ID LIS1_EMENI Reviewed; 444 AA.
AC Q00664; C8V209; Q5AZT3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Nuclear distribution protein nudF {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=Nuclear migration protein nudF;
GN Name=nudF {ECO:0000255|HAMAP-Rule:MF_03141};
GN Synonyms=lis1 {ECO:0000255|HAMAP-Rule:MF_03141}, pac1; ORFNames=AN6197;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7612965; DOI=10.1091/mbc.6.3.297;
RA Xiang X., Osmani A.H., Osmani S.A., Xin M., Morris N.R.;
RT "NudF, a nuclear migration gene in Aspergillus nidulans, is similar to the
RT human LIS-1 gene required for neuronal migration.";
RL Mol. Biol. Cell 6:297-310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP INTERACTION WITH NUDE.
RX PubMed=10931877; DOI=10.1083/jcb.150.3.681;
RA Efimov V.P., Morris N.R.;
RT "The LIS1-related NUDF protein of Aspergillus nidulans interacts with the
RT coiled-coil domain of the NUDE/RO11 protein.";
RL J. Cell Biol. 150:681-688(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11369237; DOI=10.1016/s0960-9822(01)00200-7;
RA Han G., Liu B., Zhang J., Zuo W., Morris N.R., Xiang X.;
RT "The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to
RT microtubule ends and affect microtubule dynamics.";
RL Curr. Biol. 11:719-724(2001).
RN [6]
RP SELF-ASSOCIATION, AND MUTAGENESIS OF ILE-62; LEU-65; ILE-69; LEU-72;
RP VAL-76; LEU-79 AND LEU-83.
RX PubMed=11134054; DOI=10.1074/jbc.m010233200;
RA Ahn C., Morris N.R.;
RT "Nudf, a fungal homolog of the human LIS1 protein, functions as a dimer in
RT vivo.";
RL J. Biol. Chem. 276:9903-9909(2001).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12631710; DOI=10.1091/mbc.e02-06-0359;
RA Efimov V.P.;
RT "Roles of NUDE and NUDF proteins of Aspergillus nidulans: insights from
RT intracellular localization and overexpression effects.";
RL Mol. Biol. Cell 14:871-888(2003).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15930134; DOI=10.1091/mbc.e04-12-1071;
RA Li S., Oakley C.E., Chen G., Han X., Oakley B.R., Xiang X.;
RT "Cytoplasmic dynein's mitotic spindle pole localization requires a
RT functional anaphase-promoting complex, gamma-tubulin, and NUDF/LIS1 in
RT Aspergillus nidulans.";
RL Mol. Biol. Cell 16:3591-3605(2005).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16467375; DOI=10.1091/mbc.e05-11-1084;
RA Efimov V.P., Zhang J., Xiang X.;
RT "CLIP-170 homologue and NUDE play overlapping roles in NUDF localization in
RT Aspergillus nidulans.";
RL Mol. Biol. Cell 17:2021-2034(2006).
RN [10]
RP FUNCTION, INTERACTION WITH BNFA AND NUDC, AND SUBCELLULAR LOCATION.
RX PubMed=18390647; DOI=10.1128/ec.00071-07;
RA Helmstaedt K., Laubinger K., Vosskuhl K., Bayram O., Busch S., Hoppert M.,
RA Valerius O., Seiler S., Braus G.H.;
RT "The nuclear migration protein NUDF/LIS1 forms a complex with NUDC and BNFA
RT at spindle pole bodies.";
RL Eukaryot. Cell 7:1041-1052(2008).
RN [11]
RP FUNCTION.
RX PubMed=20876661; DOI=10.1242/jcs.075259;
RA Zhang J., Zhuang L., Lee Y., Abenza J.F., Penalva M.A., Xiang X.;
RT "The microtubule plus-end localization of Aspergillus dynein is important
RT for dynein-early-endosome interaction but not for dynein ATPase
RT activation.";
RL J. Cell Sci. 123:3596-3604(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, ECO:0000269|PubMed:11369237,
CC ECO:0000269|PubMed:15930134, ECO:0000269|PubMed:16467375,
CC ECO:0000269|PubMed:18390647, ECO:0000269|PubMed:20876661}.
CC -!- SUBUNIT: Interacts with dynein (By similarity). Self-associates.
CC Interacts with bnfA, nudC and nudE. {ECO:0000250,
CC ECO:0000269|PubMed:10931877, ECO:0000269|PubMed:18390647}.
CC -!- INTERACTION:
CC Q00664; O74689: nudE; NbExp=3; IntAct=EBI-1009311, EBI-1009303;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC spindle pole. Note=Localizes to the plus ends of microtubules at the
CC hyphal tip, and this requires clipA and nudE. Localizes to the mitotic
CC spindle poles, specifically to the spindle pole bodies (SPBs).
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; U22009; AAA91301.1; -; Genomic_DNA.
DR EMBL; AACD01000105; EAA57983.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF69989.1; -; Genomic_DNA.
DR RefSeq; XP_663801.1; XM_658709.1.
DR AlphaFoldDB; Q00664; -.
DR SMR; Q00664; -.
DR BioGRID; 1951557; 1.
DR IntAct; Q00664; 1.
DR STRING; 227321.Q00664; -.
DR EnsemblFungi; CBF69989; CBF69989; ANIA_06197.
DR GeneID; 2870783; -.
DR KEGG; ani:AN6197.2; -.
DR VEuPathDB; FungiDB:AN6197; -.
DR eggNOG; KOG0295; Eukaryota.
DR HOGENOM; CLU_000288_57_15_1; -.
DR InParanoid; Q00664; -.
DR OMA; CIRWAPP; -.
DR OrthoDB; 1798470at2759; -.
DR Proteomes; UP000000560; Chromosome I.
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:0005816; C:spindle pole body; IDA:AspGD.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:AspGD.
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:0048315; P:conidium formation; IMP:AspGD.
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; IMP:AspGD.
DR GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.960.30; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR44129:SF1; PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB SUBUNIT BETA; 1.
DR PANTHER; PTHR44129; WD REPEAT-CONTAINING PROTEIN POP1; 1.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF109925; Lissencephaly-1 protein (Lis-1, PAF-AH alpha) N-terminal domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Reference proteome; Repeat; Transport; WD repeat.
FT CHAIN 1..444
FT /note="Nuclear distribution protein nudF"
FT /id="PRO_0000051108"
FT DOMAIN 9..41
FT /note="LisH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT REPEAT 112..153
FT /note="WD 1"
FT REPEAT 155..195
FT /note="WD 2"
FT REPEAT 199..239
FT /note="WD 3"
FT REPEAT 243..282
FT /note="WD 4"
FT REPEAT 285..345
FT /note="WD 5"
FT REPEAT 347..386
FT /note="WD 6"
FT REPEAT 391..437
FT /note="WD 7"
FT REGION 83..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..88
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03141"
FT COMPBIAS 91..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 62
FT /note="I->A: Impairs self-association; when associated with
FT A-65; A-69; A-72; A-76; A-79 and A-83."
FT /evidence="ECO:0000269|PubMed:11134054"
FT MUTAGEN 65
FT /note="L->A: Impairs self-association; when associated with
FT A-62; A-69; A-72; A-76; A-79 and A-83."
FT /evidence="ECO:0000269|PubMed:11134054"
FT MUTAGEN 69
FT /note="I->A: Impairs self-association; when associated with
FT A-62; A-65; A-72; A-76; A-79 and A-83."
FT /evidence="ECO:0000269|PubMed:11134054"
FT MUTAGEN 72
FT /note="L->A: Impairs self-association; when associated with
FT A-62; A-65; A-69; A-76; A-79 and A-83."
FT /evidence="ECO:0000269|PubMed:11134054"
FT MUTAGEN 72
FT /note="L->E: Impairs self-association."
FT /evidence="ECO:0000269|PubMed:11134054"
FT MUTAGEN 76
FT /note="V->A: Impairs self-association; when associated with
FT A-62; A-65; A-69; A-72; A-79 and A-83."
FT /evidence="ECO:0000269|PubMed:11134054"
FT MUTAGEN 79
FT /note="L->A: Impairs self-association; when associated with
FT A-62; A-65; A-69; A-72; A-76 and A-83."
FT /evidence="ECO:0000269|PubMed:11134054"
FT MUTAGEN 83
FT /note="L->A: Impairs self-association; when associated with
FT A-62; A-65; A-69; A-72; A-76 and A-79."
FT /evidence="ECO:0000269|PubMed:11134054"
SQ SEQUENCE 444 AA; 48841 MW; A722F3A88D4B491D CRC64;
MSQILTAPQA EALHKAMLAY LSVINAPQTA ETLREELHFD ESYNEATCKK FEGVLEKKWT
GIARLQRRIN DLEAEVRSLQ AELEASPSAA RAKNQDPTNW LPKPSSTHTL TSHRDAVTCV
AFHPVFTSLA SGSEDCTIKI WDWELGEIER TLKGHIRGVS GLDYGGQKGN TLLASCSSDL
TIKLWDPSKD YANIRTLSGH DHSVSSVRFL TSNDNHLISA SRDGTLRIWD VSTGFCVKVI
KSATESWIRD VSPSFDGKWL VSGGRDQAIT VWEVSSAEPK AALLGHENFI ECCVFAPPAS
YEHLATLAGL KKPPPATSSC EFVATGARDK TIKLWEARGR LIKTLHGHDN WVRGLVFHPG
GKYLFSVSDD KTIRCWDLSQ EGRLVKTISG AHEHFVSCIR WAPSPNTDNP DPAGEKAGKK
DAVKPSYRCV IATGCADNSV RVFS
//
