RPP2B_ARATH
ID RPP2B_ARATH Reviewed; 1207 AA.
AC F4JT80; A0A1P8B4Q1; O49469;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Disease resistance protein RPP2B {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
GN Name=RPP2B {ECO:0000303|PubMed:15165183};
GN OrderedLocusNames=At4g19510 {ECO:0000312|Araport:AT4G19510};
GN ORFNames=F24J7.70 {ECO:0000312|EMBL:CAA16928.1};
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=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 [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] (ISOFORM 2).
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 [4]
RP FUNCTION, AND MUTAGENESIS OF GLY-121; LEU-726; THR-944 AND GLU-955.
RX PubMed=15165183; DOI=10.1111/j.1365-313x.2004.02099.x;
RA Sinapidou E., Williams K., Nott L., Bahkt S., Toer M., Crute I.,
RA Bittner-Eddy P., Beynon J.;
RT "Two TIR:NB:LRR genes are required to specify resistance to Peronospora
RT parasitica isolate Cala2 in Arabidopsis.";
RL Plant J. 38:898-909(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Disease resistance protein that cooperates with RPP2A to
CC confer resistance to Hyaloperonospora parasitica isolate Cala2.
CC {ECO:0000269|PubMed:15165183}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4JT80-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4JT80-2; Sequence=VSP_059609;
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 -!- SIMILARITY: Belongs to the disease resistance TIR-NB-LRR family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE84192.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AK229040; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=ANM66560.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ANM66561.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ANM66562.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ANM66563.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA16928.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78953.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIB-LRRS; Note=Functional and comparative genomics
CC of disease resistance gene homologs;
CC URL="http://niblrrs.ucdavis.edu";
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DR EMBL; AL021768; CAA16928.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161551; CAB78953.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; ANM66561.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; ANM66562.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; ANM66563.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE84192.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; ANM66560.1; ALT_INIT; Genomic_DNA.
DR EMBL; AK229040; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T06144; T06144.
DR RefSeq; NP_001328446.1; NM_001341350.1.
DR RefSeq; NP_001328447.1; NM_001341347.1.
DR RefSeq; NP_001328448.1; NM_001341346.1.
DR RefSeq; NP_001328449.1; NM_001341349.1.
DR RefSeq; NP_193686.5; NM_118071.6.
DR AlphaFoldDB; F4JT80; -.
DR SMR; F4JT80; -.
DR STRING; 3702.AT4G19510.1; -.
DR iPTMnet; F4JT80; -.
DR PaxDb; F4JT80; -.
DR PRIDE; F4JT80; -.
DR ProMEX; F4JT80; -.
DR EnsemblPlants; AT4G19510.5; AT4G19510.5; AT4G19510.
DR GeneID; 827692; -.
DR Gramene; AT4G19510.5; AT4G19510.5; AT4G19510.
DR KEGG; ath:AT4G19510; -.
DR Araport; AT4G19510; -.
DR TAIR; locus:2122965; AT4G19510.
DR eggNOG; ENOG502SI7S; Eukaryota.
DR HOGENOM; CLU_001561_0_3_1; -.
DR InParanoid; F4JT80; -.
DR OrthoDB; 76656at2759; -.
DR PRO; PR:F4JT80; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JT80; baseline and differential.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
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; IPR045344; C-JID.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR001611; Leu-rich_rpt.
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 InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11017; PTHR11017; 2.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Hydrolase; Leucine-rich repeat; NAD;
KW Nucleotide-binding; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1207
FT /note="Disease resistance protein RPP2B"
FT /id="PRO_0000444557"
FT DOMAIN 15..180
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 201..445
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 607..630
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 653..676
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 677..699
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 720..743
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 744..767
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 769..791
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 792..815
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 840..862
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 863..886
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT ACT_SITE 89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT VAR_SEQ 445..481
FT /note="Missing (in isoform 2)"
FT /id="VSP_059609"
FT MUTAGEN 121
FT /note="G->E: Enhanced susceptibility to Hyaloperonospora
FT parasitica."
FT /evidence="ECO:0000269|PubMed:15165183"
FT MUTAGEN 726
FT /note="L->F: Enhanced susceptibility to Hyaloperonospora
FT parasitica."
FT /evidence="ECO:0000269|PubMed:15165183"
FT MUTAGEN 944
FT /note="T->M: Enhanced susceptibility to Hyaloperonospora
FT parasitica."
FT /evidence="ECO:0000269|PubMed:15165183"
FT MUTAGEN 955
FT /note="E->K: Enhanced susceptibility to Hyaloperonospora
FT parasitica."
FT /evidence="ECO:0000269|PubMed:15165183"
SQ SEQUENCE 1207 AA; 138314 MW; 55A630F0DAB9CC58 CRC64;
MAFASSSSSI VLSKCEFDVF VSFRGADTRH DFTSHLVKYL RGKGIDVFSD AKLRGGEYIS
LLFDRIEQSK MSIVVFSEDY ANSWWCLEEV GKIMQRRKEF NHGVLPIFYK VSKSDVSNQT
GSFEAVFQSP TKIFNGDEQK IEELKVALKT ASNIRGFVYP ENSSEPDFLD EIVKNTFRML
NELSPCVIPD DLPGIESRSK ELEKLLMFDN DECVRVVGVL GMTGIGKTTV ADIVYKQNFQ
RFDGYEFLED IEDNSKRYGL PYLYQKLLHK LLDGENVDVR AQGRPENFLR NKKLFIVLDN
VTEEKQIEYL IGKKNVYRQG SRIVIITRDK KLLQKNADAT YVVPRLNDRE AMELFCLQVF
GNHYPTEEFV DLSNDFVCYA KGLPLALKLL GKGLLTHDIN YWKKKLEFLQ VNPDKELQKE
LKSSYKALDD DQKSVFLDIA CFFRSEKADF VSSILKSDDI DAKDVMRELE EKCLVTISYD
RIEMHDLLHA MGKEIGKEKS IRKAGERRRL WNHKDIRDIL EHNTGTECVR GIFLNMSEVR
RIKLFPAAFT MLSKLKFLKF HSSHCSQWCD NDHIFQCSKV PDHFPDELVY LHWQGYPYDC
LPSDFDPKEL VDLSLRYSHI KQLWEDEKNT ESLRWVDLGQ SKDLLNLSGL SRAKNLERLD
LEGCTSLDLL GSVKQMNELI YLNLRDCTSL ESLPKGFKIK SLKTLILSGC LKLKDFHIIS
ESIESLHLEG TAIERVVEHI ESLHSLILLN LKNCEKLKYL PNDLYKLKSL QELVLSGCSA
LESLPPIKEK MECLEILLMD GTSIKQTPEM SCLSNLKICS FCRPVIDDST GLVVLPFSGN
SFLSDLYLTN CNIDKLPDKF SSLRSLRCLC LSRNNIETLP ESIEKLYSLL LLDLKHCCRL
KSLPLLPSNL QYLDAHGCGS LENVSKPLTI PLVTERMHTT FIFTDCFKLN QAEKEDIVAQ
AQLKSQLLAR TSRHHNHKGL LLDPLVAVCF PGHDIPSWFS HQKMGSLIET DLLPHWCNSK
FIGASLCVVV TFKDHEGHHA NRLSVRCKSK FKSQNGQFIS FSFCLGGWNE SCGSSCHEPR
KLGSDHVFIS YNNCNVPVFK WSEETNEGNR CHPTSASFEF YLTDETERKL ECCEILRCGM
NFLYARDEND RKFQGIRVTD TVERTSSEAL VTIRGQSHSR IEERRYGRIR DEIMDMTGSS
MIGGPES
