BPM2_ARATH
ID BPM2_ARATH Reviewed; 406 AA.
AC Q9M8J9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=BTB/POZ and MATH domain-containing protein 2;
DE AltName: Full=Protein BTB-POZ AND MATH DOMAIN 2;
DE Short=AtBPM2;
GN Name=BPM2; OrderedLocusNames=At3g06190; ORFNames=F28L1.13;
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=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].
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 GENE FAMILY.
RX PubMed=14693377; DOI=10.1016/j.gene.2003.09.022;
RA Huang C.-J., Chen C.-Y., Chen H.-H., Tsai S.-F., Choo K.-B.;
RT "TDPOZ, a family of bipartite animal and plant proteins that contain the
RT TRAF (TD) and POZ/BTB domains.";
RL Gene 324:117-127(2004).
RN [5]
RP INTERACTION WITH CUL3A.
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 GENE FAMILY, AND NOMENCLATURE.
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 [7]
RP INTERACTION WITH RAP2-4, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19843165; DOI=10.1111/j.1742-4658.2009.07373.x;
RA Weber H., Hellmann H.;
RT "Arabidopsis thaliana BTB/ POZ-MATH proteins interact with members of the
RT ERF/AP2 transcription factor family.";
RL FEBS J. 276:6624-6635(2009).
RN [8]
RP INTERACTION WITH MYB56.
RC STRAIN=cv. Columbia;
RX PubMed=25343985; DOI=10.1093/mp/ssu120;
RA Chen L., Bernhardt A., Lee J., Hellmann H.;
RT "Identification of Arabidopsis MYB56 as a novel substrate for CRL3BPM E3
RT ligases.";
RL Mol. Plant 0:0-0(2014).
CC -!- FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RAP2-4. Interacts with CUL3A. Binds to MYB56 at
CC the promoter of FLOWERING LOCUS T (FT) (PubMed:25343985).
CC {ECO:0000269|PubMed:15772280, ECO:0000269|PubMed:19843165,
CC ECO:0000269|PubMed:25343985}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9M8J9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19843165}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes.
CC -!- SIMILARITY: Belongs to the Tdpoz family. {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; AC018907; AAF30312.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74358.1; -; Genomic_DNA.
DR EMBL; AY045891; AAK76565.1; -; mRNA.
DR EMBL; AY091449; AAM14388.1; -; mRNA.
DR RefSeq; NP_566275.1; NM_111494.3. [Q9M8J9-1]
DR AlphaFoldDB; Q9M8J9; -.
DR SMR; Q9M8J9; -.
DR BioGRID; 5128; 4.
DR IntAct; Q9M8J9; 3.
DR MINT; Q9M8J9; -.
DR STRING; 3702.AT3G06190.1; -.
DR PaxDb; Q9M8J9; -.
DR PRIDE; Q9M8J9; -.
DR ProteomicsDB; 240378; -. [Q9M8J9-1]
DR EnsemblPlants; AT3G06190.1; AT3G06190.1; AT3G06190. [Q9M8J9-1]
DR GeneID; 819793; -.
DR Gramene; AT3G06190.1; AT3G06190.1; AT3G06190. [Q9M8J9-1]
DR KEGG; ath:AT3G06190; -.
DR Araport; AT3G06190; -.
DR TAIR; locus:2082445; AT3G06190.
DR eggNOG; KOG1987; Eukaryota.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q9M8J9; -.
DR OMA; CHEFKIS; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; Q9M8J9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M8J9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8J9; baseline and differential.
DR Genevisible; Q9M8J9; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0071472; P:cellular response to salt stress; IEP:TAIR.
DR GO; GO:0042631; P:cellular response to water deprivation; IEP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR CDD; cd14736; BACK_AtBPM-like; 1.
DR CDD; cd00121; MATH; 1.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR045005; BPM1-6.
DR InterPro; IPR034090; BPM_C.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR008974; TRAF-like.
DR PANTHER; PTHR26379; PTHR26379; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00061; MATH; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50144; MATH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..406
FT /note="BTB/POZ and MATH domain-containing protein 2"
FT /id="PRO_0000405266"
FT DOMAIN 32..166
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 202..269
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 45159 MW; D33F6BEB990262EC CRC64;
MDTIRVSKEV PGSSKSTAQS LTESTSRTET INGSHEFKIS GYSLVKGMGI GKYVASDTFM
VGGYSWAIYF YPDGKSPEDN SVYVSLFIAL ASEGADVRAL FELTLVDQSG NERHKVHSHF
GRTLESGPYT LKYRGSMWGY KRFFKRSLLE SSDYLKDNGL LVRCCVGVVK SRTEGPRCYN
IPVPVSGLGQ QFGKLLESGK GADVTFEVDG ETFPAHKLVL AARSAVFRAQ LFGPLRSENT
NCIIIEDVQA PIFKMLLHFI YWDEMPDMQD LIGTDLKWAS TLVAQHLLAA ADRYALERLR
TICESKLCEG ISINTVATTL ALAEQHHCFQ LKAACLKFIA LPENLKAVME TDGFDYLKES
CPSLLSELLE YVARLSEHSL TSSGHRKELF ADGCDLNGRR VKQRLH
