NEDD8_CAEEL
ID NEDD8_CAEEL Reviewed; 77 AA.
AC Q93725;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=NEDD8;
DE AltName: Full=Neddylin;
DE AltName: Full=Protein NED-8;
DE AltName: Full=Ubiquitin-like protein Nedd8;
DE Flags: Precursor;
GN Name=ned-8; ORFNames=F45H11.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DEVELOPMENTAL STAGE, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10993680; DOI=10.1006/dbio.2000.9847;
RA Jones D., Candido E.P.M.;
RT "The NED-8 conjugating system in Caenorhabditis elegans is required for
RT embryogenesis and terminal differentiation of the hypodermis.";
RL Dev. Biol. 226:152-165(2000).
RN [3]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11847342; DOI=10.1126/science.1067765;
RA Kurz T., Pintard L., Willis J.H., Hamill D.R., Goenczy P., Peter M.,
RA Bowerman B.;
RT "Cytoskeletal regulation by the Nedd8 ubiquitin-like protein modification
RT pathway.";
RL Science 295:1294-1298(2002).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12781129; DOI=10.1016/s0960-9822(03)00336-1;
RA Pintard L., Kurz T., Glaser S., Willis J.H., Peter M., Bowerman B.;
RT "Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin
RT for degradation at the meiosis-to-mitosis transition in C. elegans.";
RL Curr. Biol. 13:911-921(2003).
RN [5]
RP INTERACTION WITH DCN-1.
RX PubMed=15988528; DOI=10.1038/nature03662;
RA Kurz T., Oezlue N., Rudolf F., O'Rourke S.M., Luke B., Hofmann K.,
RA Hyman A.A., Bowerman B., Peter M.;
RT "The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C.
RT elegans and S. cerevisiae.";
RL Nature 435:1257-1261(2005).
RN [6]
RP INTERACTION WITH ATX-3.
RX PubMed=17935801; DOI=10.1016/j.bbamcr.2007.07.012;
RA Ferro A., Carvalho A.L., Teixeira-Castro A., Almeida C., Tome R.J.,
RA Cortes L., Rodrigues A.J., Logarinho E., Sequeiros J., Macedo-Ribeiro S.,
RA Maciel P.;
RT "NEDD8: a new ataxin-3 interactor.";
RL Biochim. Biophys. Acta 1773:1619-1627(2007).
CC -!- FUNCTION: Ubiquitin-like protein which plays an important role in cell
CC cycle control and embryogenesis. Covalent attachment to its substrates
CC requires prior activation by the E1 complex uba-3-ula-1 and linkage to
CC the E2 enzyme ubc-12. Attachment of ned-8 to cullins activates their
CC associated E3 ubiquitin ligase activity, and thus promotes
CC polyubiquitination and proteasomal degradation of cyclins and other
CC regulatory proteins. {ECO:0000269|PubMed:10993680,
CC ECO:0000269|PubMed:11847342, ECO:0000269|PubMed:12781129}.
CC -!- SUBUNIT: Interacts with dcn-1 (PubMed:15988528). Covalently attached to
CC cullins (PubMed:12781129). May interact with atx-3 (PubMed:17935801).
CC {ECO:0000269|PubMed:12781129, ECO:0000269|PubMed:15988528,
CC ECO:0000269|PubMed:17935801}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11847342}. Cytoplasm
CC {ECO:0000269|PubMed:11847342}. Note=Mainly nuclear during interphase,
CC also cytoplasmic during interphase and mitosis.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:10993680}.
CC -!- PTM: Cleavage of precursor form is necessary for function.
CC {ECO:0000250|UniProtKB:Q15843}.
CC -!- DISRUPTION PHENOTYPE: Worms either arrest during embryonic development,
CC or show vulval eversion at the L4 stage and burst at the vulva during
CC the L4-to-adult molt. Those who survive to the adult stage display
CC severe defects in terminal differentiation of seam cells, vulva and
CC male tail. {ECO:0000269|PubMed:10993680}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; Z78420; CAB01708.1; -; Genomic_DNA.
DR PIR; T22249; T22249.
DR RefSeq; NP_492717.1; NM_060316.3.
DR AlphaFoldDB; Q93725; -.
DR SMR; Q93725; -.
DR BioGRID; 38327; 52.
DR IntAct; Q93725; 1.
DR STRING; 6239.F45H11.2; -.
DR EPD; Q93725; -.
DR PaxDb; Q93725; -.
DR PeptideAtlas; Q93725; -.
DR EnsemblMetazoa; F45H11.2.1; F45H11.2.1; WBGene00003587.
DR GeneID; 172910; -.
DR UCSC; F45H11.2; c. elegans.
DR CTD; 172910; -.
DR WormBase; F45H11.2; CE10552; WBGene00003587; ned-8.
DR eggNOG; KOG0005; Eukaryota.
DR GeneTree; ENSGT00940000155856; -.
DR HOGENOM; CLU_010412_6_4_1; -.
DR InParanoid; Q93725; -.
DR OMA; YAGKQMA; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; Q93725; -.
DR Reactome; R-CEL-5689603; UCH proteinases.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-917937; Iron uptake and transport.
DR PRO; PR:Q93725; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003587; Expressed in embryo and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:WormBase.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR GO; GO:0030162; P:regulation of proteolysis; IBA:GO_Central.
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 Cytoplasm; Developmental protein; Isopeptide bond; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="NEDD8"
FT /id="PRO_0000042777"
FT PROPEP 77
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT /id="PRO_0000042778"
FT REGION 70..72
FT /note="Interaction with uba-3"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT SITE 8
FT /note="Interaction with uba-3"
FT /evidence="ECO:0000250|UniProtKB:Q15843"
FT SITE 44
FT /note="Interaction with uba-3"
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 77 AA; 8629 MW; F3387DE33C671C78 CRC64;
MLIKVKTLTG KEIELDIEPN DRVERIKEKV EEKEGIPPPQ QRLIFAGKQM NDDKTAADYK
VLGGSVLHLV LALRGGF
