NEDD8_DROME
ID NEDD8_DROME Reviewed; 84 AA.
AC Q9VJ33; Q29QE5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=NEDD8;
DE AltName: Full=Neddylin;
DE AltName: Full=Ubiquitin-like protein Nedd8;
DE Flags: Precursor;
GN Name=Nedd8; ORFNames=CG10679;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=12231629; DOI=10.1101/gad.1011402;
RA Ou C.-Y., Lin Y.-F., Chen Y.-J., Chien C.-T.;
RT "Distinct protein degradation mechanisms mediated by Cul1 and Cul3
RT controlling Ci stability in Drosophila eye development.";
RL Genes Dev. 16:2403-2414(2002).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15843622; DOI=10.1523/jneurosci.0149-05.2005;
RA Zhu S., Perez R., Pan M., Lee T.;
RT "Requirement of Cul3 for axonal arborization and dendritic elaboration in
RT Drosophila mushroom body neurons.";
RL J. Neurosci. 25:4189-4197(2005).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16127432; DOI=10.1038/ncb1301;
RA Wu J.-T., Lin H.-C., Hu Y.-C., Chien C.-T.;
RT "Neddylation and deneddylation regulate Cul1 and Cul3 protein
RT accumulation.";
RL Nat. Cell Biol. 7:1014-1020(2005).
CC -!- FUNCTION: Ubiquitin-like protein which plays an important role in cell
CC cycle control, embryogenesis and neurogenesis. Covalent attachment to
CC its substrates requires prior activation by the E1 complex Uba3-Ula1
CC and linkage to the E2 enzyme UbcE2M. Attachment of Nedd8 to cullins
CC activates their associated E3 ubiquitin ligase activity, and thus
CC promotes polyubiquitination and proteasomal degradation of cyclins and
CC other regulatory proteins. {ECO:0000269|PubMed:12231629,
CC ECO:0000269|PubMed:15843622, ECO:0000269|PubMed:16127432}.
CC -!- SUBUNIT: Covalently attached to cullins. {ECO:0000269|PubMed:12231629,
CC ECO:0000269|PubMed:15843622, ECO:0000269|PubMed:16127432}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15843}.
CC -!- PTM: Cleavage of precursor form is necessary for function.
CC {ECO:0000250|UniProtKB:Q15843}.
CC -!- DISRUPTION PHENOTYPE: Flies die from growth arrest in the first-instar
CC larval stage. {ECO:0000269|PubMed:12231629}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; AE014134; AAF53724.1; -; Genomic_DNA.
DR EMBL; BT024445; ABC86507.1; -; mRNA.
DR RefSeq; NP_001286070.1; NM_001299141.1.
DR RefSeq; NP_609919.1; NM_136075.3.
DR AlphaFoldDB; Q9VJ33; -.
DR SMR; Q9VJ33; -.
DR BioGRID; 61142; 9.
DR IntAct; Q9VJ33; 8.
DR STRING; 7227.FBpp0080733; -.
DR PaxDb; Q9VJ33; -.
DR PRIDE; Q9VJ33; -.
DR DNASU; 35151; -.
DR EnsemblMetazoa; FBtr0081192; FBpp0080733; FBgn0032725.
DR EnsemblMetazoa; FBtr0342928; FBpp0309711; FBgn0032725.
DR GeneID; 35151; -.
DR KEGG; dme:Dmel_CG10679; -.
DR CTD; 4738; -.
DR FlyBase; FBgn0032725; Nedd8.
DR VEuPathDB; VectorBase:FBgn0032725; -.
DR eggNOG; KOG0005; Eukaryota.
DR HOGENOM; CLU_010412_6_4_1; -.
DR InParanoid; Q9VJ33; -.
DR OMA; YAGKQMA; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; Q9VJ33; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8951664; Neddylation.
DR Reactome; R-DME-917937; Iron uptake and transport.
DR SignaLink; Q9VJ33; -.
DR BioGRID-ORCS; 35151; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35151; -.
DR PRO; PR:Q9VJ33; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032725; Expressed in secondary oocyte and 26 other tissues.
DR ExpressionAtlas; Q9VJ33; baseline and differential.
DR Genevisible; Q9VJ33; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031386; F:protein tag; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0045116; P:protein neddylation; IMP:FlyBase.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0030162; P:regulation of proteolysis; IMP:UniProtKB.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IMP:FlyBase.
DR GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; IMP:UniProtKB.
DR GO; GO:0030431; P:sleep; IMP:FlyBase.
DR CDD; cd01806; Ubl_NEDD8; 1.
DR InterPro; IPR038738; Nedd8-like.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="NEDD8"
FT /id="PRO_0000042775"
FT PROPEP 77..84
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT /id="PRO_0000042776"
FT REGION 70..72
FT /note="Interaction with Uba3"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT SITE 8
FT /note="Interaction with Uba3"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT SITE 44
FT /note="Interaction with Uba3"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
SQ SEQUENCE 84 AA; 9346 MW; 2B0858BB4DC77AA3 CRC64;
MLIKVKTLTG KEIEIDIEPT DKVDRIKERV EEKEGIPPQQ QRLIFSGKQM NDDKTAADYK
VQGGSVLHLV LALRGGDSIL TPCV
