ID   CUL6_CAEEL              Reviewed;         729 AA.
AC   Q21346;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=Cullin-6;
GN   Name=cul-6; ORFNames=K08E7.7;
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   INTERACTION WITH SKR-3.
RX   PubMed=11864567; DOI=10.1016/s0960-9822(02)00682-6;
RA   Nayak S., Santiago F.E., Jin H., Lin D., Schedl T., Kipreos E.T.;
RT   "The Caenorhabditis elegans Skp1-related gene family: diverse functions in
RT   cell proliferation, morphogenesis, and meiosis.";
RL   Curr. Biol. 12:277-287(2002).
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.
CC   -!- SUBUNIT: Probably interacts with skr-3. {ECO:0000269|PubMed:11864567}.
CC   -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF-like
CC       complex. {ECO:0000250|UniProtKB:Q93034}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
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DR   EMBL; Z77666; CAB01230.1; -; Genomic_DNA.
DR   PIR; T23474; T23474.
DR   RefSeq; NP_502412.1; NM_070011.3.
DR   AlphaFoldDB; Q21346; -.
DR   SMR; Q21346; -.
DR   BioGRID; 43306; 2.
DR   STRING; 6239.K08E7.7a.1; -.
DR   EPD; Q21346; -.
DR   PaxDb; 6239-K08E7-7; -.
DR   PeptideAtlas; Q21346; -.
DR   EnsemblMetazoa; K08E7.7a.1; K08E7.7a.1; WBGene00000841.
DR   GeneID; 178214; -.
DR   KEGG; cel:CELE_K08E7.7; -.
DR   UCSC; K08E7.7; c. elegans.
DR   AGR; WB:WBGene00000841; -.
DR   WormBase; K08E7.7a; CE11928; WBGene00000841; cul-6.
DR   eggNOG; KOG2166; Eukaryota.
DR   GeneTree; ENSGT00940000154774; -.
DR   HOGENOM; CLU_004747_6_1_1; -.
DR   InParanoid; Q21346; -.
DR   OMA; GEMEFYE; -.
DR   OrthoDB; 5474206at2759; -.
DR   PhylomeDB; Q21346; -.
DR   PRO; PR:Q21346; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00000841; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
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:0051607; P:defense response to virus; IMP: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; 1.20.1310.10; Cullin Repeats; 4.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; CULLIN; 1.
DR   PANTHER; PTHR11932:SF169; CULLIN-1; 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; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF74788; Cullin repeat-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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..729
FT                   /note="Cullin-6"
FT                   /id="PRO_0000119785"
FT   CROSSLNK        673
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in NEDD8)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13616"
SQ   SEQUENCE   729 AA;  84686 MW;  3D400932DE78E2CF CRC64;
     MSIEAVWGTL QDGLNLLYRR EHMSKKYYMM LYDAVYNICT TTTLANSNNN SPEFASEFLY
     KQLENYIRTY VIAIRDRISA CSGDELLGKC TIEWDNFKFS TRICNCIFQY LNRNFVSKKV
     EDKNGEIVEI YKLALDIWKA EFFDNFKVKT IDAILELILL ERCGSTINST HISSVVECLT
     ELDIYKVSFE PQFLDATKLF YKQEVLNSKE TVIEYMITVE NRLFQEEYRS RRYLGPSTND
     LLIDSCESIL ISDRLKFLHS EFERLLEARK DEHLTRMYSL CRRVTHGLED LRVYLEKRIL
     KEGHETLQRL AKDSGLKTTP KEYITKLLEV HEIYFNLINK AFDRNALFMQ SLDKASKDFI
     EANAVTMLAP EKHRSTRSAD YLARYCDQLL KKNSKVQDET ALDKALTVLK YISEKDVFQL
     YYQNWFSERI INNSSASDDA EEKFITNLTA TEGLEYTRNL VKMVEDAKIS KDLTTEFKDI
     KTEKSIDFNV ILQTTGAWPS LDQIKIILPR ELSTILKEFD TFYNASHNGR RLNWAYSQCR
     GEVNSKAFEK KYVFIVTASQ LCTLYLFNEQ DSFTIEQISK AIEMTAKSTS AIVGSLNPVI
     DPVLVVDKGN EKDGYPPDAV VSLNTKYANK KVRVDLTTAI KKATADRETD AVQNTVESDR
     KYEIKACIVR IMKTRKSLTH TLLINEIISQ LKSRFTPNVQ MIKICIEILI EQLYIRRSEN
     EHNVYEYLA
//