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NPR3_ARATH
ID   NPR3_ARATH              Reviewed;         586 AA.
AC   Q8L746; Q9FHE3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Regulatory protein NPR3;
DE   AltName: Full=BTB/POZ domain-containing protein NPR3;
GN   Name=NPR3; OrderedLocusNames=At5g45110; ORFNames=K17O22_11;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15634206; DOI=10.1111/j.1365-313x.2004.02296.x;
RA   Liu G., Holub E.B., Alonso J.M., Ecker J.R., Fobert P.R.;
RT   "An Arabidopsis NPR1-like gene, NPR4, is required for disease resistance.";
RL   Plant J. 41:304-318(2005).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH TGA FACTORS,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=17076807; DOI=10.1111/j.1365-313x.2006.02903.x;
RA   Zhang Y., Cheng Y.T., Qu N., Zhao Q., Bi D., Li X.;
RT   "Negative regulation of defense responses in Arabidopsis by two NPR1
RT   paralogs.";
RL   Plant J. 48:647-656(2006).
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 (By similarity). Involved in the regulation of basal defense
CC       responses against pathogens. {ECO:0000250,
CC       ECO:0000269|PubMed:17076807}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with TGA2, TGA3, TGA5 and TGA6. Interacts with TGA2
CC       in vivo in the nucleus. {ECO:0000269|PubMed:17076807}.
CC   -!- INTERACTION:
CC       Q8L746; Q9LUX9: At5g58800; NbExp=3; IntAct=EBI-4441365, EBI-4445291;
CC       Q8L746; Q9FNZ5: NIMIN-1; NbExp=4; IntAct=EBI-4441365, EBI-541099;
CC       Q8L746; Q9LUA3: NIMIN-2; NbExp=3; IntAct=EBI-4441365, EBI-541107;
CC       Q8L746; Q9FNZ4: NIMIN-3; NbExp=3; IntAct=EBI-4441365, EBI-541115;
CC       Q8L746; P93002: NPR1; NbExp=2; IntAct=EBI-4441365, EBI-1392127;
CC       Q8L746; Q8L746: NPR3; NbExp=4; IntAct=EBI-4441365, EBI-4441365;
CC       Q8L746; Q5ICL9: NPR4; NbExp=5; IntAct=EBI-4441365, EBI-1392093;
CC       Q8L746; Q93ZX1: RFC4; NbExp=3; IntAct=EBI-4441365, EBI-4470690;
CC       Q8L746; Q39237: TGA1; NbExp=3; IntAct=EBI-4441365, EBI-541351;
CC       Q8L746; P43273: TGA2; NbExp=9; IntAct=EBI-4441365, EBI-541307;
CC       Q8L746; Q39234: TGA3; NbExp=6; IntAct=EBI-4441365, EBI-541366;
CC       Q8L746; Q39163: TGA5; NbExp=4; IntAct=EBI-4441365, EBI-541381;
CC       Q8L746; Q93XM6: TGA9; NbExp=3; IntAct=EBI-4441365, EBI-1237844;
CC       Q8L746; Q94AI7: TPL; NbExp=3; IntAct=EBI-4441365, EBI-2119299;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17076807}.
CC   -!- INDUCTION: Up-regulated following pathogen challenge or salicylic acid
CC       (SA) treatment. {ECO:0000269|PubMed:17076807}.
CC   -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC       of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC   -!- DISRUPTION PHENOTYPE: Elevated PR-1 expression level and enhanced
CC       resistance to Hyaloperonospora parasitica.
CC       {ECO:0000269|PubMed:17076807}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB019224; BAB09496.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED95205.1; -; Genomic_DNA.
DR   EMBL; AY139763; AAM98084.1; -; mRNA.
DR   EMBL; BT004537; AAO42783.1; -; mRNA.
DR   RefSeq; NP_199324.2; NM_123879.3.
DR   AlphaFoldDB; Q8L746; -.
DR   SMR; Q8L746; -.
DR   BioGRID; 19794; 18.
DR   DIP; DIP-59898N; -.
DR   IntAct; Q8L746; 18.
DR   STRING; 3702.AT5G45110.1; -.
DR   PaxDb; Q8L746; -.
DR   PRIDE; Q8L746; -.
DR   ProteomicsDB; 250547; -.
DR   EnsemblPlants; AT5G45110.1; AT5G45110.1; AT5G45110.
DR   GeneID; 834545; -.
DR   Gramene; AT5G45110.1; AT5G45110.1; AT5G45110.
DR   KEGG; ath:AT5G45110; -.
DR   Araport; AT5G45110; -.
DR   TAIR; locus:2153192; AT5G45110.
DR   eggNOG; KOG0504; Eukaryota.
DR   HOGENOM; CLU_034895_1_0_1; -.
DR   InParanoid; Q8L746; -.
DR   OrthoDB; 631377at2759; -.
DR   PhylomeDB; Q8L746; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q8L746; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8L746; baseline and differential.
DR   Genevisible; Q8L746; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:1901149; F:salicylic acid binding; IDA:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IEA:InterPro.
DR   GO; GO:0009627; P:systemic acquired resistance; IGI:TAIR.
DR   GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IEA:InterPro.
DR   Gene3D; 1.25.40.20; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR044292; NPR.
DR   InterPro; IPR021094; NPR1/NIM1-like_C.
DR   InterPro; IPR024228; NPR_central_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   PANTHER; PTHR46475; PTHR46475; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF11900; DUF3420; 1.
DR   Pfam; PF12313; NPR1_like_C; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Nucleus; Phosphoprotein; Plant defense; Reference proteome;
KW   Repeat; Ubl conjugation pathway.
FT   CHAIN           1..586
FT                   /note="Regulatory protein NPR3"
FT                   /id="PRO_0000407992"
FT   DOMAIN          60..135
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   REPEAT          261..291
FT                   /note="ANK 1"
FT   REPEAT          293..320
FT                   /note="ANK 2"
FT   REPEAT          324..353
FT                   /note="ANK 3"
FT   REGION          554..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P93002"
SQ   SEQUENCE   586 AA;  66061 MW;  E0C065A1F4A9F692 CRC64;
     MATLTEPSSS LSFTSSHFSY GSIGSNHFSS SSASNPEVVS LTKLSSNLEQ LLSNSDCDYS
     DAEIIVDGVP VGVHRCILAA RSKFFQDLFK KEKKISKTEK PKYQLREMLP YGAVAHEAFL
     YFLSYIYTGR LKPFPLEVST CVDPVCSHDC CRPAIDFVVQ LMYASSVLQV PELVSSFQRR
     LCNFVEKTLV ENVLPILMVA FNCKLTQLLD QCIERVARSD LYRFCIEKEV PPEVAEKIKQ
     LRLISPQDEE TSPKISEKLL ERIGKILKAL DSDDVELVKL LLTESDITLD QANGLHYSVV
     YSDPKVVAEI LALDMGDVNY RNSRGYTVLH FAAMRREPSI IISLIDKGAN ASEFTSDGRS
     AVNILRRLTN PKDYHTKTAK GRESSKARLC IDILEREIRK NPMVLDTPMC SISMPEDLQM
     RLLYLEKRVG LAQLFFPTEA KVAMDIGNVE GTSEFTGLSP PSSGLTGNLS QVDLNETPHM
     QTQRLLTRMV ALMKTVETGR RFFPYGSEVL DKYMAEYIDD DILDDFHFEK GSTHERRLKR
     MRYRELKDDV QKAYSKDKES KIARSCLSAS SSPSSSSIRD DLHNTT
 
 
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