ID   DCN1_CAEBR              Reviewed;         367 AA.
AC   Q60YT5; A8XT09;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 3.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Defective in cullin neddylation protein 1;
GN   Name=dcn-1; ORFNames=CBG18096;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Required for neddylation of cullin components of SCF-type E3
CC       ubiquitin ligase complexes. Neddylation of cullins play an essential
CC       role in the regulation of SCF-type complexes activity. Does not act by
CC       preventing deneddylation, but rather facilitates neddylation, possibly
CC       by acting with rbx-1 to recruit the Nedd8-charged E2 enzyme to the
CC       cullin component of SCF-type complexes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the cullin cul-3. Interacts with ubiquitin via
CC       its UBA-like domain. Interacts with ned-8/nedd8 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; HE600963; CAP35612.3; -; Genomic_DNA.
DR   RefSeq; XP_002642144.1; XM_002642098.1.
DR   AlphaFoldDB; Q60YT5; -.
DR   SMR; Q60YT5; -.
DR   STRING; 6238.CBG18096; -.
DR   EnsemblMetazoa; CBG18096.1; CBG18096.1; WBGene00037582.
DR   GeneID; 8584139; -.
DR   KEGG; cbr:CBG_18096; -.
DR   CTD; 8584139; -.
DR   WormBase; CBG18096; CBP10752; WBGene00037582; Cbr-dcn-1.
DR   eggNOG; KOG3077; Eukaryota.
DR   HOGENOM; CLU_047042_0_1_1; -.
DR   InParanoid; Q60YT5; -.
DR   OMA; PIVAGNK; -.
DR   OrthoDB; 1418097at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblMetazoa.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR   GO; GO:0030953; P:astral microtubule organization; IEA:EnsemblMetazoa.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IEA:EnsemblMetazoa.
DR   GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0030163; P:protein catabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR   Gene3D; 1.10.238.200; -; 1.
DR   InterPro; IPR014764; DCN-prot.
DR   InterPro; IPR042460; DCN1-like_PONY.
DR   InterPro; IPR005176; PONY_dom.
DR   InterPro; IPR009060; UBA-like_sf.
DR   PANTHER; PTHR12281; PTHR12281; 1.
DR   Pfam; PF03556; Cullin_binding; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   PROSITE; PS51229; DCUN1; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..367
FT                   /note="Defective in cullin neddylation protein 1"
FT                   /id="PRO_0000129506"
FT   DOMAIN          83..120
FT                   /note="UBA-like"
FT   DOMAIN          134..345
FT                   /note="DCUN1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   367 AA;  42028 MW;  075ECA421DB4C3A2 CRC64;
     MNRLKADQKT KVGKRKQDPP ETLSEAEYDV KKCRAQNNAN LVGVSNMTSS QTVMPITHLS
     YASSSSQGLA QSSILSKNCP KNYENILRQF VQWTQATEPV SLNFLAKANW NIEYAMTLYY
     DNPNLFSSSA PATVDQSKTI QLFTQYVDKR DGLGERIGPH GMQRLLIDLG YEPIDRRVLI
     LAWVFKAETQ CEFSLQEFTN GMASLQVDSI QGLKQKIDAL DAGMKADLTK TRDLCIFTFN
     YGKSAASRSL DLEMAICYWD VIFGARKPLM SQWIDFLYGQ ERMAYARLEE ELGPTNAKKV
     KSVWITRDTW NLFWDFIVLG KEDLSDYDEE GAWPVLIDQF VDHCRENLNY PKPLRENSNA
     MEHQSYY