ID   CUL3B_ARATH             Reviewed;         732 AA.
AC   Q9C9L0; Q711G4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Cullin-3B;
DE            Short=AtCUL3b;
GN   Name=CUL3B; OrderedLocusNames=At1g69670; ORFNames=T6C23.13;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 132-732.
RA   Shen W.H., Genschik P.;
RT   "Characterization of plant cullins.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH BPM1.
RX   PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA   Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA   Vierstra R.D.;
RT   "Cullins 3a and 3b assemble with members of the broad
RT   complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT   ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL   J. Biol. Chem. 280:18810-18821(2005).
RN   [5]
RP   FUNCTION, INTERACTION WITH RBX1A, NEDDYLATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15772280; DOI=10.1105/tpc.105.031989;
RA   Figueroa P., Gusmaroli G., Serino G., Habashi J., Ma L., Shen Y., Feng S.,
RA   Bostick M., Callis J., Hellmann H., Deng X.W.;
RT   "Arabidopsis has two redundant Cullin3 proteins that are essential for
RT   embryo development and that interact with RBX1 and BTB proteins to form
RT   multisubunit E3 ubiquitin ligase complexes in vivo.";
RL   Plant Cell 17:1180-1195(2005).
RN   [6]
RP   FUNCTION, INTERACTION WITH RBX1A, AND DISRUPTION PHENOTYPE.
RX   PubMed=15659098; DOI=10.1111/j.1365-313x.2004.02302.x;
RA   Dieterle M., Thomann A., Renou J.P., Parmentier Y., Cognat V.,
RA   Lemonnier G., Muller R., Shen W.H., Kretsch T., Genschik P.;
RT   "Molecular and functional characterization of Arabidopsis Cullin 3A.";
RL   Plant J. 41:386-399(2005).
RN   [7]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=16045478; DOI=10.1111/j.1365-313x.2005.02467.x;
RA   Thomann A., Brukhin V., Dieterle M., Gheyeselinck J., Vantard M.,
RA   Grossniklaus U., Genschik P.;
RT   "Arabidopsis CUL3A and CUL3B genes are essential for normal
RT   embryogenesis.";
RL   Plant J. 43:437-448(2005).
RN   [8]
RP   CUL3-RBX1-BTB UBIQUITIN-PROTEIN LIGASE COMPLEX, AND INTERACTION WITH BPM3.
RX   PubMed=15618422; DOI=10.1104/pp.104.052654;
RA   Weber H., Bernhardt A., Dieterle M., Hano P., Mutlu A., Estelle M.,
RA   Genschik P., Hellmann H.;
RT   "Arabidopsis AtCUL3a and AtCUL3b form complexes with members of the
RT   BTB/POZ-MATH protein family.";
RL   Plant Physiol. 137:83-93(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=19132085; DOI=10.1371/journal.pgen.1000328;
RA   Thomann A., Lechner E., Hansen M., Dumbliauskas E., Parmentier Y.,
RA   Kieber J., Scheres B., Genschik P.;
RT   "Arabidopsis CULLIN3 genes regulate primary root growth and patterning by
RT   ethylene-dependent and -independent mechanisms.";
RL   PLoS Genet. 5:E1000328-E1000328(2009).
CC   -!- FUNCTION: Component of the cullin-RING ubiquitin ligases (CRL), or
CC       CUL3-RBX1-BTB protein E3 ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. The functional specificity of the CRL complex depends on the
CC       BTB domain-containing protein as the susbstrate recognition component.
CC       Involved in embryo pattern formation and endosperm development.
CC       Required for the normal division and organization of the root stem
CC       cells and columella root cap cells. Regulates primary root growth by an
CC       unknown pathway, but in an ethylene-dependent manner. Functions in
CC       distal root patterning, by an ethylene-independent mechanism.
CC       Functionally redundant with CUL3A. {ECO:0000269|PubMed:15659098,
CC       ECO:0000269|PubMed:15772280, ECO:0000269|PubMed:16045478,
CC       ECO:0000269|PubMed:19132085}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with BTB/POZ-MATH proteins BPM1 and BPM3.
CC       {ECO:0000269|PubMed:15618422, ECO:0000269|PubMed:15659098,
CC       ECO:0000269|PubMed:15749712, ECO:0000269|PubMed:15772280}.
CC   -!- INTERACTION:
CC       Q9C9L0; Q8L765: BPM1; NbExp=3; IntAct=EBI-541687, EBI-540891;
CC       Q9C9L0; Q940X7: RBX1A; NbExp=3; IntAct=EBI-541687, EBI-532404;
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing and mature reproductive
CC       organs and during embryogenesis. {ECO:0000269|PubMed:16045478}.
CC   -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC       signalosome (CSN) complex. {ECO:0000250|UniProtKB:Q17391}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Cul3a and cul3b double
CC       mutant is embryonic lethal (PubMed:16045478).
CC       {ECO:0000269|PubMed:15659098, ECO:0000269|PubMed:15772280,
CC       ECO:0000269|PubMed:16045478}.
CC   -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00330}.
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DR   EMBL; AC013289; AAG52544.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34961.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60547.1; -; Genomic_DNA.
DR   EMBL; AJ344541; CAC87839.1; -; mRNA.
DR   PIR; E96718; E96718.
DR   RefSeq; NP_001319357.1; NM_001334418.1.
DR   RefSeq; NP_177125.3; NM_105635.4.
DR   AlphaFoldDB; Q9C9L0; -.
DR   SMR; Q9C9L0; -.
DR   BioGRID; 28524; 7.
DR   IntAct; Q9C9L0; 7.
DR   STRING; 3702.AT1G69670.1; -.
DR   PaxDb; Q9C9L0; -.
DR   PRIDE; Q9C9L0; -.
DR   ProteomicsDB; 220506; -.
DR   EnsemblPlants; AT1G69670.1; AT1G69670.1; AT1G69670.
DR   EnsemblPlants; AT1G69670.2; AT1G69670.2; AT1G69670.
DR   GeneID; 843303; -.
DR   Gramene; AT1G69670.1; AT1G69670.1; AT1G69670.
DR   Gramene; AT1G69670.2; AT1G69670.2; AT1G69670.
DR   KEGG; ath:AT1G69670; -.
DR   Araport; AT1G69670; -.
DR   TAIR; locus:2205020; AT1G69670.
DR   eggNOG; KOG2166; Eukaryota.
DR   HOGENOM; CLU_004747_7_1_1; -.
DR   InParanoid; Q9C9L0; -.
DR   OMA; ARNMNIN; -.
DR   OrthoDB; 1040292at2759; -.
DR   PhylomeDB; Q9C9L0; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9C9L0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C9L0; baseline and differential.
DR   Genevisible; Q9C9L0; AT.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; 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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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   1: Evidence at protein level;
KW   Isopeptide bond; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN           1..732
FT                   /note="Cullin-3B"
FT                   /id="PRO_0000396850"
FT   CROSSLNK        676
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in NEDD8)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13616"
SQ   SEQUENCE   732 AA;  85610 MW;  83B667E9CE3C7C7D CRC64;
     MSNQKKRNFQ IEAFKQRVVV DPKYADKTWK ILEHAIHEIY NHNASGLSFE ELYRNAYNMV
     LHKYGDKLYT GLVTTMTFHL KEICKSIEEA QGGAFLELLN RKWNDHNKAL QMIRDILMYM
     DRTYVSTTKK THVHELGLHL WRDNVVYSSK IQTRLLNTLL DLVHKERTGE VIDRVLMRNV
     IKMFMDLGES VYQDDFEKPF LEASAEFYKV ESMEFIESCD CGEYLKKAEK PLVEEVERVV
     NYLDAKSEAK ITSVVEREMI ANHVQRLVHM ENSGLVNMLL NDKYEDMGRM YSLFRRVANG
     LVTVRDVMTL HLREMGKQLV TDPEKSKDPV EFVQRLLDER DKYDRIINMA FNNDKTFQNA
     LNSSFEYFVN LNTRSPEFIS LFVDDKLRKG LKGVGEEDVD LILDKVMMLF RYLQEKDVFE
     KYYKQHLAKR LLSGKTVSDD AERNLIVKLK TECGYQFTSK LEGMFTDMKT SHDTLLGFYN
     SHPELSEGPT LVVQVLTTGS WPTQPTIQCN LPAEVSVLCE KFRSYYLGTH TGRRLSWQTN
     MGTADIKAVF GKGQKHELNV STFQMCVLML FNNSDRLSYK EIEQATEIPT PDLKRCLQSM
     ACVKGKNVLR KEPMSKEIAE EDWFVVNDRF ASKFYKVKIG TVVAQKETEP EKQETRQRVE
     EDRKPQIEAA IVRIMKSRRV LDHNNIIAEV TKQLQTRFLA NPTEIKKRIE SLIERDFLER
     DNTDRKLYRY LA