CUL4_CAEEL
ID CUL4_CAEEL Reviewed; 840 AA.
AC Q17392; Q20428;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cullin-4;
DE Short=CUL-4;
GN Name=cul-4; ORFNames=F45E12.3;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 18-840.
RC STRAIN=Bristol N2;
RX PubMed=8681378; DOI=10.1016/s0092-8674(00)81267-2;
RA Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.;
RT "cul-1 is required for cell cycle exit in C. elegans and identifies a novel
RT gene family.";
RL Cell 85:829-839(1996).
RN [3]
RP FUNCTION.
RX PubMed=17509881; DOI=10.1016/j.cub.2007.04.055;
RA Kim J., Feng H., Kipreos E.T.;
RT "C. elegans CUL-4 prevents rereplication by promoting the nuclear export of
RT CDC-6 via a CKI-1-dependent pathway.";
RL Curr. Biol. 17:966-972(2007).
RN [4]
RP FUNCTION, AND INTERACTION WITH DDB-1.
RX PubMed=17145765; DOI=10.1128/mcb.00736-06;
RA Kim Y., Kipreos E.T.;
RT "The Caenorhabditis elegans replication licensing factor CDT-1 is targeted
RT for degradation by the CUL-4/DDB-1 complex.";
RL Mol. Cell. Biol. 27:1394-1406(2007).
CC -!- FUNCTION: Component of cullin-based E3 ubiquitin-protein ligase
CC complexes which mediate the ubiquitination and subsequent proteasomal
CC degradation of target proteins. The functional specificity of the E3
CC ubiquitin-protein ligase complex depends on the variable substrate
CC recognition component. In association with ddb-1 directs ubiquitination
CC of cdt-1 during S phase and is required for restraining DNA
CC rereplication. Probably is involved in ubiquitination of cki-1.
CC {ECO:0000269|PubMed:17145765, ECO:0000269|PubMed:17509881}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of an E3 ubiquitin-protein ligase complex including cul-4
CC and ddb-1.
CC -!- DEVELOPMENTAL STAGE: Highest levels in embryos and lower levels in
CC larvae and adults.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC47123.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FO080734; CCD66265.1; -; Genomic_DNA.
DR EMBL; U58086; AAC47123.1; ALT_INIT; mRNA.
DR PIR; T16367; T16367.
DR RefSeq; NP_495525.2; NM_063124.5.
DR AlphaFoldDB; Q17392; -.
DR SMR; Q17392; -.
DR BioGRID; 39534; 4.
DR IntAct; Q17392; 2.
DR STRING; 6239.F45E12.3; -.
DR EPD; Q17392; -.
DR PaxDb; Q17392; -.
DR PeptideAtlas; Q17392; -.
DR EnsemblMetazoa; F45E12.3.1; F45E12.3.1; WBGene00000839.
DR GeneID; 174198; -.
DR KEGG; cel:CELE_F45E12.3; -.
DR UCSC; F45E12.3; c. elegans.
DR CTD; 174198; -.
DR WormBase; F45E12.3; CE36545; WBGene00000839; cul-4.
DR eggNOG; KOG2167; Eukaryota.
DR GeneTree; ENSGT00990000209871; -.
DR HOGENOM; CLU_004747_7_2_1; -.
DR InParanoid; Q17392; -.
DR OMA; VITPEYW; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q17392; -.
DR Reactome; R-CEL-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-CEL-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-CEL-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-CEL-5696400; Dual Incision in GG-NER.
DR Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-8951664; Neddylation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q17392; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00000839; Expressed in germ line (C elegans) and 5 other tissues.
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: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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:WormBase.
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; 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; 1.
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 1: Evidence at protein level;
KW Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..840
FT /note="Cullin-4"
FT /id="PRO_0000119783"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 786
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT CONFLICT 18..23
FT /note="QLRKSS -> AGIRHE (in Ref. 2; AAC47123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 840 AA; 96540 MW; E244DDF97BCE0AB6 CRC64;
MTSGAPPTIS TEKSRSKQLR KSSKRTASTV EGTEAKQMRG DTENRSDGEM DDVSTSSEIR
HGNGFIENFR SQTGNSSRTT ATNERIKKKL VIKNFKANAN QNDVAMGDTN IDSTDGSVGR
DWAVLSDNVF AILEDRKTVT TLEGLFSKVR SVCDKNQSKV LYDRLVAIVV QFAKSLKESL
NAVEQVPLAE DNCEQYLEKF GQIWQAYPVK INLIRNIFLH LDRIALGATD TEILPLWECF
MQIFQKTFFP NIFKEFKATK LFNALYMAMQ KIMQRYPVDS PLRSLVDMLQ TVHVSEEFAK
FLISQLREHY NNERIDKVPK MNCNDYMEYC EDQINRYSQL VKVNFDEPSA LKDVQATVTN
CLIQQAIPEI LTHDFDDLID SDNISDIGRM FNLCRQCVGG EDEVRTQFSK YLKKRGEKLI
ATCPDEDLVS ELLAFKKKVD FIMTGSFKSA NDPVKMRQCL SDAFESFVNK QVDRSAELIS
KHFHTLLHSS NKNVSDDTTL DQMVDEAIVL FRYLRGKDVF EAYYKRGLAK RLFLERSASV
DAEKMVLCKL KTECGSAFTY KLEGMFKDMD ASENYGRLFN QYLEHMNKEK ANFTARVITP
EYWPTYDTYE INIPKEMRDT LTDYQDFYRV QHGNRNVKWH HGLASAVISA SFRPGCKKEL
IATMYQTVIL LLFNKCETWT VAEIVEHTKI LEIEVVKNVL ALLGGRDKPK VLQRVEGGGS
EKKEGTVENL KNEKFVVNSK FTEKRCRVRI AQVNIKTAVE ETKEVKEEVN SDRQYKIDAA
VVRIMKARKQ LNHQTLMTEL LQQLRFPVST ADIKKRLESL IEREYISRDP EEASSYNYVA
