BT1_ARATH
ID BT1_ARATH Reviewed; 365 AA.
AC Q9FMK7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=BTB/POZ and TAZ domain-containing protein 1;
DE AltName: Full=BTB and TAZ domain protein 1;
GN Name=BT1; OrderedLocusNames=At5g63160; ORFNames=MDC12.13;
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, SUBCELLULAR
RP LOCATION, INTERACTION WITH GTE9 AND GTE11, TISSUE SPECIFICITY, AND
RP 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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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;
RA Kim C.J., Chen H., Cheuk R., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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, 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).
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. Also targeted for degradation by the 26S proteasome pathway.
CC May be involved in gametophyte development.
CC {ECO:0000269|PubMed:19054356}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CUL3A. Interacts with GTE9/BET9 and GTE11/BET10
CC through the BTB domain. {ECO:0000269|PubMed:15316289,
CC ECO:0000269|PubMed:15772280}.
CC -!- INTERACTION:
CC Q9FMK7; Q93ZB7: GTE11; NbExp=3; IntAct=EBI-541001, EBI-1394728;
CC Q9FMK7; P13868: PCM1; Xeno; NbExp=2; IntAct=EBI-541001, EBI-1394541;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in young leaves, roots and
CC stems. {ECO:0000269|PubMed:15316289, ECO:0000269|PubMed:19054356}.
CC -!- INDUCTION: Up-regulated by auxin (IAA). Down-regulated by salicylic
CC acid (SA) and hydrogen peroxide. {ECO:0000269|PubMed:15316289,
CC ECO:0000269|PubMed:19054356}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
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DR EMBL; AY316674; AAQ87004.1; -; mRNA.
DR EMBL; AB008265; BAB10558.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97712.1; -; Genomic_DNA.
DR EMBL; BT010872; AAR24650.1; -; mRNA.
DR EMBL; AK227278; BAE99302.1; -; mRNA.
DR RefSeq; NP_201121.1; NM_125711.5.
DR AlphaFoldDB; Q9FMK7; -.
DR SMR; Q9FMK7; -.
DR BioGRID; 21680; 6.
DR IntAct; Q9FMK7; 8.
DR STRING; 3702.AT5G63160.1; -.
DR PaxDb; Q9FMK7; -.
DR PRIDE; Q9FMK7; -.
DR ProteomicsDB; 222821; -.
DR EnsemblPlants; AT5G63160.1; AT5G63160.1; AT5G63160.
DR GeneID; 836437; -.
DR Gramene; AT5G63160.1; AT5G63160.1; AT5G63160.
DR KEGG; ath:AT5G63160; -.
DR Araport; AT5G63160; -.
DR TAIR; locus:2161962; AT5G63160.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_037906_0_0_1; -.
DR OrthoDB; 1164872at2759; -.
DR PhylomeDB; Q9FMK7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FMK7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMK7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009553; P:embryo sac development; IGI:TAIR.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
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:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IEP: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..365
FT /note="BTB/POZ and TAZ domain-containing protein 1"
FT /id="PRO_0000406142"
FT DOMAIN 25..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 205..304
FT /note="TAZ-type"
FT REGION 315..338
FT /note="CaM-binding"
FT MOTIF 193..202
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 365 AA; 41480 MW; 53142FB681946BE5 CRC64;
MAITATQNDG VSLNANKISY DLVETDVEII TSGRRSIPAH SGILASVSPV LTNIIEKPRK
IHGGSSKKVI KILGVPCDAV SVFVRFLYSP SVTENEMEKY GIHLLALSHV YMVTQLKQRC
TKGVGERVTA ENVVDILQLA RLCDAPDLCL KCMRFIHYKF KTVEQTEGWK FLQEHDPFLE
LDILQFIDDA ESRKKRRRRH RREQNLYLQL SEAMECIEHI CTEGCTLVGP SSNLDNKSTC
QAKPGPCSAF STCYGLQLLI RHFAVCKKRV DGKGCVRCKR MIQLLRLHSS ICDQSESCRV
PLCRQYKNRG EKDKKMVEDT KWKVLVRRVA SAKAMSSLSQ SKKKKSEVLF KEEAEDLIRI
RNKLM
