CUL3_DICDI
ID CUL3_DICDI Reviewed; 769 AA.
AC Q54NZ5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cullin-3;
DE Short=CUL-3;
DE AltName: Full=Cullin-C;
GN Name=culC; Synonyms=cul3; ORFNames=DDB_G0284903;
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC signalosome (CSN) complex. {ECO:0000250|UniProtKB:Q17391}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; AAFI02000073; EAL64915.1; -; Genomic_DNA.
DR RefSeq; XP_639922.1; XM_634830.1.
DR AlphaFoldDB; Q54NZ5; -.
DR SMR; Q54NZ5; -.
DR STRING; 44689.DDB0266742; -.
DR PaxDb; Q54NZ5; -.
DR PRIDE; Q54NZ5; -.
DR EnsemblProtists; EAL64915; EAL64915; DDB_G0284903.
DR GeneID; 8624834; -.
DR KEGG; ddi:DDB_G0284903; -.
DR dictyBase; DDB_G0284903; culC.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_7_1_1; -.
DR InParanoid; Q54NZ5; -.
DR OMA; MFKDMTI; -.
DR PhylomeDB; Q54NZ5; -.
DR Reactome; R-DDI-4641258; Degradation of DVL.
DR Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DDI-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-DDI-9706019; RHOBTB3 ATPase cycle.
DR Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q54NZ5; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0031463; C:Cul3-RING 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; IEA:UniProtKB-SubCell.
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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; 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; Nucleus; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..769
FT /note="Cullin-3"
FT /id="PRO_0000330939"
FT REGION 614..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 713
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
SQ SEQUENCE 769 AA; 88886 MW; 44932C30FFA11EDE CRC64;
MMAKPNGKIQ FKNLQSHGVL ADPDFPKRTW KLLKTAMRQI HQQNASNLSF EELYRNGYNM
VLQKHGDLLY NNLKKMVDKH LKAVAKTVSE SIDEKFLLEL NSSWINHKTS MLMIRDILMY
MDRNYVKQNN LSSVFDLGLY LFRDNVAHCS TIKDRLLNTL LSMVQKEREG EVIDRILIKN
IVQMLIDLGV NSKNVYIEDF EKPLLLKTSS HYQAQSQTLI QTCSCPDYMK KVEICLKEEL
ERVSHYLDSS SEPKLKEVCE KQLISNHMRT LIDMENSGLI SMLKDDKIED LKRMYNLFSR
VSDGLNLMKD VISSYVKEIG RGIVMDEEKT KESGTYFQSL LDLKDKYDNL LQNALYNDKQ
FIHSIQQAFE YFINLNPKSP EYISLFIDEK LKKGLKGVSE EEVDIILDKI LMLFRLIQEK
DVFEKYYKQH LAKRLLLGRS ISDDAERNMI AKLKTECGYQ FTSKLEGMFT DMRLSQDTMS
GFKTYIQNLK KALPIDLNVH VLTTGFWPTQ NTANCNLPRE ILLCCEAFKS YYLSNHNGRL
LLWQTNMGTA EIKANFPSKS HELQVSSYQM VILLLFNDQS KLTFKEIADQ TGIPTIDLKR
NLLALTNPKN KILDRELPST TSSTTTTTTT ATSSSTSTSP SSSSSSISTP TPSKSIDESD
VFAFNTKFKS KLFRVKVMAV VQKETPVEEK ETRDKVDEDR KHQIEASIVR IMKARKTLEH
SNLVSEVIKQ LQSRFVPNPV IVKKRIESLI EREYLERSKQ DRKIYNYMA
