BPM6_ARATH
ID BPM6_ARATH Reviewed; 415 AA.
AC A1L4W5; Q9M2B6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=BTB/POZ and MATH domain-containing protein 6;
DE AltName: Full=Protein BTB-POZ AND MATH DOMAIN 6;
DE Short=AtBPM6;
GN Name=BPM6; OrderedLocusNames=At3g43700; ORFNames=F23N14_80;
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;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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, NOMENCLATURE, SUBUNIT, AND TISSUE SPECIFICITY.
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: Heterodimer with BPM1. Interacts with RAP2-4. Interacts with
CC CUL3A. Binds to MYB56 at the promoter of FLOWERING LOCUS T (FT)
CC (PubMed:25343985). {ECO:0000269|PubMed:15618422,
CC ECO:0000269|PubMed:15772280, ECO:0000269|PubMed:19843165,
CC ECO:0000269|PubMed:25343985}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843165}. Cytoplasm
CC {ECO:0000269|PubMed:19843165}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15618422,
CC 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 -!- SEQUENCE CAUTION:
CC Sequence=CAB83071.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL138638; CAB83071.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE77819.1; -; Genomic_DNA.
DR EMBL; BT029752; ABM06022.1; -; mRNA.
DR PIR; T47406; T47406.
DR RefSeq; NP_189956.2; NM_114238.3.
DR AlphaFoldDB; A1L4W5; -.
DR SMR; A1L4W5; -.
DR BioGRID; 8798; 5.
DR IntAct; A1L4W5; 4.
DR MINT; A1L4W5; -.
DR STRING; 3702.AT3G43700.1; -.
DR PaxDb; A1L4W5; -.
DR PRIDE; A1L4W5; -.
DR ProteomicsDB; 240437; -.
DR EnsemblPlants; AT3G43700.1; AT3G43700.1; AT3G43700.
DR GeneID; 823478; -.
DR Gramene; AT3G43700.1; AT3G43700.1; AT3G43700.
DR KEGG; ath:AT3G43700; -.
DR Araport; AT3G43700; -.
DR TAIR; locus:2080188; AT3G43700.
DR eggNOG; KOG1987; Eukaryota.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; A1L4W5; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; A1L4W5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:A1L4W5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; A1L4W5; baseline and differential.
DR Genevisible; A1L4W5; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0071472; P:cellular response to salt stress; 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 Pfam; PF00917; MATH; 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 Cytoplasm; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..415
FT /note="BTB/POZ and MATH domain-containing protein 6"
FT /id="PRO_0000405270"
FT DOMAIN 35..169
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 205..271
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45748 MW; AF911274AC17794D CRC64;
MSKLMTRTSG SSSPNTIPDQ IESPTSSRSV TQTTNGSHQF VIQGYSLAKG IGVGKHIASD
NFSVGGYQWT IFVYPDGKNP EDNSSYVSVF IVLASECTEV RALFELSLVD QSGKGKHKVH
SHFNRSLDGG PYTLKYRGSM WGYKRFFRRS LLETSDYLKD DCLKINCTVG VVVSEMHCPR
LLSIHVPDSE LGSHFGKLLD TLQGSDVTFD VAGEKFQAHK LVLAARSQFF RSMFYNTLAE
NNSDVVISDL EPKVFKALLH FMYKDSLPGD VEPLTAHSFD LLRPSEIDDT LIVKLLAAAE
MYNLSRLRLL CESHICKGIS ISSVSKILAL SDKYNASELK SVSLKFTAEN LAAVLQTKAY
EDLKDDCPNL QSELLKAVAG YDDTSSSGGG KSQSVWAQLS NGGETSSRRV RQRTT
