ADR2_ARATH
ID ADR2_ARATH Reviewed; 1007 AA.
AC Q9C7X0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Disease resistance protein ADR2 {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Protein ACTIVATED DISEASE RESISTANCE 2 {ECO:0000303|PubMed:19549129};
DE AltName: Full=Protein WHITE RUST RESISTANCE 4 {ECO:0000303|PubMed:18624640};
GN Name=ADR2 {ECO:0000303|PubMed:19549129};
GN Synonyms=WRR4 {ECO:0000303|PubMed:18624640};
GN OrderedLocusNames=At1g56510 {ECO:0000312|Araport:AT1G56510};
GN ORFNames=F13N6.5 {ECO:0000312|EMBL:AAG51508.1};
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=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 [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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia GL1;
RX PubMed=18624640; DOI=10.1094/mpmi-21-6-0757;
RA Borhan M.H., Gunn N., Cooper A., Gulden S., Tor M., Rimmer S.R.,
RA Holub E.B.;
RT "WRR4 encodes a TIR-NB-LRR protein that confers broad-spectrum white rust
RT resistance in Arabidopsis thaliana to four physiological races of Albugo
RT candida.";
RL Mol. Plant Microbe Interact. 21:757-768(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19549129; DOI=10.1111/j.1469-8137.2009.02902.x;
RA Aboul-Soud M.A., Chen X., Kang J.G., Yun B.W., Raja M.U., Malik S.I.,
RA Loake G.J.;
RT "Activation tagging of ADR2 conveys a spreading lesion phenotype and
RT resistance to biotrophic pathogens.";
RL New Phytol. 183:1163-1175(2009).
RN [7]
RP FUNCTION, AND INDUCTION BY UV.
RX PubMed=25656510; DOI=10.1016/j.plaphy.2015.01.011;
RA Piofczyk T., Jeena G., Pecinka A.;
RT "Arabidopsis thaliana natural variation reveals connections between UV
RT radiation stress and plant pathogen-like defense responses.";
RL Plant Physiol. Biochem. 93:34-43(2015).
CC -!- FUNCTION: TIR-NB-LRR receptor-like protein that confers broad-spectrum
CC resistance and full immunity to several races of the pathogen Albugo
CC candida (white rust disease) (PubMed:18624640). Confers resistance to
CC the biotrophic pathogens Pseudomonas syringae pv. tomato DC3000 and
CC Hyaloperonospora arabidopsis isolate Noco2 (PubMed:19549129). May play
CC a role in the response to UV stress (PubMed:25656510).
CC {ECO:0000269|PubMed:18624640, ECO:0000269|PubMed:19549129,
CC ECO:0000269|PubMed:25656510}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:18624640}.
CC -!- INDUCTION: By UV treatment. {ECO:0000269|PubMed:25656510}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000255|PROSITE-ProRule:PRU00204}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are susceptible to white rust fungal
CC pathogen Albugo candida subsp. B (PubMed:18624640). Increased
CC resistance on UV-induced growth inhibition (PubMed:25656510).
CC {ECO:0000269|PubMed:18624640}.
CC -!- MISCELLANEOUS: The gain-of-function mutants adr2 (T-DNA tagging) are
CC dwarf, develop HR-like lesions on leaves, express constitutively
CC defense and antioxidant-related genes, and have increased resistance to
CC biotrophic pathogens. {ECO:0000269|PubMed:19549129}.
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DR EMBL; AC058785; AAG51508.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33401.1; -; Genomic_DNA.
DR EMBL; BT014857; AAT41840.1; -; mRNA.
DR EMBL; AK226771; BAE98869.1; -; mRNA.
DR PIR; G96606; G96606.
DR RefSeq; NP_176043.1; NM_104527.4.
DR AlphaFoldDB; Q9C7X0; -.
DR SMR; Q9C7X0; -.
DR STRING; 3702.AT1G56510.1; -.
DR PaxDb; Q9C7X0; -.
DR PRIDE; Q9C7X0; -.
DR ProteomicsDB; 243285; -.
DR EnsemblPlants; AT1G56510.1; AT1G56510.1; AT1G56510.
DR GeneID; 842104; -.
DR Gramene; AT1G56510.1; AT1G56510.1; AT1G56510.
DR KEGG; ath:AT1G56510; -.
DR Araport; AT1G56510; -.
DR TAIR; locus:2010738; AT1G56510.
DR HOGENOM; CLU_001561_0_1_1; -.
DR InParanoid; Q9C7X0; -.
DR OMA; HAPESSI; -.
DR OrthoDB; 1021451at2759; -.
DR PhylomeDB; Q9C7X0; -.
DR PRO; PR:Q9C7X0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7X0; baseline and differential.
DR Genevisible; Q9C7X0; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0002229; P:defense response to oomycetes; IMP:TAIR.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR011713; Leu-rich_rpt_3.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR11017; PTHR11017; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50104; TIR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Hydrolase; Leucine-rich repeat; NAD;
KW Nucleotide-binding; Plant defense; Reference proteome; Repeat;
KW Stress response.
FT CHAIN 1..1007
FT /note="Disease resistance protein ADR2"
FT /id="PRO_0000433374"
FT DOMAIN 11..175
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 190..443
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 533..556
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 578..600
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 601..623
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 624..647
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 649..670
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 671..693
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 694..714
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 715..737
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 759..782
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 783..809
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT ACT_SITE 86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ SEQUENCE 1007 AA; 113978 MW; E7D55CB5D010F0CF CRC64;
MASSSSSPRN WRYNVFTSFH GPDVRIKFLS HLRQQFVYNG ITMFDDNGIE RSQIIAPALK
KAIGESRVAI VLLSKNYASS SWCLDELLEI LKCKEYIGQI VMTVFYEVDP SHVRKQTGDF
GIAFKETCAH KTEEERSKWS QALTYVGNIA GEDFIHWKDE AKMIEKIARD VSTKINVTPC
RDFDDMVGLE RHLKEMVSLL DLDKEGVKMV GISGPAGIGK STIAKALHSR HSSTFQHNCF
VDNLWENYKI CTGEHGVKLR LHEQFVSKIL KQNGLELTHL SVIKDRLQDK KVLIILDDVE
SLAQLETLAD MTWFGPGSRV IVTTENKEIL QQHGIGDIYQ VGYPSESEAL TIFCLSAFKQ
ASPPDGFMDL ADEVVRICDK LPLALCVLGS SLLRKSQTDW EDELPRLRNC LDGIESVLKV
GFESLNEKDQ ALFLYITVFF NYECADHVTL MLAKSNLNVR LGLKNLANRY LIHIDHDQKK
RVVVHRLLRV MAIQVCTKQK PWKSQILVDA EKIAYVLEEA TGNRSIKGVS FDTAEIDELM
ISPKAFEKMC NLLFLKVYDA GWHTGKRKLD IPEDIKFPRT IRLFHWDAYS GKRLPSSFFA
ENLVEVNMQD SELQKLWEGT QCLANLKKID LSRSSCLTEL PDLSNATNLE DLYVGSCTAL
VELPSSIGNL HKLAHIMMYS CESLEVIPSL INLTSLTFLN MNKCSRLRRF PDIPTSIEDV
QVTGTTLEEL PASLTHCSGL QTIKISGSVN LKIFYTELPV SVSHINISNS GIEWITEDCI
KGLHNLHDLC LSGCKRLVSL PELPRSLKIL QADDCDSLES LNGHLNTPNA ELYFANCFKL
DAEARRAIIQ QSFVSGWALL PGLEVPPEFG HRARGNSLII PYSASNRFKV CVVMSLNHHQ
PFELVPRNLL YRWTVIGDSV SSDEKTFHLS HMFNADSVNS KLQKPHLFIF HSCLPFIFHS
CLPFIFDISN IMLEFSSEYK DFDILECGVQ ILTDETDERN IWGSLVF
