CUL5_CAEEL
ID CUL5_CAEEL Reviewed; 765 AA.
AC Q23639;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cullin-5;
DE Short=CUL-5;
GN Name=cul-5; ORFNames=ZK856.1;
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 FUNCTION, AND INTERACTION WITH RBX-1 AND RBX-2.
RX PubMed=17184777; DOI=10.1016/j.febslet.2006.12.009;
RA Sasagawa Y., Sato S., Ogura T., Higashitani A.;
RT "C. elegans RBX-2-CUL-5- and RBX-1-CUL-2-based complexes are redundant for
RT oogenesis and activation of the MAP kinase MPK-1.";
RL FEBS Lett. 581:145-150(2007).
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. In association
CC with rbx-2 seems to be involved in meiotic cell cycle progression in
CC the germline. Required for phosphorylation of the MAP kinase MPK-1 in
CC the germline. {ECO:0000269|PubMed:17184777}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with rbx-1 and rbx-2. {ECO:0000269|PubMed:17184777}.
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; Z70783; CAA94852.2; -; Genomic_DNA.
DR PIR; T28043; T28043.
DR RefSeq; NP_505616.2; NM_073215.4.
DR AlphaFoldDB; Q23639; -.
DR SMR; Q23639; -.
DR BioGRID; 44444; 4.
DR DIP; DIP-25847N; -.
DR IntAct; Q23639; 2.
DR MINT; Q23639; -.
DR STRING; 6239.ZK856.1; -.
DR iPTMnet; Q23639; -.
DR EPD; Q23639; -.
DR PaxDb; Q23639; -.
DR PeptideAtlas; Q23639; -.
DR PRIDE; Q23639; -.
DR EnsemblMetazoa; ZK856.1.1; ZK856.1.1; WBGene00000840.
DR GeneID; 179413; -.
DR KEGG; cel:CELE_ZK856.1; -.
DR UCSC; ZK856.1; c. elegans.
DR CTD; 179413; -.
DR WormBase; ZK856.1; CE41096; WBGene00000840; cul-5.
DR eggNOG; KOG2285; Eukaryota.
DR GeneTree; ENSGT00940000169483; -.
DR HOGENOM; CLU_004747_5_0_1; -.
DR InParanoid; Q23639; -.
DR OMA; YRENFEA; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q23639; -.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q23639; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000840; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
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: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..765
FT /note="Cullin-5"
FT /id="PRO_0000119784"
FT CROSSLNK 709
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 765 AA; 88908 MW; 2C264BB19B36D04D CRC64;
MQFDEEWSKA DPIVHALLHQ KSVTPAAWQD LFYHVYKITS WVDDGPLKIR DILTRCINDY
VHEANKRIRS LQTDGSLLIG YIKEWNRFYQ QANILPLPFK KIDESSRRRS VPETPEESIR
TVMLEKWNEI IFMNISEQLL VEALRLVKEE RDGNIIDAQN VIGIRESFVA LNDRAGEDPL
LVYRQSFERQ FIEQTTEYYK KICGNLLNEL GVLEYMVYAD KKLEEEQQRA KRYLEMNSPT
SGKHMEKAVI ALVESFEDTI LAECSKLIAS KDVERLQRLY RLIRRTRSGI DTVLKCIDTH
IRTEGLNDMR NNAENLSTDP ERYVQQLLLM FDKFSSLVRE GFCDDARLLT ARDKAFRAVV
NDSSIFKTEM MNKKGRTLSV ESKCAELLAN YCDLLLRKTQ LSKKLTSEEI DEKLNQVLLV
LKYVENKDVF MRFHRAHLSR RLILEMSADQ EKEEMMVTKL RECGMPSDAV NKLSRMLQDI
ELNKDMNSSF KKALTGTNNN KSIADSINMK VLNGGAWGRG GSERIRFSLP RELEDFVPEM
EAFYKKQHNG RKLCWMHHWS SGTMVFGTAN GGRFDLECTT FQMAVLFCFN DRAHDKISLE
TLRLATELPD AELNRTLLSL VAYPKMRYQI LLCDVPSTTV TARDFTDSTK FLINHDFNVV
KNGKSQQRGK VNLIGRLQLS LEANAEKEHE SIVALRELRV QEGIVKILKT RKTYTLAQLT
MELVEILKPL FIPNRKIIKE QIDWLIENKY MERRADDINT FVYIS
