NDE1_EMENI
ID NDE1_EMENI Reviewed; 586 AA.
AC O74689; C8V2D2; Q5B005;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Nuclear distribution protein nudE;
GN Name=nudE; ORFNames=AN6125;
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 [MRNA], AND INTERACTION WITH NUDF.
RC STRAIN=XX20;
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 [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 FUNCTION, AND 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 [5]
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).
CC -!- FUNCTION: Required for nuclear migration within hyphae during
CC vegetative growth. {ECO:0000269|PubMed:12631710,
CC ECO:0000269|PubMed:16467375}.
CC -!- SUBUNIT: Self-associates (By similarity). Interacts with nudF.
CC {ECO:0000250, ECO:0000269|PubMed:10931877}.
CC -!- INTERACTION:
CC O74689; Q00664: nudF; NbExp=3; IntAct=EBI-1009303, EBI-1009311;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12631710, ECO:0000269|PubMed:16467375}.
CC Note=Localizes to the plus ends of microtubules.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
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DR EMBL; AF085679; AAC35556.1; -; Genomic_DNA.
DR EMBL; AACD01000104; EAA58100.1; -; Genomic_DNA.
DR EMBL; BN001301; CBF70134.1; -; Genomic_DNA.
DR RefSeq; XP_663729.1; XM_658637.1.
DR AlphaFoldDB; O74689; -.
DR SMR; O74689; -.
DR BioGRID; 1951833; 1.
DR IntAct; O74689; 1.
DR STRING; 162425.CADANIAP00006887; -.
DR EnsemblFungi; CBF70134; CBF70134; ANIA_06125.
DR EnsemblFungi; EAA58100; EAA58100; AN6125.2.
DR GeneID; 2871059; -.
DR KEGG; ani:AN6125.2; -.
DR VEuPathDB; FungiDB:AN6125; -.
DR eggNOG; KOG1853; Eukaryota.
DR HOGENOM; CLU_034391_0_0_1; -.
DR InParanoid; O74689; -.
DR OMA; WKTKYKQ; -.
DR OrthoDB; 801243at2759; -.
DR Proteomes; UP000000560; Chromosome I.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007097; P:nuclear migration; IMP:AspGD.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome;
KW Transport.
FT CHAIN 1..586
FT /note="Nuclear distribution protein nudE"
FT /id="PRO_0000240224"
FT REGION 1..215
FT /note="Interaction with nudF"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..586
FT /note="Localization to microtubule plus ends"
FT REGION 297..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 17..197
FT /evidence="ECO:0000255"
FT COMPBIAS 219..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 586 AA; 64640 MW; 967BF91F066D1389 CRC64;
MPSADEPSST RTNGTSSRSD QLAYYKKQYE QLESELADFQ ASSRELEAEL EKEIEASEKR
ERQLKEKVDN LRYEVEEWKS KYKQSKSEAS TAQNALQKEI TSLRDANLTL QLKLRDTEVA
NDDYERQARH TTSSLEDMES KYNQALEREV LLDMEYKQGE QERESLRIEN QRLRDELNDL
KIETEIVQER LRNNNRRRRP APLGRSPSTP HTPEIFDRSP GESTVSSPLF STPPTKLSLT
LASATATPPS PPMSETSSSM RKSLTAASGF PLQKASASES FGTRSLYGNR PQRFQAHSRA
TSYAFSNGRS TPSATTTRPS LPKANNTTAN RPSGIPKSGS LHQIRGLIGK MQKLEERVQS
AKSKLPPPSE TASRASSRAG SMLDASPGAA TIAMRRDTRK RLSGSSFSSS VRDGDGAPSY
VTSSRPSYGT RTQGDSRPSS RTSFSSSLSH STHPSVTPSN RPESRQSRTK TPLGHYSTNP
TTESRRPRSS LSNPAGQSTP INGMTYIDED EDLAEQFNMR ATISSTRPTR LPSFSNPAFS
TPTGLKKRST SGMSGIPAPR TLRRGNTMGP PKTKPKPVAG DLGETF
