CUL3A_ARATH
ID CUL3A_ARATH Reviewed; 732 AA.
AC Q9ZVH4; Q0WL17; Q7Y1Y8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cullin-3A;
DE Short=AtCUL3a;
GN Name=CUL3A; Synonyms=CUL3; OrderedLocusNames=At1g26830; ORFNames=T2P11.2;
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 [MRNA].
RA Shen W.H., Genschik P.;
RT "Characterization of plant cullins.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH CSN2.
RX PubMed=12615944; DOI=10.1105/tpc.009092;
RA Serino G., Su H., Peng Z., Tsuge T., Wei N., Gu H., Deng X.-W.;
RT "Characterization of the last subunit of the Arabidopsis COP9 signalosome:
RT implications for the overall structure and origin of the complex.";
RL Plant Cell 15:719-731(2003).
RN [6]
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 [7]
RP FUNCTION, INTERACTION WITH RBX1A AND BTB PROTEINS, MUTAGENESIS OF
RP 48-SER-PHE-49, 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 [8]
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 [9]
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 [10]
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 [11]
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).
RN [12]
RP INTERACTION WITH SR1IP1.
RX PubMed=24528504; DOI=10.1111/tpj.12473;
RA Zhang L., Du L., Shen C., Yang Y., Poovaiah B.W.;
RT "Regulation of plant immunity through ubiquitin-mediated modulation of
RT Ca(2+) -calmodulin-AtSR1/CAMTA3 signaling.";
RL Plant J. 78:269-281(2014).
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 CUL3B. {ECO:0000269|PubMed:15659098,
CC ECO:0000269|PubMed:15772280, ECO:0000269|PubMed:16045478,
CC ECO:0000269|PubMed:19132085}.
CC -!- SUBUNIT: Interacts with CSN2 and RBX1A. Interacts with BTB/POZ domain-
CC containing proteins BPM1, BPM2, BPM3, BPM6, BT1, BT2, BT3, BT5,
CC AT1G01640, AT1G21780 and AT5G48510 (PubMed:12615944, PubMed:15618422,
CC PubMed:15659098, PubMed:15749712, PubMed:15772280). Interacts with
CC SR1IP1 (PubMed:24528504). {ECO:0000269|PubMed:12615944,
CC ECO:0000269|PubMed:15618422, ECO:0000269|PubMed:15659098,
CC ECO:0000269|PubMed:15749712, ECO:0000269|PubMed:15772280,
CC ECO:0000269|PubMed:24528504}.
CC -!- INTERACTION:
CC Q9ZVH4; Q9XHZ8: At1g21780; NbExp=4; IntAct=EBI-531362, EBI-541047;
CC Q9ZVH4; Q8L765: BPM1; NbExp=5; IntAct=EBI-531362, EBI-540891;
CC Q9ZVH4; O22286: BPM3; NbExp=3; IntAct=EBI-531362, EBI-540923;
CC Q9ZVH4; P93002: NPR1; NbExp=3; IntAct=EBI-531362, EBI-1392127;
CC Q9ZVH4; Q940X7: RBX1A; NbExp=4; IntAct=EBI-531362, EBI-532404;
CC -!- DEVELOPMENTAL STAGE: Expressed during flower development in floral
CC meristem, sepals, petals, developing carpels, growing integuments and
CC tetrads of megaspores. In mature ovules, expressed in the cells of the
CC embryo sac. Expressed in the sporogenous cells, tetrads of microspores
CC and mature pollen in stamens After fertilization, expressed in the
CC embryo and endosperm at the globular and heart stages. The
CC progressively decreases during ovule development and is not observed in
CC the developing seed coat. {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 under normal growth
CC condition. Reduced sensitivity of the inhibition of hypocotyl growth in
CC far-red light. Cul3a and cul3b double mutant is embryonic lethal
CC (PubMed:16045478). {ECO:0000269|PubMed:15659098,
CC ECO:0000269|PubMed:15772280, ECO:0000269|PubMed:16045478}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; AJ319540; CAC85344.1; -; mRNA.
DR EMBL; AJ344252; CAC87120.1; -; mRNA.
DR EMBL; AC005508; AAD14503.1; -; Genomic_DNA.
DR EMBL; AC006535; AAF87034.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30747.1; -; Genomic_DNA.
DR EMBL; AK230392; BAF02190.1; -; mRNA.
DR PIR; A86395; A86395.
DR RefSeq; NP_174005.1; NM_102447.5.
DR AlphaFoldDB; Q9ZVH4; -.
DR SMR; Q9ZVH4; -.
DR BioGRID; 24462; 26.
DR DIP; DIP-33568N; -.
DR IntAct; Q9ZVH4; 19.
DR STRING; 3702.AT1G26830.1; -.
DR iPTMnet; Q9ZVH4; -.
DR PaxDb; Q9ZVH4; -.
DR PRIDE; Q9ZVH4; -.
DR ProteomicsDB; 220374; -.
DR EnsemblPlants; AT1G26830.1; AT1G26830.1; AT1G26830.
DR GeneID; 839226; -.
DR Gramene; AT1G26830.1; AT1G26830.1; AT1G26830.
DR KEGG; ath:AT1G26830; -.
DR Araport; AT1G26830; -.
DR TAIR; locus:2200670; AT1G26830.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_7_1_1; -.
DR InParanoid; Q9ZVH4; -.
DR OMA; MFKDMTI; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q9ZVH4; -.
DR PRO; PR:Q9ZVH4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZVH4; baseline and differential.
DR Genevisible; Q9ZVH4; 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:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR.
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-3A"
FT /id="PRO_0000396849"
FT CROSSLNK 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT MUTAGEN 48..49
FT /note="SF->AA: Abolishes the interaction with AT1G21780
FT protein."
FT /evidence="ECO:0000269|PubMed:15772280"
FT CONFLICT 458
FT /note="T -> I (in Ref. 4; BAF02190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 85313 MW; 40F58A46BB5572ED CRC64;
MSNQKKRNFQ IEAFKHRVVV DPKYADKTWQ ILERAIHQIY NQDASGLSFE ELYRNAYNMV
LHKFGEKLYT GFIATMTSHL KEKSKLIEAA QGGSFLEELN KKWNEHNKAL EMIRDILMYM
DRTYIESTKK THVHPMGLNL WRDNVVHFTK IHTRLLNTLL DLVQKERIGE VIDRGLMRNV
IKMFMDLGES VYQEDFEKPF LDASSEFYKV ESQEFIESCD CGDYLKKSEK RLTEEIERVA
HYLDAKSEEK ITSVVEKEMI ANHMQRLVHM ENSGLVNMLL NDKYEDLGRM YNLFRRVTNG
LVTVRDVMTS HLREMGKQLV TDPEKSKDPV EFVQRLLDER DKYDKIINTA FGNDKTFQNA
LNSSFEYFIN LNARSPEFIS LFVDDKLRKG LKGITDVDVE VILDKVMMLF RYLQEKDVFE
KYYKQHLAKR LLSGKTVSDD AERSLIVKLK TECGYQFTSK LEGMFTDMKT SEDTMRGFYG
SHPELSEGPT LIVQVLTTGS WPTQPAVPCN LPAEVSVLCE KFRSYYLGTH TGRRLSWQTN
MGTADIKAIF GKGQKHELNV STFQMCVLML FNNSDRLSYK EIEQATEIPA ADLKRCLQSL
ACVKGKNVIK KEPMSKDIGE EDLFVVNDKF TSKFYKVKIG TVVAQKETEP EKQETRQRVE
EDRKPQIEAA IVRIMKSRKI LDHNNIIAEV TKQLQPRFLA NPTEIKKRIE SLIERDFLER
DSTDRKLYRY LA
