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Nuclear distribution protein nudF (Lissencephaly-1 homolog) (LIS-1) (Nuclear migration protein nudF)

 LIS1_EMENI              Reviewed;         444 AA.
Q00664; C8V209; Q5AZT3;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 117.
RecName: Full=Nuclear distribution protein nudF {ECO:0000255|HAMAP-Rule:MF_03141};
AltName: Full=Lissencephaly-1 homolog {ECO:0000255|HAMAP-Rule:MF_03141};
Short=LIS-1 {ECO:0000255|HAMAP-Rule:MF_03141};
AltName: Full=Nuclear migration protein nudF;
Name=nudF {ECO:0000255|HAMAP-Rule:MF_03141};
Synonyms=lis1 {ECO:0000255|HAMAP-Rule:MF_03141}, pac1;
ORFNames=AN6197;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7612965; DOI=10.1091/mbc.6.3.297;
Xiang X., Osmani A.H., Osmani S.A., Xin M., Morris N.R.;
"NudF, a nuclear migration gene in Aspergillus nidulans, is similar to
the human LIS-1 gene required for neuronal migration.";
Mol. Biol. Cell 6:297-310(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[3]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[4]
INTERACTION WITH NUDE.
PubMed=10931877; DOI=10.1083/jcb.150.3.681;
Efimov V.P., Morris N.R.;
"The LIS1-related NUDF protein of Aspergillus nidulans interacts with
the coiled-coil domain of the NUDE/RO11 protein.";
J. Cell Biol. 150:681-688(2000).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11369237; DOI=10.1016/S0960-9822(01)00200-7;
Han G., Liu B., Zhang J., Zuo W., Morris N.R., Xiang X.;
"The Aspergillus cytoplasmic dynein heavy chain and NUDF localize to
microtubule ends and affect microtubule dynamics.";
Curr. Biol. 11:719-724(2001).
[6]
SELF-ASSOCIATION, AND MUTAGENESIS OF ILE-62; LEU-65; ILE-69; LEU-72;
VAL-76; LEU-79 AND LEU-83.
PubMed=11134054; DOI=10.1074/jbc.M010233200;
Ahn C., Morris N.R.;
"Nudf, a fungal homolog of the human LIS1 protein, functions as a
dimer in vivo.";
J. Biol. Chem. 276:9903-9909(2001).
[7]
SUBCELLULAR LOCATION.
PubMed=12631710; DOI=10.1091/mbc.E02-06-0359;
Efimov V.P.;
"Roles of NUDE and NUDF proteins of Aspergillus nidulans: insights
from intracellular localization and overexpression effects.";
Mol. Biol. Cell 14:871-888(2003).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15930134; DOI=10.1091/mbc.E04-12-1071;
Li S., Oakley C.E., Chen G., Han X., Oakley B.R., Xiang X.;
"Cytoplasmic dynein's mitotic spindle pole localization requires a
functional anaphase-promoting complex, gamma-tubulin, and NUDF/LIS1 in
Aspergillus nidulans.";
Mol. Biol. Cell 16:3591-3605(2005).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16467375; DOI=10.1091/mbc.E05-11-1084;
Efimov V.P., Zhang J., Xiang X.;
"CLIP-170 homologue and NUDE play overlapping roles in NUDF
localization in Aspergillus nidulans.";
Mol. Biol. Cell 17:2021-2034(2006).
[10]
FUNCTION, INTERACTION WITH BNFA AND NUDC, AND SUBCELLULAR LOCATION.
PubMed=18390647; DOI=10.1128/EC.00071-07;
Helmstaedt K., Laubinger K., Vosskuhl K., Bayram O., Busch S.,
Hoppert M., Valerius O., Seiler S., Braus G.H.;
"The nuclear migration protein NUDF/LIS1 forms a complex with NUDC and
BNFA at spindle pole bodies.";
Eukaryot. Cell 7:1041-1052(2008).
[11]
FUNCTION.
PubMed=20876661; DOI=10.1242/jcs.075259;
Zhang J., Zhuang L., Lee Y., Abenza J.F., Penalva M.A., Xiang X.;
"The microtubule plus-end localization of Aspergillus dynein is
important for dynein-early-endosome interaction but not for dynein
ATPase activation.";
J. Cell Sci. 123:3596-3604(2010).
-!- FUNCTION: Positively regulates the activity of the minus-end
directed microtubule motor protein dynein. May enhance dynein-
mediated microtubule sliding by targeting dynein to the
microtubule plus end. Required for nuclear migration during
vegetative growth as well as development. Required for retrograde
early endosome (EE) transport from the hyphal tip. Required for
localization of dynein to the mitotic spindle poles. Recruits
additional proteins to the dynein complex at SPBs.
{ECO:0000255|HAMAP-Rule:MF_03141, ECO:0000269|PubMed:11369237,
ECO:0000269|PubMed:15930134, ECO:0000269|PubMed:16467375,
ECO:0000269|PubMed:18390647, ECO:0000269|PubMed:20876661}.
-!- SUBUNIT: Interacts with dynein (By similarity). Self-associates.
Interacts with bnfA, nudC and nudE. {ECO:0000250,
ECO:0000269|PubMed:10931877, ECO:0000269|PubMed:18390647}.
-!- INTERACTION:
O74689:nudE; NbExp=3; IntAct=EBI-1009311, EBI-1009303;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, spindle pole. Note=Localizes to the plus ends of
microtubules at the hyphal tip, and this requires clipA and nudE.
Localizes to the mitotic spindle poles, specifically to the
spindle pole bodies (SPBs).
-!- DOMAIN: Dimerization mediated by the LisH domain may be required
to activate dynein. {ECO:0000255|HAMAP-Rule:MF_03141}.
-!- SIMILARITY: Belongs to the WD repeat LIS1/nudF family.
{ECO:0000255|HAMAP-Rule:MF_03141}.
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EMBL; U22009; AAA91301.1; -; Genomic_DNA.
EMBL; AACD01000105; EAA57983.1; -; Genomic_DNA.
EMBL; BN001301; CBF69989.1; -; Genomic_DNA.
RefSeq; XP_663801.1; XM_658709.1.
ProteinModelPortal; Q00664; -.
BioGrid; 1951557; 1.
IntAct; Q00664; 1.
STRING; 162425.CADANIAP00006811; -.
EnsemblFungi; CADANIAT00006811; CADANIAP00006811; CADANIAG00006811.
EnsemblFungi; EAA57983; EAA57983; AN6197.2.
GeneID; 2870783; -.
KEGG; ani:AN6197.2; -.
HOGENOM; HOG000184015; -.
InParanoid; Q00664; -.
KO; K16794; -.
OMA; DAHGHFV; -.
OrthoDB; EOG092C10HM; -.
Proteomes; UP000000560; Chromosome I.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0005938; C:cell cortex; IBA:GO_Central.
GO; GO:0000776; C:kinetochore; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IBA:GO_Central.
GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0005816; C:spindle pole body; IDA:AspGD.
GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IDA:AspGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0048315; P:conidium formation; IMP:AspGD.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
GO; GO:0007097; P:nuclear migration; IMP:AspGD.
GO; GO:2000574; P:regulation of microtubule motor activity; IMP:AspGD.
GO; GO:0043935; P:sexual sporulation resulting in formation of a cellular spore; IMP:AspGD.
GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
HAMAP; MF_03141; lis1; 1.
InterPro; IPR017252; Dynein_regulator_LIS1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR037190; LIS1_N.
InterPro; IPR006594; LisH.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 7.
PIRSF; PIRSF037647; Dynein_regulator_Lis1; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF109925; SSF109925; 1.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50896; LISH; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Microtubule; Mitosis; Reference proteome; Repeat;
Transport; WD repeat.
CHAIN 1 444 Nuclear distribution protein nudF.
/FTId=PRO_0000051108.
DOMAIN 9 41 LisH. {ECO:0000255|HAMAP-Rule:MF_03141}.
REPEAT 112 153 WD 1.
REPEAT 155 195 WD 2.
REPEAT 199 239 WD 3.
REPEAT 243 282 WD 4.
REPEAT 285 345 WD 5.
REPEAT 347 386 WD 6.
REPEAT 391 437 WD 7.
COILED 60 88 {ECO:0000255|HAMAP-Rule:MF_03141}.
MUTAGEN 62 62 I->A: Impairs self-association; when
associated with A-65; A-69; A-72; A-76;
A-79 and A-83.
{ECO:0000269|PubMed:11134054}.
MUTAGEN 65 65 L->A: Impairs self-association; when
associated with A-62; A-69; A-72; A-76;
A-79 and A-83.
{ECO:0000269|PubMed:11134054}.
MUTAGEN 69 69 I->A: Impairs self-association; when
associated with A-62; A-65; A-72; A-76;
A-79 and A-83.
{ECO:0000269|PubMed:11134054}.
MUTAGEN 72 72 L->A: Impairs self-association; when
associated with A-62; A-65; A-69; A-76;
A-79 and A-83.
{ECO:0000269|PubMed:11134054}.
MUTAGEN 72 72 L->E: Impairs self-association.
{ECO:0000269|PubMed:11134054}.
MUTAGEN 76 76 V->A: Impairs self-association; when
associated with A-62; A-65; A-69; A-72;
A-79 and A-83.
{ECO:0000269|PubMed:11134054}.
MUTAGEN 79 79 L->A: Impairs self-association; when
associated with A-62; A-65; A-69; A-72;
A-76 and A-83.
{ECO:0000269|PubMed:11134054}.
MUTAGEN 83 83 L->A: Impairs self-association; when
associated with A-62; A-65; A-69; A-72;
A-76 and A-79.
{ECO:0000269|PubMed:11134054}.
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


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