BT2_ARATH
ID BT2_ARATH Reviewed; 364 AA.
AC Q94BN0; Q9STL6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=BTB/POZ and TAZ domain-containing protein 2;
DE AltName: Full=BTB and TAZ domain protein 2;
GN Name=BT2; OrderedLocusNames=At3g48360; ORFNames=T29H11.120;
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 [MRNA], GENE FAMILY, NOMENCLATURE, INTERACTION WITH
RP GTE11, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=15316289; DOI=10.1023/b:plan.0000038269.98972.bb;
RA Du L., Poovaiah B.W.;
RT "A novel family of Ca2+/calmodulin-binding proteins involved in
RT transcriptional regulation: interaction with fsh/Ring3 class transcription
RT activators.";
RL Plant Mol. Biol. 54:549-569(2004).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
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 FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY AUXIN.
RX PubMed=17220202; DOI=10.1105/tpc.106.044321;
RA Ren S., Mandadi K.K., Boedeker A.L., Rathore K.S., McKnight T.D.;
RT "Regulation of telomerase in Arabidopsis by BT2, an apparent target of
RT TELOMERASE ACTIVATOR1.";
RL Plant Cell 19:23-31(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY AUXIN, AND TISSUE SPECIFICITY.
RX PubMed=19054356; DOI=10.1111/j.1365-313x.2008.03764.x;
RA Robert H.S., Quint A., Brand D., Vivian-Smith A., Offringa R.;
RT "BTB AND TAZ DOMAIN scaffold proteins perform a crucial function in
RT Arabidopsis development.";
RL Plant J. 58:109-121(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=19525324; DOI=10.1104/pp.109.139220;
RA Mandadi K.K., Misra A., Ren S., McKnight T.D.;
RT "BT2, a BTB protein, mediates multiple responses to nutrients, stresses,
RT and hormones in Arabidopsis.";
RL Plant Physiol. 150:1930-1939(2009).
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. Plays a key role as a component of the TAC1-mediated
CC telomerase activation pathway certainly by targeting a telomerase
CC repressor to degradation. Seems to occupy an integral position in a
CC complex signaling network that perceives, integrates, and responds to
CC multiple, and sometimes competing, signals. Enhances responses to auxin
CC in postgermination and vegetative development. Also negatively
CC regulates ABA- and sugar-mediated inhibition of the germination.
CC Essential for female and male gametophyte development.
CC {ECO:0000269|PubMed:17220202, ECO:0000269|PubMed:19054356,
CC ECO:0000269|PubMed:19525324}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CUL3A. Interacts with GTE11/BET10 through the
CC BTB domain. {ECO:0000269|PubMed:15316289, ECO:0000269|PubMed:15772280}.
CC -!- INTERACTION:
CC Q94BN0; Q39016: CPK11; NbExp=7; IntAct=EBI-540986, EBI-979321;
CC Q94BN0; Q38869: CPK4; NbExp=7; IntAct=EBI-540986, EBI-979475;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19054356}. Cytoplasm
CC {ECO:0000269|PubMed:19054356}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in young leaves and roots.
CC {ECO:0000269|PubMed:15316289, ECO:0000269|PubMed:19054356}.
CC -!- INDUCTION: Up-regulated by auxin (IAA), methyl jasmonate (MeJA),
CC hydrogen peroxide and nitrates. Down-regulated by salicylic acid (SA),
CC abscisic acid (ABA), hydrogen peroxide, sugars, cold and NaCl.
CC Positively regulated by the transcriptional factor TAC1. Circadian-
CC regulation; expression increase during the dark phase and decrease
CC during the light phase. {ECO:0000269|PubMed:15316289,
CC ECO:0000269|PubMed:17220202, ECO:0000269|PubMed:19054356,
CC ECO:0000269|PubMed:19525324}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- DISRUPTION PHENOTYPE: Altered response to auxin. Blocked ability of
CC TAC1 to induce telomerase. Hypersensitive response to both sugar and
CC abscisic acid (ABA)-mediated inhibition of germination.
CC {ECO:0000269|PubMed:17220202, ECO:0000269|PubMed:19525324}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41162.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY316675; AAQ87005.1; -; mRNA.
DR EMBL; AL049659; CAB41162.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78407.1; -; Genomic_DNA.
DR EMBL; AY040015; AAK64172.1; -; mRNA.
DR EMBL; AY079408; AAL85139.1; -; mRNA.
DR EMBL; BT000678; AAN31824.1; -; mRNA.
DR EMBL; AK226596; BAE98711.1; -; mRNA.
DR PIR; T06706; T06706.
DR RefSeq; NP_566902.1; NM_114697.4.
DR AlphaFoldDB; Q94BN0; -.
DR SMR; Q94BN0; -.
DR BioGRID; 9313; 6.
DR IntAct; Q94BN0; 7.
DR STRING; 3702.AT3G48360.1; -.
DR PaxDb; Q94BN0; -.
DR PRIDE; Q94BN0; -.
DR ProteomicsDB; 240363; -.
DR EnsemblPlants; AT3G48360.1; AT3G48360.1; AT3G48360.
DR GeneID; 823994; -.
DR Gramene; AT3G48360.1; AT3G48360.1; AT3G48360.
DR KEGG; ath:AT3G48360; -.
DR Araport; AT3G48360; -.
DR TAIR; locus:2101135; AT3G48360.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_037906_0_0_1; -.
DR InParanoid; Q94BN0; -.
DR OrthoDB; 1164872at2759; -.
DR PhylomeDB; Q94BN0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94BN0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94BN0; baseline and differential.
DR Genevisible; Q94BN0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IGI:TAIR.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IGI:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009743; P:response to carbohydrate; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR GO; GO:0010167; P:response to nitrate; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR GO; GO:0010182; P:sugar mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.20.1020.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR044513; BT1/2/3/4/5.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR000197; Znf_TAZ.
DR PANTHER; PTHR46287; PTHR46287; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF02135; zf-TAZ; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00551; ZnF_TAZ; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57933; SSF57933; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..364
FT /note="BTB/POZ and TAZ domain-containing protein 2"
FT /id="PRO_0000406143"
FT DOMAIN 34..106
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 215..316
FT /note="TAZ-type"
FT REGION 327..350
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT MOTIF 203..212
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 364 AA; 41561 MW; 59235A953EC36CD6 CRC64;
MEAVLVAMSV PATTEDDGFS LITDKLSYNL TPTSDVEIVT SDNRRIPAHS GVLASASPVL
MNIMKKPMRR YRGCGSKRVI KILGVPCDAV SVFIKFLYSS SLTEDEMERY GIHLLALSHV
YMVTQLKQRC SKGVVQRLTT ENVVDVLQLA RLCDAPDVCL RSMRLIHSQF KTVEQTEGWK
FIQEHDPFLE LDILQFIDDA ESRKKRRRRH RKEQDLYMQL SEAMECIEHI CTQGCTLVGP
SNVVDNNKKS MTAEKSEPCK AFSTCYGLQL LIRHFAVCKR RNNDKGCLRC KRMLQLFRLH
SLICDQPDSC RVPLCRQFRK RGEQDKKMGE DTKWKLLVTR VVSAKAMTSL CQSKKNKCEQ
AQGV
