BB_ARATH
ID BB_ARATH Reviewed; 248 AA.
AC Q8L649; C0Z296;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=E3 ubiquitin-protein ligase BIG BROTHER;
DE EC=2.3.2.27 {ECO:0000269|PubMed:16461280, ECO:0000269|PubMed:18483219};
DE AltName: Full=Protein ENHANCER OF DA1-1;
DE AltName: Full=RING-type E3 ubiquitin transferase BIG BROTHER {ECO:0000305};
GN Name=BB; Synonyms=EOD1; OrderedLocusNames=At3g63530; ORFNames=TEL3S.1;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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-2009) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, RAPID TURN-OVER, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-197 AND CYS-200,
RP INTERACTION WITH UBC10, AND UBIQUITINATION.
RX PubMed=16461280; DOI=10.1016/j.cub.2005.12.026;
RA Disch S., Anastasiou E., Sharma V.K., Laux T., Fletcher J.C., Lenhard M.;
RT "The E3 ubiquitin ligase BIG BROTHER controls arabidopsis organ size in a
RT dosage-dependent manner.";
RL Curr. Biol. 16:272-279(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18483219; DOI=10.1101/gad.463608;
RA Li Y., Zheng L., Corke F., Smith C., Bevan M.W.;
RT "Control of final seed and organ size by the DA1 gene family in Arabidopsis
RT thaliana.";
RL Genes Dev. 22:1331-1336(2008).
RN [8]
RP FUNCTION, AND INTERACTION WITH DA1.
RX PubMed=28167503; DOI=10.1101/gad.292235.116;
RA Dong H., Dumenil J., Lu F.H., Na L., Vanhaeren H., Naumann C., Klecker M.,
RA Prior R., Smith C., McKenzie N., Saalbach G., Chen L., Xia T., Gonzalez N.,
RA Seguela M., Inze D., Dissmeyer N., Li Y., Bevan M.W.;
RT "Ubiquitylation activates a peptidase that promotes cleavage and
RT destabilization of its activating E3 ligases and diverse growth regulatory
RT proteins to limit cell proliferation in Arabidopsis.";
RL Genes Dev. 31:197-208(2017).
RN [9]
RP FUNCTION.
RX PubMed=28003326; DOI=10.1104/pp.16.01410;
RA Vanhaeren H., Nam Y.J., De Milde L., Chae E., Storme V., Weigel D.,
RA Gonzalez N., Inze D.;
RT "Forever young: the role of ubiquitin receptor DA1 and E3 ligase BIG
RT BROTHER in controlling leaf growth and development.";
RL Plant Physiol. 173:1269-1282(2017).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF PRO-235.
RX PubMed=28922745; DOI=10.1093/pcp/pcx091;
RA Cattaneo P., Hardtke C.S.;
RT "BIG BROTHER uncouples cell proliferation from elongation in the
RT Arabidopsis primary root.";
RL Plant Cell Physiol. 58:1519-1527(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that limits organ size, and
CC possibly seed size, in a dose-dependent manner. Negatively regulates
CC the duration of cell proliferation in leaves and petals independently
CC of the major phytohormones (e.g. auxin, cytokinin, gibberellin,
CC brassinosteroids, ethylene, abscisic acid, jasmonic acid), probably by
CC targeting growth stimulators for degradation (PubMed:16461280,
CC PubMed:18483219). Limits the proliferation of root meristematic cells
CC (PubMed:28922745). Polyubiquitinates DA1 (PubMed:28167503). Involved in
CC the promotion of leaf senescence, in addition to its function in
CC restricting plant growth (PubMed:28003326). Possesses E3 ubiquitin-
CC protein ligase activity in vitro (PubMed:16461280, PubMed:18483219,
CC PubMed:28167503). {ECO:0000269|PubMed:16461280,
CC ECO:0000269|PubMed:18483219, ECO:0000269|PubMed:28003326,
CC ECO:0000269|PubMed:28167503, ECO:0000269|PubMed:28922745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:16461280,
CC ECO:0000269|PubMed:18483219};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with the E2 ubiquitin conjugating enzyme UBC10 via
CC the RING domain (PubMed:16461280). Interacts with DA1
CC (PubMed:28167503). {ECO:0000269|PubMed:16461280,
CC ECO:0000269|PubMed:28167503}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L649-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L649-2; Sequence=VSP_039629, VSP_039630;
CC -!- TISSUE SPECIFICITY: Mostly expressed in inflorescence, and, to a lower
CC extent, in seedlings, roots, stems, leaves and siliques.
CC {ECO:0000269|PubMed:16461280}.
CC -!- DEVELOPMENTAL STAGE: Confined to proliferating cells. Mainly present in
CC proliferating tissues (e.g. root, shoot and floral meristems, and young
CC organs) and vasculature. During petal growth, gradually restricted to
CC the distal part of the petal. Expressed in developing embryos.
CC {ECO:0000269|PubMed:16461280}.
CC -!- INDUCTION: Rapid turn-over by proteasome-mediated degradation (at
CC protein level).
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:16461280}.
CC -!- DISRUPTION PHENOTYPE: Enlarged floral organs (e.g. petals and sepals)
CC and thick stems mainly due to altered numbers of normally sized cells.
CC Enhanced da1-1 phenotype leading to increased seed and organ size.
CC {ECO:0000269|PubMed:16461280, ECO:0000269|PubMed:18483219}.
CC -!- MISCELLANEOUS: Plants overexpressing BB exhibit early senescence.
CC {ECO:0000269|PubMed:28003326}.
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DR EMBL; AL732522; CAD32249.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80499.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80500.1; -; Genomic_DNA.
DR EMBL; BT010197; AAQ22666.1; -; mRNA.
DR EMBL; AK318710; BAH56825.1; -; mRNA.
DR EMBL; AK227673; BAE99660.1; -; mRNA.
DR RefSeq; NP_001030922.1; NM_001035845.2. [Q8L649-1]
DR RefSeq; NP_680148.1; NM_148885.3. [Q8L649-1]
DR AlphaFoldDB; Q8L649; -.
DR SMR; Q8L649; -.
DR STRING; 3702.AT3G63530.1; -.
DR PaxDb; Q8L649; -.
DR PRIDE; Q8L649; -.
DR EnsemblPlants; AT3G63530.1; AT3G63530.1; AT3G63530. [Q8L649-1]
DR EnsemblPlants; AT3G63530.2; AT3G63530.2; AT3G63530. [Q8L649-1]
DR GeneID; 825528; -.
DR Gramene; AT3G63530.1; AT3G63530.1; AT3G63530. [Q8L649-1]
DR Gramene; AT3G63530.2; AT3G63530.2; AT3G63530. [Q8L649-1]
DR KEGG; ath:AT3G63530; -.
DR Araport; AT3G63530; -.
DR TAIR; locus:504955576; AT3G63530.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_063973_0_1_1; -.
DR InParanoid; Q8L649; -.
DR OMA; YKFGSLF; -.
DR PhylomeDB; Q8L649; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8L649; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L649; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0048437; P:floral organ development; IMP:TAIR.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:TAIR.
DR GO; GO:0046621; P:negative regulation of organ growth; IMP:TAIR.
DR GO; GO:1900057; P:positive regulation of leaf senescence; IMP:TAIR.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR033276; BB.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46400; PTHR46400; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..248
FT /note="E3 ubiquitin-protein ligase BIG BROTHER"
FT /id="PRO_0000396943"
FT ZN_FING 197..238
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT VAR_SEQ 234..236
FT /note="CPV -> FVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039629"
FT VAR_SEQ 237..248
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_039630"
FT MUTAGEN 197
FT /note="C->S: Loss of ubiquitin ligase activity and enlarged
FT floral organs; when associated with S-200."
FT /evidence="ECO:0000269|PubMed:16461280"
FT MUTAGEN 200
FT /note="C->S: Loss of ubiquitin ligase activity and enlarged
FT floral organs; when associated with S-197."
FT /evidence="ECO:0000269|PubMed:16461280"
FT MUTAGEN 235
FT /note="P->L: Increased root meristem size due to a high
FT number of dividing meristematic cells."
FT /evidence="ECO:0000269|PubMed:28922745"
FT CONFLICT 62
FT /note="K -> Q (in Ref. 4; BAH56825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27983 MW; 8A5993FC14107F58 CRC64;
MNGDNRPVED AHYTETGFPY AATGSYMDFY GGAAQGPLNY DHAATMHPQD NLYWTMNTNA
YKFGFSGSDN ASFYGSYDMN DHLSRMSIGR TNWDYHPMVN VADDPENTVA RSVQIGDTDE
HSEAEECIAN EHDPDSPQVS WQDDIDPDTM TYEELVELGE AVGTESRGLS QELIETLPTK
KYKFGSIFSR KRAGERCVIC QLKYKIGERQ MNLPCKHVYH SECISKWLSI NKVCPVCNSE
VFGEPSIH
