CUL5_DICDI
ID CUL5_DICDI Reviewed; 750 AA.
AC Q54XF7;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Cullin-5;
DE Short=CUL-5;
DE AltName: Full=Cullin-E;
GN Name=culE; Synonyms=cul5; ORFNames=DDB_G0278991;
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; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000026; EAL67917.1; -; Genomic_DNA.
DR RefSeq; XP_641893.1; XM_636801.1.
DR AlphaFoldDB; Q54XF7; -.
DR SMR; Q54XF7; -.
DR STRING; 44689.DDB0266744; -.
DR PaxDb; Q54XF7; -.
DR PRIDE; Q54XF7; -.
DR EnsemblProtists; EAL67917; EAL67917; DDB_G0278991.
DR GeneID; 8621819; -.
DR KEGG; ddi:DDB_G0278991; -.
DR dictyBase; DDB_G0278991; culE.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_6_1_1; -.
DR InParanoid; Q54XF7; -.
DR OMA; DNVVQSC; -.
DR PhylomeDB; Q54XF7; -.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q54XF7; -.
DR Proteomes; UP000002195; Chromosome 3.
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:0043223; C:cytoplasmic SCF ubiquitin ligase complex; 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; IPR045093; Cullin.
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; PS50069; CULLIN_2; 1.
PE 3: Inferred from homology;
KW Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..750
FT /note="Cullin-5"
FT /id="PRO_0000345013"
FT CROSSLNK 691
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 750 AA; 87131 MW; DDC9C0B83C0E6438 CRC64;
MSDQITVDEL WAECEQTFED LFLNLKKGLS RKRYMEIYTK IYNYCSSANE KALIDFYIPK
VKVLVAQKAV EIMSRSESYP NDALLLFFRN QWNEWKMSSN VLKNLLSPVN KIHSSDKKTT
SSSANQNESV VYSDTLNSWR ETAFNPLKNK LSVSLLQIIK NDRTGFSTNL QVLSDSLECY
VQLGPEKNKL EIYQSCFEQQ FLQETETFYK AESADFIEKN GVCEYMRHVY NRIEQETNRV
NQYMPISTLE KLTKILNNVL ISNYKEQFAS KFLDILIEDK SSDLVMMYSL LSRVNHLTPL
KNIFSDFIKS EGLKEIESNL KEAQEKPQVL ISILLKIYSR FNIMIKECYG NDTDFTTAMD
KSFSILVNEN PASYDPKKKE SNIPVVLSKF CDQILRKGPH HISDEAELEK KLTEAVCLFK
YLPDKDIFML NYQKMLSKRL VEDLSASEDA ETLMINKLKN YQGFDYCTKL TRMITDMRLC
KDININFQNH LNEKSLTLPY QFNFYVLTNG SWTLTNKQTA TPFKPPSEML SSITYFESFY
KKSYQGRVLT FLYDFSRADV DSRQAKGKIY KLTTTAYQMA ILLMFNGADK ITRFLINDTI
GLDETSIRLP LLALIKTGII ECSEPSFKNW NNDTEFTVNS KFSSKKMKVS CNIAVQIGET
KQSEGQQTVS EQEIEKERFF KLQAAIVRIM KSKKTMTHND LTVETTTQVS KWFTPKITAI
KKAIEYLIDQ EYIRRTTDDN PSARKYEYMA
