BPM4_ARATH
ID BPM4_ARATH Reviewed; 465 AA.
AC Q9SRV1; Q8LGI9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=BTB/POZ and MATH domain-containing protein 4;
DE AltName: Full=Protein BTB-POZ AND MATH DOMAIN 4;
DE Short=AtBPM4;
GN Name=BPM4; OrderedLocusNames=At3g03740; ORFNames=F20H23.23;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-465.
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 [5]
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 [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, 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 [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. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with RAP2-4 (PubMed:19843165). Binds to MYB56 at the
CC promoter of FLOWERING LOCUS T (FT) (PubMed:25343985).
CC {ECO:0000269|PubMed:19843165, ECO:0000269|PubMed:25343985}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19843165}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {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=AAM60841.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009540; AAF00643.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73980.1; -; Genomic_DNA.
DR EMBL; AF367309; AAK32896.1; -; mRNA.
DR EMBL; AY059150; AAL15375.1; -; mRNA.
DR EMBL; AY084246; AAM60841.1; ALT_INIT; mRNA.
DR RefSeq; NP_566212.2; NM_111245.3.
DR AlphaFoldDB; Q9SRV1; -.
DR SMR; Q9SRV1; -.
DR BioGRID; 6503; 3.
DR IntAct; Q9SRV1; 1.
DR MINT; Q9SRV1; -.
DR STRING; 3702.AT3G03740.1; -.
DR iPTMnet; Q9SRV1; -.
DR PaxDb; Q9SRV1; -.
DR PRIDE; Q9SRV1; -.
DR ProteomicsDB; 240503; -.
DR EnsemblPlants; AT3G03740.1; AT3G03740.1; AT3G03740.
DR GeneID; 821170; -.
DR Gramene; AT3G03740.1; AT3G03740.1; AT3G03740.
DR KEGG; ath:AT3G03740; -.
DR Araport; AT3G03740; -.
DR TAIR; locus:2079384; AT3G03740.
DR eggNOG; KOG1987; Eukaryota.
DR HOGENOM; CLU_004253_2_0_1; -.
DR InParanoid; Q9SRV1; -.
DR OMA; VRSTIEC; -.
DR OrthoDB; 864323at2759; -.
DR PhylomeDB; Q9SRV1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SRV1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRV1; baseline and differential.
DR Genevisible; Q9SRV1; AT.
DR GO; GO:0005829; C:cytosol; 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; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..465
FT /note="BTB/POZ and MATH domain-containing protein 4"
FT /id="PRO_0000405268"
FT DOMAIN 46..180
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT DOMAIN 216..282
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 12..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 50998 MW; 5D687CF3683AC004 CRC64;
MKSVIFTEEK NLQRQNPLQK SEQQRRNFEM PSPPTTTSLS VTQTINGSHS FTIKGYSLAK
GIGIGKHIAS DTFTVGGYQW AIYFYPDGKN PEDNSAYVSV FIALASDGTD VRALFELSLL
DQSGKGKHKV HSHFDRALES GPYTLKYRGS MWGYKRFFRR LMLETSDFLK DDCLKINCTV
GVVVSEIDCP RLHSIHVPAS DIGSHFGMLL ENEDGSDITF NVSGEKFRAH RLVLAARSPV
FESEFLDVTG EEDRDIEVTD MEPKVFKALL HYIYKDALIE DAESSSSSGS SVGPSASDTL
AAKLLGAADK YKLPRLSLMC ESVLCKDISV DSVANILALA DRYNASALKS VCLKFAAENL
IAVMRSDGFD YLREHCPSLQ SELLKTVAGC EEELSGGGGK TRSVWGQFSD GGAETNGRQA
QTWGDINGGA ERSQSVWVEV VNANGSGRNN NDNNNSDDPM AELED
