAP-Rule:MF_03141,
CC       ECO:0000269|PubMed:16688221}. Note=Localizes to the plus ends of
CC       microtubules at the hyphal tip and the mitotic spindle poles.
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; CM003147; KIS68592.1; -; Genomic_DNA.
DR   RefSeq; XP_011389620.1; XM_011391318.1.
DR   AlphaFoldDB; Q4P9P9; -.
DR   SMR; Q4P9P9; -.
DR   STRING; 5270.UM03164P0; -.
DR   EnsemblFungi; KIS68592; KIS68592; UMAG_03164.
DR   GeneID; 23563709; -.
DR   KEGG; uma:UMAG_03164; -.
DR   VEuPathDB; FungiDB:UMAG_03164; -.
DR   eggNOG; KOG0295; Eukaryota.
DR   HOGENOM; CLU_000288_57_15_1; -.
DR   InParanoid; Q4P9P9; -.
DR   OMA; TQECKCV; -.
DR   OrthoDB; 995692at2759; -.
DR   Proteomes; UP000000561; Chromosome 8.
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; SM00667; LisH; 1.
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; 5.
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..453
FT                   /note="Nuclear distribution protein PAC1"
FT                   /id="PRO_0000240429"
FT   DOMAIN          19..51
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT   REPEAT          120..161
FT                   /note="WD 1"
FT   REPEAT          162..201
FT                   /note="WD 2"
FT   REPEAT          205..244
FT                   /note="WD 3"
FT   REPEAT          247..286
FT                   /note="WD 4"
FT   REPEAT          314..355
FT                   /note="WD 5"
FT   REPEAT          356..395
FT                   /note="WD 6"
FT   REPEAT          413..452
FT                   /note="WD 7"
FT   COILED          69..96
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
SQ   SEQUENCE   453 AA;  50145 MW;  408C963C1C25C66B CRC64;
     MSGFNGTSTS SNSILSERQK DELHKSILDY FKTNNLHESF ATLMREANQE GFVPDPRAKY
     AGLLEKKWTS VIRLQKKIME MESRISQLQE ELSAAPSAKR SASLNDWLPA ASSARHTMQG
     HRLPVTKVSF HPVFSQIASA SEDTTVKLWD WETGDFERTL KGHTKAVQDV DFDSKGNYVL
     SCSSDLSIKV WDANNDYKNI KTLQGHDHSV SSVRFLPGDD YIVSASRDKT IKIWEFSTGF
     CTKTLQGHAE WVRSAIPSDD AKWLVSCSTD QTARVWDVSS GETKVELRGH EHVVEVAIFA
     PVASYAAIRQ LASLDPNASK DASASMAGQF VATGSRDKTI RIWDSISGQC LKTLTGHDNW
     VRGLAFSPNG KSLLSVSDDK TMRLWDLQSG RCTRTIEAHQ HFATGIAWGK AKIEAPIPPA
     QDGEEAGRKQ PEARTVNVVA TSSVDLTIKI WTP