BPM3_ARATH
ID BPM3_ARATH Reviewed; 408 AA.
AC O22286; Q2V416; Q8L977;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=BTB/POZ and MATH domain-containing protein 3;
DE AltName: Full=Protein BTB-POZ AND MATH DOMAIN 3;
DE Short=AtBPM3;
GN Name=BPM3; OrderedLocusNames=At2g39760; ORFNames=T5I7.6;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP GENE FAMILY, NOMENCLATURE, FUNCTION, IDENTIFICATION IN THE CUL3-RBX1-BTB
RP UBIQUITIN-PROTEIN LIGASE COMPLEX, INTERACTION WITH CUL3A AND CUL3B,
RP 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 [9]
RP INTERACTION WITH RAP2-4 AND RAP2-13, TISSUE SPECIFICITY, AND SUBCELLULAR
RP 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 [10]
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. {ECO:0000269|PubMed:15618422}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer or heterodimer with BPM3 and BPM5. Interacts with
CC CUL3A and CUL3B. Interacts with RAP2-4 and RAP2-13. Binds to MYB56 at
CC the promoter of FLOWERING LOCUS T (FT) (PubMed:25343985).
CC {ECO:0000269|PubMed:15618422, ECO:0000269|PubMed:15772280,
CC ECO:0000269|PubMed:19843165, ECO:0000269|PubMed:25343985}.
CC -!- INTERACTION:
CC O22286; Q9FWW2: At1g12120; NbExp=3; IntAct=EBI-540923, EBI-25518624;
CC O22286; F4JUM1: At4g14160; NbExp=4; IntAct=EBI-540923, EBI-25510940;
CC O22286; O22286: BPM3; NbExp=5; IntAct=EBI-540923, EBI-540923;
CC O22286; B9DGI8: BZIP63; NbExp=3; IntAct=EBI-540923, EBI-942713;
CC O22286; Q9ZVH4: CUL3A; NbExp=3; IntAct=EBI-540923, EBI-531362;
CC O22286; O65665: ERF060; NbExp=3; IntAct=EBI-540923, EBI-7529041;
CC O22286; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-540923, EBI-2000137;
CC O22286; O49653: GCP2; NbExp=4; IntAct=EBI-540923, EBI-4458381;
CC O22286; Q9LV52: HSFC1; NbExp=5; IntAct=EBI-540923, EBI-4457746;
CC O22286; Q9SWI1: PKS1; NbExp=3; IntAct=EBI-540923, EBI-626200;
CC O22286; Q8H1E4: RAP2-4; NbExp=2; IntAct=EBI-540923, EBI-7528315;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843165}. Cytoplasm
CC {ECO:0000269|PubMed:19843165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O22286-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O22286-2; Sequence=VSP_040655, VSP_040656;
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 -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Tdpoz family. {ECO:0000305}.
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DR EMBL; AC003000; AAB87125.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09719.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09720.1; -; Genomic_DNA.
DR EMBL; AY128315; AAM91518.1; -; mRNA.
DR EMBL; BT000044; AAN15363.1; -; mRNA.
DR EMBL; AK316691; BAH19418.1; -; mRNA.
DR EMBL; AY088598; AAM66127.1; -; mRNA.
DR PIR; T01006; T01006.
DR RefSeq; NP_001031516.1; NM_001036439.2. [O22286-2]
DR RefSeq; NP_030522.1; NM_129534.4. [O22286-1]
DR AlphaFoldDB; O22286; -.
DR SMR; O22286; -.
DR BioGRID; 3899; 43.
DR IntAct; O22286; 35.
DR MINT; O22286; -.
DR STRING; 3702.AT2G39760.1; -.
DR PaxDb; O22286; -.
DR ProteomicsDB; 240502; -. [O22286-1]
DR EnsemblPlants; AT2G39760.1; AT2G39760.1; AT2G39760. [O22286-1]
DR EnsemblPlants; AT2G39760.2; AT2G39760.2; AT2G39760. [O22286-2]
DR GeneID; 818561; -.
DR Gramene; AT2G39760.1; AT2G39760.1; AT2G39760. [O22286-1]
DR Gramene; AT2G39760.2; AT2G39760.2; AT2G39760. [O22286-2]
DR KEGG; ath:AT2G39760; -.
DR Araport; AT2G39760; -.
DR TAIR; locus:2063953; AT2G39760.
DR eggNOG; KOG1987; Eukaryota.
DR InParanoid; O22286; -.
DR OMA; GAVMQSD; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; O22286; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O22286; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22286; baseline and differential.
DR Genevisible; O22286; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
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:0031396; P:regulation of protein ubiquitination; IMP:TAIR.
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 Alternative splicing; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..408
FT /note="BTB/POZ and MATH domain-containing protein 3"
FT /id="PRO_0000405267"
FT DOMAIN 24..158
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 194..261
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT VAR_SEQ 339..343
FT /note="AVMKS -> GTGCI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040655"
FT VAR_SEQ 344..408
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040656"
FT CONFLICT 329
FT /note="E -> K (in Ref. 5; AAM66127)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="L -> F (in Ref. 5; AAM66127)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 44890 MW; 31B93225F439926B CRC64;
MSTVGGIEQL IPDSVSTSFI ETVNGSHQFT IQGYSLAKGM SPGKFIQSDI FSVGGYDWAI
YFYPDGKNPE DQSSYISLFI ALASDSNDIR ALFELTLMDQ SGKGKHKVHS HFDRALEGGP
YTLKYKGSMW GYKRFFKRSA LETSDYLKDD CLVINCTVGV VRARLEGPKQ YGIVLPLSNM
GQGLKDLLDS EVGCDIAFQV GDETYKAHKL ILAARSPVFR AQFFGPIGNN NVDRIVIDDI
EPSIFKAMLS FIYTDVLPNV HEITGSTSAS SFTNMIQHLL AAADLYDLAR LKILCEVLLC
EKLDVDNVAT TLALAEQHQF LQLKAFCLEF VASPANLGAV MKSEGFKHLK QSCPTLLSEL
LNTVAAADKS STSGQSNKKR SASSVLGCDT TNVRQLRRRT RKEVRAVS
