BT5_ARATH
ID BT5_ARATH Reviewed; 368 AA.
AC Q6EJ98; Q8GW52; Q8LFA7; Q9SZF4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=BTB/POZ and TAZ domain-containing protein 5;
DE AltName: Full=BTB and TAZ domain protein 5;
GN Name=BT5; OrderedLocusNames=At4g37610; ORFNames=F19F18.100;
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, TISSUE SPECIFICITY,
RP 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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [9]
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.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CUL3A. {ECO:0000269|PubMed:15772280}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19054356}.
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), salicylic acid (SA), hydrogen
CC peroxide and cold. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38300.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80426.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY316678; AAQ87008.1; -; mRNA.
DR EMBL; AL035605; CAB38300.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161591; CAB80426.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86816.1; -; Genomic_DNA.
DR EMBL; AK119075; BAC43651.1; -; mRNA.
DR EMBL; BT025247; ABF19000.1; -; mRNA.
DR EMBL; AY084954; AAM61515.1; -; mRNA.
DR PIR; T04718; T04718.
DR RefSeq; NP_568031.1; NM_119924.3.
DR AlphaFoldDB; Q6EJ98; -.
DR SMR; Q6EJ98; -.
DR BioGRID; 15196; 2.
DR IntAct; Q6EJ98; 3.
DR STRING; 3702.AT4G37610.1; -.
DR PaxDb; Q6EJ98; -.
DR PRIDE; Q6EJ98; -.
DR EnsemblPlants; AT4G37610.1; AT4G37610.1; AT4G37610.
DR GeneID; 829915; -.
DR Gramene; AT4G37610.1; AT4G37610.1; AT4G37610.
DR KEGG; ath:AT4G37610; -.
DR Araport; AT4G37610; -.
DR TAIR; locus:2120056; AT4G37610.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_037906_1_0_1; -.
DR InParanoid; Q6EJ98; -.
DR OMA; VCESEFE; -.
DR OrthoDB; 1164872at2759; -.
DR PhylomeDB; Q6EJ98; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6EJ98; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q6EJ98; baseline and differential.
DR Genevisible; Q6EJ98; AT.
DR GO; GO:0005737; C:cytoplasm; 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: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:0009409; P:response to cold; IEP:UniProtKB.
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.
DR PROSITE; PS50134; ZF_TAZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Reference proteome; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..368
FT /note="BTB/POZ and TAZ domain-containing protein 5"
FT /id="PRO_0000406146"
FT DOMAIN 55..123
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 233..324
FT /note="TAZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..358
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT CONFLICT 107
FT /note="L -> V (in Ref. 6; AAM61515)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Missing (in Ref. 6; AAM61515)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="N -> K (in Ref. 6; AAM61515)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> T (in Ref. 4; BAC43651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 42314 MW; CB531228DAB7212B CRC64;
MENMDDFSPE NVLAPPPPPP PMKKSTDLFM QRSNSFVSKA TRDSWDRMFD EAHGADVLIH
TDDNGLIYAH SNVIGMASDV IRGMMKQHKR KSHRKSISIL GVPHHALRVF IRFLYSSCYE
KQDMEDFAIH LLVLSHVYVV PHLKRVCESE FESSLLNKEN VIDVFQLALL CDAPRLGLLC
HRMILNNFEE VSTSEGWQAM KESHPRLQKE LLRSVAYELN SLKQRNRKQK EIQTYTQLYE
AMEAFVHICR DGCREIGPTK TETPHMSCGF QACNGLEQLL KHLAGCKLRS IPGGCSRCKR
MWQLLELHSR ICVDSEQCKV PLCSSLKERM KTQSRKDEKR WKLLVRNVLS TKRIGGSPFF
LQAIDVTL
