CUL3_SCHPO
ID CUL3_SCHPO Reviewed; 785 AA.
AC Q09760; O74185;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Cullin-3;
DE Short=Cul-3;
GN Name=cul3; Synonyms=pcu3; ORFNames=SPAC24H6.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-543.
RA Kominami K., Toda T.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH BTB1; BTB2; BTB3; NEDD8 AND PIP1, AND
RP MUTAGENESIS OF TYR-50 AND LYS-729.
RX PubMed=14527422; DOI=10.1016/s1097-2765(03)00341-1;
RA Geyer R., Wee S., Anderson S., Yates J. III, Wolf D.A.;
RT "BTB/POZ domain proteins are putative substrate adaptors for cullin 3
RT ubiquitin ligases.";
RL Mol. Cell 12:783-790(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Probable core component of multiple cullin-RING-based BC3B
CC (BTB-CUL3-BTB) E3 ubiquitin-protein ligase complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. As a scaffold protein may contribute to catalysis through
CC positioning of the substrate and the ubiquitin-conjugating enzyme. The
CC functional specificity of the BC3B complex depends on the substrate
CC recognition component (By similarity). Involved in ubiquitin-mediated
CC degradation of btb3. {ECO:0000250, ECO:0000269|PubMed:14527422}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Probable component of multiple cullin-RING-based BC3B (BTB-
CC CUL3-BTB) E3 ubiquitin-protein ligase complexes formed by cul-3, rbx-1
CC and a variable BTB domain-containing protein as adapter and substrate
CC recognition component (By similarity). Interacts with btb1, btb2, btb3,
CC nedd8 and pip1. {ECO:0000250, ECO:0000269|PubMed:14527422}.
CC -!- INTERACTION:
CC Q09760; O74881: btb1; NbExp=3; IntAct=EBI-3647930, EBI-3647943;
CC Q09760; O74778: btb2; NbExp=2; IntAct=EBI-3647930, EBI-3648173;
CC Q09760; Q10225: btb3; NbExp=4; IntAct=EBI-3647930, EBI-3648208;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Neddylated; enhancing the ubiquitin-ligase activity.
CC {ECO:0000250|UniProtKB:P47050}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32519.1; Type=Frameshift; Evidence={ECO:0000305};
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; CU329670; CAA90847.1; -; Genomic_DNA.
DR EMBL; AB017028; BAA32519.1; ALT_FRAME; Genomic_DNA.
DR PIR; S62405; S62405.
DR PIR; T38359; T38359.
DR PIR; T43406; T43406.
DR RefSeq; NP_592949.1; NM_001018350.2.
DR AlphaFoldDB; Q09760; -.
DR SMR; Q09760; -.
DR BioGRID; 279091; 21.
DR IntAct; Q09760; 14.
DR STRING; 4896.SPAC24H6.03.1; -.
DR MaxQB; Q09760; -.
DR PaxDb; Q09760; -.
DR PRIDE; Q09760; -.
DR EnsemblFungi; SPAC24H6.03.1; SPAC24H6.03.1:pep; SPAC24H6.03.
DR GeneID; 2542637; -.
DR KEGG; spo:SPAC24H6.03; -.
DR PomBase; SPAC24H6.03; cul3.
DR VEuPathDB; FungiDB:SPAC24H6.03; -.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_7_1_1; -.
DR InParanoid; Q09760; -.
DR OMA; MFKDMTI; -.
DR PhylomeDB; Q09760; -.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q09760; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISO:PomBase.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; 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; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..785
FT /note="Cullin-3"
FT /id="PRO_0000119809"
FT CROSSLNK 729
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT MUTAGEN 50
FT /note="Y->G: Reduced btb3 binding and ubiquitination."
FT /evidence="ECO:0000269|PubMed:14527422"
FT MUTAGEN 729
FT /note="K->R: No cross-link with NEDD8."
FT /evidence="ECO:0000269|PubMed:14527422"
FT CONFLICT 476
FT /note="R -> RYALIVFTVFNTFR (in Ref. 2; BAA32519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 90512 MW; 0830F7A857DF6CE7 CRC64;
MQRSAKLKIR APRKFSANQV DFATHWEVLQ RAIGDIFQKS TSQLSFEELY RNAYILVLHK
YGEKLYNHVQ DVIRSRLKEE TVPAIYKNYD ASLLGNALLD IRKNDSYSTS WSRSLEAAHR
FLSSLVNSWK DHIVSMQMIS SVLKYLDKVY SKSADKVPVN ENGIYIFREV VLLNSFEIGE
KCVETILILV YLERKGNTIN RPLINDCLDM LNSLPSENKK ETLYDVLFAP KFLSYTRNFY
EIESSTVIGV FGVVEYLKKA EKRFEEEKER SKNYLFTKIA SPLLSVVEDE LLSKHLDDLL
ENQSTGFFSM IDSSNFEGLQ LVYESFSRVE LGVKSLKKYL AKYVAHHGKL INETTSQALE
GKMAVGRLSS NATMATLWVQ KVLALWDRLN TIISTTMDAD RSILNSLSDA FVTFVDGYTR
APEYISLFID DNLKKDARKA IEGSIEATLQ NSVTLFRFIS EKDVFEKYYK THLAKRLLNN
RSISSDAELG MISRLKQEAG NVFTQKLEGM FNDMNLSQEL LQEYKHNSAL QSAKPALDLN
VSILASTFWP IDLSPHKIKC NFPKVLLAQI DQFTDFYLSK HTGRKLLWYP SMGSADVRVN
FKDRKYDLNV STIASVILLL FQDLKENQCL IFEEILEKTN IEVGDLKRNL QSLACAKYKI
LLKDPKGREV NAGDKFYFNE NFVSNLARIK ISTVAQTRVE DDSERKRTLE KVDESRKHQA
DACIVRVMKD RKVCEHNQLM AEVTRQLNPR FHPSPMMIKR RIEALIEREY LQRQADNGRI
YEYLA
