BT4_ARATH
ID BT4_ARATH Reviewed; 372 AA.
AC Q9FJX5; Q3E848;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=BTB/POZ and TAZ domain-containing protein 4;
DE AltName: Full=BTB and TAZ domain protein 4;
GN Name=BT4; OrderedLocusNames=At5g67480; ORFNames=K9I9.4;
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] (ISOFORM 1), GENE FAMILY, NOMENCLATURE,
RP INTERACTION WITH 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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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] (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 [5]
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 [6]
RP 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. {ECO:0000250}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with GTE11/BET10 through the BTB domain.
CC {ECO:0000269|PubMed:15316289}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19054356}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FJX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FJX5-2; Sequence=VSP_040776;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in leaves, stems and
CC flowers. {ECO:0000269|PubMed:15316289, ECO:0000269|PubMed:19054356}.
CC -!- INDUCTION: Up-regulated by auxin (IAA), salicylic acid (SA), methyl
CC jasmonate (MeJA), hydrogen peroxide, wounding and NaCl.
CC {ECO:0000269|PubMed:15316289, 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}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
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DR EMBL; AY316677; AAQ87007.1; -; mRNA.
DR EMBL; AB013390; BAB08456.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98349.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98350.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68746.1; -; Genomic_DNA.
DR EMBL; AF446873; AAL38606.1; -; mRNA.
DR EMBL; AY052213; AAK97683.1; -; mRNA.
DR RefSeq; NP_001330470.1; NM_001345832.1. [Q9FJX5-1]
DR RefSeq; NP_201549.1; NM_126148.4. [Q9FJX5-1]
DR RefSeq; NP_975007.1; NM_203278.2. [Q9FJX5-2]
DR AlphaFoldDB; Q9FJX5; -.
DR SMR; Q9FJX5; -.
DR BioGRID; 22126; 3.
DR IntAct; Q9FJX5; 4.
DR STRING; 3702.AT5G67480.2; -.
DR PaxDb; Q9FJX5; -.
DR PRIDE; Q9FJX5; -.
DR EnsemblPlants; AT5G67480.1; AT5G67480.1; AT5G67480. [Q9FJX5-1]
DR EnsemblPlants; AT5G67480.2; AT5G67480.2; AT5G67480. [Q9FJX5-2]
DR EnsemblPlants; AT5G67480.3; AT5G67480.3; AT5G67480. [Q9FJX5-1]
DR GeneID; 836884; -.
DR Gramene; AT5G67480.1; AT5G67480.1; AT5G67480. [Q9FJX5-1]
DR Gramene; AT5G67480.2; AT5G67480.2; AT5G67480. [Q9FJX5-2]
DR Gramene; AT5G67480.3; AT5G67480.3; AT5G67480. [Q9FJX5-1]
DR KEGG; ath:AT5G67480; -.
DR Araport; AT5G67480; -.
DR TAIR; locus:2158586; AT5G67480.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_037906_1_0_1; -.
DR InParanoid; Q9FJX5; -.
DR OrthoDB; 1164872at2759; -.
DR PhylomeDB; Q9FJX5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FJX5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJX5; baseline and differential.
DR Genevisible; Q9FJX5; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0009739; P:response to gibberellin; IEP:TAIR.
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: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 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 Alternative splicing; Cytoplasm; Metal-binding; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..372
FT /note="BTB/POZ and TAZ domain-containing protein 4"
FT /id="PRO_0000406145"
FT DOMAIN 60..128
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 238..330
FT /note="TAZ-type"
FT REGION 14..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..364
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MQGREDKLNKRM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040776"
SQ SEQUENCE 372 AA; 42461 MW; 99A73DB48E66652F CRC64;
MVTGCVDLHQ SFKSADSSSV PIPPPLPSKS DGLKKKLGHS SVSTATRDMW DRLFNDGYKA
DVVIYTDNGS IIYAHANILG TASTVIKGML KQAKRHGKWH TISIRGVPHD AVRVFIRFLY
SSCYEKEEMN EFIMHLLLLS HAYVVPQLKR VCEWHLEHGL LTTENVVDVF QLALLCDFPR
LSLISHRMIM KHFNELSATE AWTAMKKSHP FLEKEVRDSV IIEANTRKER MRKRNDQRIY
SQLYEAMEAL VHICRDGCKT IGPHDKDFKP NHATCNYEAC KGLESLIRHF AGCKLRVPGG
CVHCKRMWQL LELHSRVCAG SDQCRVPLCR NLKEKMEKQS KKDESRWKLL VKNVLGSKKI
GGSPFFLPVT NC
