LIS11_CHAGB
ID LIS11_CHAGB Reviewed; 454 AA.
AC Q2HBX6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=CHGG_02278;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408030; EAQ90343.1; -; Genomic_DNA.
DR RefSeq; XP_001228794.1; XM_001228793.1.
DR AlphaFoldDB; Q2HBX6; -.
DR SMR; Q2HBX6; -.
DR STRING; 38033.XP_001228794.1; -.
DR EnsemblFungi; EAQ90343; EAQ90343; CHGG_02278.
DR GeneID; 4388592; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q2HBX6; -.
DR OMA; TQECKCV; -.
DR OrthoDB; 995692at2759; -.
DR Proteomes; UP000001056; 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..454
FT /note="Nuclear distribution protein PAC1-1"
FT /id="PRO_0000405076"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 104..145
FT /note="WD 1"
FT REPEAT 147..187
FT /note="WD 2"
FT REPEAT 191..236
FT /note="WD 3"
FT REPEAT 239..278
FT /note="WD 4"
FT REPEAT 283..342
FT /note="WD 5"
FT REPEAT 344..383
FT /note="WD 6"
FT REPEAT 388..450
FT /note="WD 7"
FT REGION 71..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 454 AA; 49338 MW; 937ADAED133B8D84 CRC64;
MAQLLTSRQA EELHRALIAY LSSNNLTSTA AALRAEIGLG EDVFDATTAK KYEGLLEKKW
TSVVRLQKKV RHTSQLSNAT PTSRQNKDPV NWLPKSPARH TLQSHRQPIT CVAFHPVFSS
LASGSEDQTI KIWDWELGEL ERTIKGHTKT VLDVDFGGPR GNTLLASCSS DLTIKLWDPS
DDYKNIRTLP GHDHSVSAVR FIPSGVAGGA GNLLVSASRD KTLRIWDVST GYCVKTLRGH
AEWVRDVCPS VDGRFILSTS DDYTSRLWDV SIANPEPKTT LIGHEHVVLC CAIAPSASYP
HLAAIAGVKK PPTTSAVEFM ATGSRDKTIR LWDARGTCIK ILVGHDNWVR GLVFHPGGKY
LLSASDDYTL RCWDLTQEGR CVKTISDAHA HFVQCIRWAP SVVKDVSVAN GGDGQGGEAN
GTPRQAAGAG AAEAQIRCVL ATGSVDLNVR IFAN
