BT3_ARATH
ID BT3_ARATH Reviewed; 364 AA.
AC Q9SYL0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=BTB/POZ and TAZ domain-containing protein 3;
DE AltName: Full=BTB and TAZ domain protein 3;
GN Name=BT3; OrderedLocusNames=At1g05690; ORFNames=F3F20.14;
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 2), GENE FAMILY, NOMENCLATURE, TISSUE
RP 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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 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 [7]
RP FUNCTION.
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. Essential for female and male gametophyte development.
CC {ECO:0000269|PubMed:19054356}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with CUL3A. {ECO:0000269|PubMed:15772280}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SYL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SYL0-2; Sequence=VSP_040775;
CC -!- TISSUE SPECIFICITY: Preferentially expressed in leaves.
CC {ECO:0000269|PubMed:15316289}.
CC -!- INDUCTION: Down-regulated by salicylic acid (SA), ethylene, hydrogen
CC peroxide and cold. Up-regulated by NaCl. {ECO:0000269|PubMed:15316289}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD30625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY316676; AAQ87006.1; -; mRNA.
DR EMBL; AC007153; AAD30625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27877.1; -; Genomic_DNA.
DR EMBL; BX813844; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B86191; B86191.
DR RefSeq; NP_172060.2; NM_100449.4. [Q9SYL0-1]
DR AlphaFoldDB; Q9SYL0; -.
DR SMR; Q9SYL0; -.
DR BioGRID; 22318; 1.
DR IntAct; Q9SYL0; 2.
DR STRING; 3702.AT1G05690.1; -.
DR PaxDb; Q9SYL0; -.
DR PRIDE; Q9SYL0; -.
DR EnsemblPlants; AT1G05690.1; AT1G05690.1; AT1G05690. [Q9SYL0-1]
DR GeneID; 837076; -.
DR Gramene; AT1G05690.1; AT1G05690.1; AT1G05690. [Q9SYL0-1]
DR KEGG; ath:AT1G05690; -.
DR Araport; AT1G05690; -.
DR TAIR; locus:2031993; AT1G05690.
DR eggNOG; KOG1778; Eukaryota.
DR HOGENOM; CLU_037906_1_0_1; -.
DR InParanoid; Q9SYL0; -.
DR OMA; GIRCIKI; -.
DR OrthoDB; 1164872at2759; -.
DR PhylomeDB; Q9SYL0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SYL0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYL0; baseline and differential.
DR Genevisible; Q9SYL0; AT.
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:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; 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 GO; GO:0009651; P:response to salt stress; 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 Alternative splicing; Metal-binding; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..364
FT /note="BTB/POZ and TAZ domain-containing protein 3"
FT /id="PRO_0000406144"
FT DOMAIN 54..122
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 232..322
FT /note="TAZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 333..355
FT /note="CaM-binding"
FT /evidence="ECO:0000250"
FT VAR_SEQ 323..364
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15316289"
FT /id="VSP_040775"
SQ SEQUENCE 364 AA; 41524 MW; 7011FA737154DF34 CRC64;
MSSSTKNIPK PPPLPCITYQ RFQSSTRKPS SLMRLVPKEA LETWDKLFKE GSGADTYVET
DNKSHFPAHS SVLAAASPVI ATLLNQSRDK NGNTYLKIHG VPCEAVYMFI RFLYSSCYEE
EEMKKFVLHL LVLSHCYSVP SLKRLCVEIL DQGWINKENV IDVLQLARNC DVTRICFVCL
SMVIKDFKSV SSTEGWKVMK RSNPLLEQEL IEAVIESDSR KQERRRKLEE REVYLQLYEA
MEALVHICRE GCGTIGPRDK ALKGSHTVCK FPACKGLEGA LRHFLGCKSR ASCSHCKRMW
QLLQLHSCIC DDSNSCKVSL CWNFKEKMKK LSKKEQSKWR LLVENIIRAR NSLGPFSSRS
SGLI
