CUL4_DICDI
ID CUL4_DICDI Reviewed; 802 AA.
AC Q54CS2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Cullin-4;
DE Short=CUL-4;
DE AltName: Full=Cullin-D;
GN Name=culD; Synonyms=cul4; ORFNames=DDB_G0292794;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Probable core component of cullin-based SCF-like E3
CC ubiquitin-protein ligase complexes which mediate the ubiquitination and
CC subsequent proteasomal degradation of target proteins. The E3
CC ubiquitin-protein ligase activity of the complex is dependent on the
CC neddylation of the cullin subunit (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC signalosome (CSN) complex. {ECO:0000250|UniProtKB:Q13620}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; AAFI02000196; EAL61071.1; -; Genomic_DNA.
DR RefSeq; XP_629469.1; XM_629467.1.
DR AlphaFoldDB; Q54CS2; -.
DR SMR; Q54CS2; -.
DR STRING; 44689.DDB0266743; -.
DR PaxDb; Q54CS2; -.
DR EnsemblProtists; EAL61071; EAL61071; DDB_G0292794.
DR GeneID; 8628859; -.
DR KEGG; ddi:DDB_G0292794; -.
DR dictyBase; DDB_G0292794; culD.
DR eggNOG; KOG2167; Eukaryota.
DR HOGENOM; CLU_004747_7_2_1; -.
DR InParanoid; Q54CS2; -.
DR OMA; WPTYPVM; -.
DR PhylomeDB; Q54CS2; -.
DR Reactome; R-DDI-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DDI-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DDI-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DDI-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q54CS2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR033044; CUL4B.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 2.
DR PANTHER; PTHR11932:SF66; PTHR11932:SF66; 2.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..802
FT /note="Cullin-4"
FT /id="PRO_0000345012"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 748
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 802 AA; 92291 MW; 7664D2ACA8152308 CRC64;
MNFNNNNNNN NNNNNNNNLN NNNNNVNNIN NNNKKPLTNS LAGTPPAKKI LVIKNLKQIP
KTPDNYEDSS WNKLSSAITS INMKQATTLT QEELYKMVEN LCFDKILASN LYNKISVQIE
KHITLTIKHL VLTMSSDPII FLKSINSIWK DHTNQMIMIR SIFLYLDRTY VIQNSNTVKS
IWDLGLFYFG NNLSQQSNLE RKTIDSLLYS IRCEREGDEI DRDLIHSLVK MLSSLNIYTK
FEIEFIKETN RFYDMEGNSK INEIETPMYL KYVCERLNQE GERLMRYLEQ STKKQLMAVL
DRQLIERHVD VILEKGFNAM VNGDRLEDLG KLYQLLNSVG EIKKIKESWQ SYIKQTGIQM
LNDKEKEATL IQDLLDYKDR LDRILSQSFS KNELLTYALK ESFEYFINTK QNKPAELVAR
FIDSKLKVGG KRMSEEELET VLNKSLILFR YIQGKDVFEA FYKQDLSKRL LLDKSTSIDA
EKSMISKLKT ECGTTFTAKL EEMFKDIELS NDIMNSFRDS PMTQNFKSIE MNIYVLTSGN
WPIQPPIEAT LPKEFLEYQE VFNKFYLSKH NGKTLKWQNA LSYCVLKANF IQGKKELSVS
LFQTIILYLF NDVIDGGELS FRDIQANTGL AIPELKKNLL SLCSSKSDIL IQKKSSTSSN
TSSNTSSNTS SSASGSASGG ASGGATKTKV IDETDTFLFN SKFSSKLFKI KVNSIQIQET
VEENQKTNEN IISDRQYQVD AAIVRIMKTR KTLAHNLLIS ELVSLLKFQP KPVDLKKRIE
ILIEKEYLCR DPENAMIYNY MA
