BPM5_ARATH
ID BPM5_ARATH Reviewed; 410 AA.
AC Q1EBV6; Q8LFW4; Q94B33;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=BTB/POZ and MATH domain-containing protein 5;
DE AltName: Full=Protein BTB-POZ AND MATH DOMAIN 5;
DE Short=AtBPM5;
GN Name=BPM5; OrderedLocusNames=At5g21010; ORFNames=F22D1, T10F18.30;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 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 [8]
RP INTERACTION WITH RAP2-4, TISSUE SPECIFICITY, INDUCTION, 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 [9]
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:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Heterodimer with BPM1 and BPM3. Interacts with RAP2-4. Binds
CC to MYB56 at the promoter of FLOWERING LOCUS T (FT) (PubMed:25343985).
CC {ECO:0000269|PubMed:15618422, ECO:0000269|PubMed:19843165,
CC ECO:0000269|PubMed:25343985}.
CC -!- INTERACTION:
CC Q1EBV6; O65665: ERF060; NbExp=3; IntAct=EBI-630650, EBI-7529041;
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 -!- INDUCTION: By drought. {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=AAK68819.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC069325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92919.1; -; Genomic_DNA.
DR EMBL; AY042879; AAK68819.1; ALT_FRAME; mRNA.
DR EMBL; BT025978; ABG25067.1; -; mRNA.
DR EMBL; AY084611; AAM61175.1; -; mRNA.
DR RefSeq; NP_197600.1; NM_122109.4.
DR AlphaFoldDB; Q1EBV6; -.
DR SMR; Q1EBV6; -.
DR BioGRID; 17500; 6.
DR IntAct; Q1EBV6; 4.
DR MINT; Q1EBV6; -.
DR STRING; 3702.AT5G21010.1; -.
DR iPTMnet; Q1EBV6; -.
DR PaxDb; Q1EBV6; -.
DR PRIDE; Q1EBV6; -.
DR ProteomicsDB; 240361; -.
DR EnsemblPlants; AT5G21010.1; AT5G21010.1; AT5G21010.
DR GeneID; 832225; -.
DR Gramene; AT5G21010.1; AT5G21010.1; AT5G21010.
DR KEGG; ath:AT5G21010; -.
DR Araport; AT5G21010; -.
DR TAIR; locus:2147167; AT5G21010.
DR eggNOG; KOG1987; Eukaryota.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q1EBV6; -.
DR OMA; SKFFNEP; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; Q1EBV6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q1EBV6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1EBV6; baseline and differential.
DR Genevisible; Q1EBV6; 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: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 Cytoplasm; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..410
FT /note="BTB/POZ and MATH domain-containing protein 5"
FT /id="PRO_0000405269"
FT DOMAIN 28..162
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 198..264
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 57
FT /note="V -> I (in Ref. 5; AAM61175)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 45191 MW; 0AC2FE4586F092B2 CRC64;
MSESVIQGSN PDRVLSPTSS KSVTQTVNGS HQFVIQGYSL AKGMGIGKHI ASDNFSVGGY
QWGIFFYPDG KNPEDNSSYV SVFIALASEG TEVRALFELA LVDQSGKGKH KVHSHFERSL
DGGPYTLKYR GSMWGYKRFF RRSILETSDY LKDDCLIINC TVGVVVSEIL CPQLHSVHVP
DSELGSHFGV LLDSMEGSDI TFNIAGEKFL AHKLVLAARS PFFKSKFFSE FEANNTEVTI
NDLEPKVFKA LLQFMYKDSL PEDVEPATAH TFERLKLSEI YETLIVKVLA AADKYDLIRL
RLLCESHICK GVSVKSVAKI LALADRYNAK ELKGVCLKFT AENLAAVLET DAYQQMKDEC
VTLQSELLKA VAGHEEGSNS TGGAKSQSVW AQLSDGGGDT TSRHVRQRTT
