LOCUS NPR2_ARATH 600 aa linear PLN 27-NOV-2024
DEFINITION RecName: Full=Regulatory protein NPR2; AltName: Full=BTB/POZ
domain-containing protein NPR2.
ACCESSION Q9SZI3
VERSION Q9SZI3.1
DBSOURCE UniProtKB: locus NPR2_ARATH, accession Q9SZI3;
class: standard.
created: May 3, 2011.
sequence updated: May 1, 2000.
annotation updated: Nov 27, 2024.
xrefs: AL049483.1, CAB39677.1, AL161564.2, CAB79467.1, CP002687.1,
AEE85160.1, T04267, NP_194342.1
xrefs (non-sequence databases): AlphaFoldDB:Q9SZI3, SMR:Q9SZI3,
DIP:DIP-59899N, IntAct:Q9SZI3, STRING:3702.Q9SZI3,
PaxDb:3702-AT4G26120.1, EnsemblPlants:AT4G26120.1,
EnsemblPlants:AT4G26120.1, EnsemblPlants:AT4G26120, GeneID:828718,
Gramene:AT4G26120.1, KEGG:ath:AT4G26120, Araport:AT4G26120,
TAIR:AT4G26120, eggNOG:KOG0504, HOGENOM:CLU_034895_1_0_1,
InParanoid:Q9SZI3, OMA:NICGETY, PhylomeDB:Q9SZI3,
UniPathway:UPA00143, PRO:PR:Q9SZI3, Proteomes:UP000006548,
ExpressionAtlas:Q9SZI3, GO:0005737, GO:0016604, GO:0046872,
GO:0042742, GO:0045087, GO:0016567, GO:0031347, GO:2000022,
GO:2000031, GO:0009862, CDD:cd18310, FunFam:1.25.40.20:FF:000239,
FunFam:3.30.710.10:FF:000192, Gene3D:1.25.40.20,
InterPro:IPR002110, InterPro:IPR036770, InterPro:IPR000210,
InterPro:IPR044292, InterPro:IPR021094, InterPro:IPR024228,
InterPro:IPR011333, PANTHER:PTHR46475:SF1, PANTHER:PTHR46475,
Pfam:PF12796, Pfam:PF00651, Pfam:PF11900, Pfam:PF12313,
SMART:SM00248, SMART:SM00225, SUPFAM:SSF48403, SUPFAM:SSF54695,
PROSITE:PS50297, PROSITE:PS50088, PROSITE:PS50097, PROSITE:PS52046
KEYWORDS ANK repeat; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
Plant defense; Reference proteome; Repeat; S-nitrosylation; Ubl
conjugation pathway; Zinc; Zinc-finger.
SOURCE Arabidopsis thaliana (thale cress)
ORGANISM Arabidopsis thaliana
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae;
Camelineae; Arabidopsis.
REFERENCE 1 (residues 1 to 600)
AUTHORS Mayer,K., Schuller,C., Wambutt,R., Murphy,G., Volckaert,G.,
Pohl,T., Dusterhoft,A., Stiekema,W., Entian,K.D., Terryn,N.,
Harris,B., Ansorge,W., Brandt,P., Grivell,L., Rieger,M.,
Weichselgartner,M., de Simone,V., Obermaier,B., Mache,R.,
Muller,M., Kreis,M., Delseny,M., Puigdomenech,P., Watson,M.,
Schmidtheini,T., Reichert,B., Portatelle,D., Perez-Alonso,M.,
Boutry,M., Bancroft,I., Vos,P., Hoheisel,J., Zimmermann,W.,
Wedler,H., Ridley,P., Langham,S.A., McCullagh,B., Bilham,L.,
Robben,J., Van der Schueren,J., Grymonprez,B., Chuang,Y.J.,
Vandenbussche,F., Braeken,M., Weltjens,I., Voet,M., Bastiaens,I.,
Aert,R., Defoor,E., Weitzenegger,T., Bothe,G., Ramsperger,U.,
Hilbert,H., Braun,M., Holzer,E., Brandt,A., Peters,S., van
Staveren,M., Dirske,W., Mooijman,P., Klein Lankhorst,R., Rose,M.,
Hauf,J., Kotter,P., Berneiser,S., Hempel,S., Feldpausch,M.,
Lamberth,S., Van den Daele,H., De Keyser,A., Buysshaert,C.,
Gielen,J., Villarroel,R., De Clercq,R., Van Montagu,M., Rogers,J.,
Cronin,A., Quail,M., Bray-Allen,S., Clark,L., Doggett,J., Hall,S.,
Kay,M., Lennard,N., McLay,K., Mayes,R., Pettett,A.,
Rajandream,M.A., Lyne,M., Benes,V., Rechmann,S., Borkova,D.,
Blocker,H., Scharfe,M., Grimm,M., Lohnert,T.H., Dose,S., de
Haan,M., Maarse,A., Schafer,M., Muller-Auer,S., Gabel,C., Fuchs,M.,
Fartmann,B., Granderath,K., Dauner,D., Herzl,A., Neumann,S.,
Argiriou,A., Vitale,D., Liguori,R., Piravandi,E., Massenet,O.,
Quigley,F., Clabauld,G., Mundlein,A., Felber,R., Schnabl,S.,
Hiller,R., Schmidt,W., Lecharny,A., Aubourg,S., Chefdor,F.,
Cooke,R., Berger,C., Montfort,A., Casacuberta,E., Gibbons,T.,
Weber,N., Vandenbol,M., Bargues,M., Terol,J., Torres,A.,
Perez-Perez,A., Purnelle,B., Bent,E., Johnson,S., Tacon,D.,
Jesse,T., Heijnen,L., Schwarz,S., Scholler,P., Heber,S., Francs,P.,
Bielke,C., Frishman,D., Haase,D., Lemcke,K., Mewes,H.W.,
Stocker,S., Zaccaria,P., Bevan,M., Wilson,R.K., de la Bastide,M.,
Habermann,K., Parnell,L., Dedhia,N., Gnoj,L., Schutz,K., Huang,E.,
Spiegel,L., Sehkon,M., Murray,J., Sheet,P., Cordes,M.,
Abu-Threideh,J., Stoneking,T., Kalicki,J., Graves,T., Harmon,G.,
Edwards,J., Latreille,P., Courtney,L., Cloud,J., Abbott,A.,
Scott,K., Johnson,D., Minx,P., Bentley,D., Fulton,B., Miller,N.,
Greco,T., Kemp,K., Kramer,J., Fulton,L., Mardis,E., Dante,M.,
Pepin,K., Hillier,L., Nelson,J., Spieth,J., Ryan,E., Andrews,S.,
Geisel,C., Layman,D., Du,H., Ali,J., Berghoff,A., Jones,K.,
Drone,K., Cotton,M., Joshu,C., Antonoiu,B., Zidanic,M., Strong,C.,
Sun,H., Lamar,B., Yordan,C., Ma,P., Zhong,J., Preston,R., Vil,D.,
Shekher,M., Matero,A., Shah,R., Swaby,I.K., O'Shaughnessy,A.,
Rodriguez,M., Hoffmann,J., Till,S., Granat,S., Shohdy,N.,
Hasegawa,A., Hameed,A., Lodhi,M., Johnson,A., Chen,E., Marra,M.,
Martienssen,R. and McCombie,W.R.
TITLE Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana
JOURNAL Nature 402 (6763), 769-777 (1999)
PUBMED 10617198
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
STRAIN=cv. Columbia
REFERENCE 2 (residues 1 to 600)
AUTHORS Cheng,C.Y., Krishnakumar,V., Chan,A.P., Thibaud-Nissen,F.,
Schobel,S. and Town,C.D.
TITLE Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome
JOURNAL Plant J 89 (4), 789-804 (2017)
PUBMED 27862469
REMARK GENOME REANNOTATION.;
STRAIN=cv. Columbia
REFERENCE 3 (residues 1 to 600)
AUTHORS Gingerich,D.J., Gagne,J.M., Salter,D.W., Hellmann,H., Estelle,M.,
Ma,L. and Vierstra,R.D.
TITLE Cullins 3a and 3b assemble with members of the broad
complex/tramtrack/bric-a-brac (BTB) protein family to form
essential ubiquitin-protein ligases (E3s) in Arabidopsis
JOURNAL J Biol Chem 280 (19), 18810-18821 (2005)
PUBMED 15749712
REMARK DOMAIN BTB.
REFERENCE 4 (residues 1 to 600)
AUTHORS Liu,G., Holub,E.B., Alonso,J.M., Ecker,J.R. and Fobert,P.R.
TITLE An Arabidopsis NPR1-like gene, NPR4, is required for disease
resistance
JOURNAL Plant J 41 (2), 304-318 (2005)
PUBMED 15634206
REMARK GENE FAMILY, AND NOMENCLATURE.
REFERENCE 5 (residues 1 to 600)
AUTHORS Fu,Z.Q., Yan,S., Saleh,A., Wang,W., Ruble,J., Oka,N., Mohan,R.,
Spoel,S.H., Tada,Y., Zheng,N. and Dong,X.
TITLE NPR3 and NPR4 are receptors for the immune signal salicylic acid in
plants
JOURNAL Nature 486 (7402), 228-232 (2012)
PUBMED 22699612
REMARK INTERACTION WITH NPR1.;
STRAIN=cv. Columbia
Publication Status: Online-Only
COMMENT On Sep 14, 2005 this sequence version replaced gi:7487977.
[FUNCTION] Salicylic acid (SA)-binding substrate-specific adapter
of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which
mediates the ubiquitination and subsequent proteasomal degradation
of target proteins (By similarity). Transcription cofactor that
represses gene expression in the absence of salicylic acid (SA),
when attached to negative cis-elements (W-box) with WRKY
transcription factors, but stimulates gene expression upon
activation by SA, when sumoylated and attached to positive
cis-elements (as-1) with TGA transcription factors, thus confering
immunity through a series of gene regulations ending in a
significant increase in antimicrobial and defense genes expression
(By similarity). May be involved in regulating basal defense
responses against pathogens, and may be involved in crosstalk
between SA- and JA-dependent signaling pathways (By similarity).
{ECO:0000250|UniProtKB:O22286, ECO:0000250|UniProtKB:P93002,
ECO:0000250|UniProtKB:Q5ICL9}.
[PATHWAY] Protein modification; protein ubiquitination.
{ECO:0000250|UniProtKB:O22286}.
[SUBUNIT] Interacts with NPR1 independently of SA.
{ECO:0000269|PubMed:22699612}.
[INTERACTION] Q9SZI3; P93002: NPR1; NbExp=2; IntAct=EBI-15987489,
EBI-1392127.
[SUBCELLULAR LOCATION] Cytoplasm {ECO:0000250|UniProtKB:P93002}.
Nucleus {ECO:0000250|UniProtKB:P93002}. Nucleus, nuclear body
{ECO:0000250|UniProtKB:P93002}. Note=Accumulation in nucleus after
induction by salicylic acid (SA) treatment or after pathogen
infection. {ECO:0000250|UniProtKB:P93002}.
[DOMAIN] The BTB/POZ domain mediates the interaction with some
component of ubiquitin ligase complexes.
{ECO:0000269|PubMed:15749712}.
[SIMILARITY] Belongs to the plant 'ANKYRIN-BTB/POZ' family.
'NPR1-like' subfamily. {ECO:0000305}.
FEATURES Location/Qualifiers
source 1..600
/organism="Arabidopsis thaliana"
/db_xref="taxon:3702"
gene 1..600
/gene="NPR2"
/locus_tag="At4g26120"
/gene_synonym="F20B18.230"
Protein 1..600
/product="Regulatory protein NPR2"
/note="BTB/POZ domain-containing protein NPR2"
/UniProtKB_evidence="Evidence at protein level"
Region 1..600
/region_name="Mature chain"
/note="Regulatory protein NPR2. /id=PRO_0000407991."
Site 15
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P93002."
Site 19
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P93002."
Region 49..193
/region_name="BTB_POZ_NPR_plant"
/note="BTB (Broad-Complex, Tramtrack and Bric a brac) /POZ
(poxvirus and zinc finger) domain found in plant
regulatory proteins, NPR1-4, and similar proteins;
cd18310"
/db_xref="CDD:349619"
Region 67..143
/region_name="Domain"
/note="BTB.
/evidence=ECO:0000255|PROSITE-ProRule:PRU00037."
Region 146..160
/region_name="Zinc finger region"
/note="C2HC NPR-type.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01391."
Site 155
/site_type="modified"
/note="S-nitrosocysteine.
/evidence=ECO:0000255|PROSITE-ProRule:PRU01391."
Region 230..270
/region_name="DUF3420"
/note="Domain of unknown function (DUF3420); pfam11900"
/db_xref="CDD:314729"
Region 264..294
/region_name="Repetitive region"
/note="ANK 1. /evidence=ECO:0000255."
Region <269..>386
/region_name="ANKYR"
/note="Ankyrin repeat [Signal transduction mechanisms];
COG0666"
/db_xref="CDD:440430"
Region 287..325
/region_name="ANK repeat"
/note="ANK repeat [structural motif]"
/db_xref="CDD:293786"
Region 296..323
/region_name="Repetitive region"
/note="ANK 2. /evidence=ECO:0000255."
Region 327..358
/region_name="ANK repeat"
/note="ANK repeat [structural motif]"
/db_xref="CDD:293786"
Region 327..356
/region_name="Repetitive region"
/note="ANK 3. /evidence=ECO:0000255."
Region 369..572
/region_name="NPR1_like_C"
/note="NPR1/NIM1 like defence protein C terminal;
pfam12313"
/db_xref="CDD:372037"
Region 386..523
/region_name="Region of interest in the sequence"
/note="Salicylic acid-binding core (SBC).
/evidence=ECO:0000250|UniProtKB:Q5ICL9."
Region 554..600
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
Region 585..600
/region_name="Compositionally biased region"
/note="Basic and acidic residues.
/evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
1 mattttttta rfsdsyefsn tsgnsffaae ssldyptefl tppevsalkl lsnclesvfd
61 spetfysdak lvlaggrevs fhrcilsari pvfksalatv keqkssttvk lqlkeiardy
121 evgfdsvvav layvysgrvr sppkgasacv dddcchvacr skvdfmvevl ylsfvfqiqe
181 lvtlyerqfl eivdkvvved ilvifkldtl cgttykklld rcieiivksd ielvsleksl
241 pqhifkqiid irealclepp klerhvkniy kaldsddvel vkmllleght nldeayalhf
301 aiahcavkta ydllelelad vnlrnprgyt vlhvaamrke pkliisllmk ganildttld
361 grtalvivkr ltkaddykts tedgtpslkg glcievlehe qkleylspie aslslpvtpe
421 elrmrllyye nrvalarllf pvetetvqgi akleetceft asslepdhhi gekrtsldln
481 mapfqihekh lsrlralckt velgkryfkr csldhfmdte dlnhlasvee dtpekrlqkk
541 qrymelqetl mktfsedkee cgksstpkpt savrsnrkls hrrlkvdkrd flkrpygngd
//