DCN1_YARLI
ID DCN1_YARLI Reviewed; 240 AA.
AC Q6C0B6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Defective in cullin neddylation protein 1;
GN Name=DCN1; OrderedLocusNames=YALI0F26147g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: May contribute to neddylation of cullin components of SCF-
CC type E3 ubiquitin ligase complexes. Neddylation of cullins play an
CC essential role in the regulation of SCF-type complexes activity (By
CC similarity). {ECO:0000250}.
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DR EMBL; CR382132; CAG78708.1; -; Genomic_DNA.
DR RefSeq; XP_505896.1; XM_505896.1.
DR AlphaFoldDB; Q6C0B6; -.
DR SMR; Q6C0B6; -.
DR STRING; 4952.CAG78708; -.
DR EnsemblFungi; CAG78708; CAG78708; YALI0_F26147g.
DR GeneID; 2908110; -.
DR KEGG; yli:YALI0F26147g; -.
DR VEuPathDB; FungiDB:YALI0_F26147g; -.
DR HOGENOM; CLU_047042_0_1_1; -.
DR InParanoid; Q6C0B6; -.
DR OMA; FTQTGEQ; -.
DR Proteomes; UP000001300; Chromosome F.
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:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0032182; F:ubiquitin-like protein binding; IBA:GO_Central.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IBA:GO_Central.
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 Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..240
FT /note="Defective in cullin neddylation protein 1"
FT /id="PRO_0000129517"
FT DOMAIN 7..44
FT /note="UBA-like"
FT DOMAIN 49..239
FT /note="DCUN1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00574"
SQ SEQUENCE 240 AA; 27579 MW; 11AEC198FF393B83 CRC64;
MVRSDWRAQE IRRVMTFTGS KEKTARDALE KFDWNVEVAI DHILNTPQVD LSGASKVFDK
YRNADSDEID LDGTIQYITD LGLSLEEPTV LAVAMTAGSP SVGTFTRKPF VEGWAAIGGD
TLPAQQKLCR SFAESMTSLN ADFQKIYKFT YGFLLQEGQR VLPQETAVDY WRLLLTGKYE
HLDKWLSFVT EKYKRNISRD AWNMLYEFML FQAKDPSLES YDEDGAWPSV IDEYVEFLKE
