ID   RPP2A_ARATH             Reviewed;        1309 AA.
AC   F4JT78; O49468; Q0WNV7;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Disease resistance protein RPP2A {ECO:0000305};
DE            EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
GN   Name=RPP2A {ECO:0000303|PubMed:15165183};
GN   OrderedLocusNames=At4g19500 {ECO:0000312|Araport:AT4G19500};
GN   ORFNames=F24J7.60 {ECO:0000312|EMBL:CAA16927.2};
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].
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.
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).
CC   -!- FUNCTION: Disease resistance protein that cooperates with RPP2B 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   -!- 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=BAF01192.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA16927.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78952.1; 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; CAA16927.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161551; CAB78952.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84190.1; -; Genomic_DNA.
DR   EMBL; AK229329; BAF01192.1; ALT_INIT; mRNA.
DR   PIR; T06143; T06143.
DR   RefSeq; NP_193685.6; NM_118070.7.
DR   AlphaFoldDB; F4JT78; -.
DR   SMR; F4JT78; -.
DR   IntAct; F4JT78; 1.
DR   STRING; 3702.F4JT78; -.
DR   PaxDb; 3702-AT4G19500-1; -.
DR   ProteomicsDB; 228076; -.
DR   EnsemblPlants; AT4G19500.1; AT4G19500.1; AT4G19500.
DR   GeneID; 827691; -.
DR   Gramene; AT4G19500.1; AT4G19500.1; AT4G19500.
DR   KEGG; ath:AT4G19500; -.
DR   Araport; AT4G19500; -.
DR   TAIR; AT4G19500; -.
DR   HOGENOM; CLU_260879_0_0_1; -.
DR   InParanoid; F4JT78; -.
DR   OrthoDB; 692483at2759; -.
DR   PRO; PR:F4JT78; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JT78; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR006936; ALOG_dom.
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   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR11017:SF549; DISEASE RESISTANCE PROTEIN RPP2A; 1.
DR   PANTHER; PTHR11017; LEUCINE-RICH REPEAT-CONTAINING PROTEIN; 1.
DR   Pfam; PF04852; ALOG_dom; 1.
DR   Pfam; PF07725; LRR_3; 1.
DR   Pfam; PF00931; NB-ARC; 2.
DR   Pfam; PF01582; TIR; 2.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00255; TIR; 2.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51697; ALOG; 1.
DR   PROSITE; PS50104; TIR; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Hydrolase; Leucine-rich repeat; NAD;
KW   Nucleotide-binding; Plant defense; Reference proteome; Repeat.
FT   CHAIN           1..1309
FT                   /note="Disease resistance protein RPP2A"
FT                   /id="PRO_0000444556"
FT   DOMAIN          9..173
FT                   /note="TIR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          187..418
FT                   /note="NB-ARC 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          488..585
FT                   /note="ALOG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01033"
FT   DOMAIN          574..737
FT                   /note="TIR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          755..987
FT                   /note="NB-ARC 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1145..1167
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1168..1195
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1214..1237
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1238..1258
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1259..1283
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          1285..1307
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   COILED          1114..1141
FT                   /evidence="ECO:0000303|PubMed:15165183"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
SQ   SEQUENCE   1309 AA;  148976 MW;  8F1875C842B3078C CRC64;
     MAASFCGSRR YDVFPSFSKV DVRRSFLAHL LKELDRRLIN TFTDHGMERN LPIDAELLSA
     IAESRISIVI FSKNYASSTW CLDELVEIHT CYKELAQIVV PVFFNVHPSQ VKKQTGEFGK
     VFGKTCKGKP ENRKLRWMQA LAAVANIAGY DLQNWPDEAV MIEMVADDVS KKLFKSSNDF
     SDIVGIEAHL EAMSSILRLK SEKARMVGIS GPSGIGKTTI AKALFSKLSP QFHLRAFVTY
     KRTNQDDYDM KLCWIEKFLS EILGQKDLKV LDLGAVEQSL MHKKVLIILD DVDDLELLKT
     LVGQTGWFGF GSRIVVITQD RQLLKAHDIN LIYEVAFPSA HLALEIFCQS AFGKIYPPSD
     FRELSVEFAY LAGNLPLDLR VLGLAMKGKH REEWIEMLPR LRNDLDGKFK KTLRNYLPVI
     RKRVSNEEGG REKLKKGNKK LDLDEEFPGG EIYSDEIPSP TSNWKDTDDF DSGDIIPIIA
     DKSTTIIPNR RHSNDDWCSF CEFLRNRIPP LNPFKCSAND VIDFLRTRQV LGSTEALVDR
     LIFSSEAFGI KPEENPFRSQ AVTSYLKAAR DMTREKECIL VFSCHDNLDV DETSFIEAIS
     KELHKQGFIP LTYNLLGREN LDEEMLYGSR VGIMILSSSY VSSRQSLDHL VAVMEHWKTT
     DLVIIPIYFK VRLSDICGLK GRFEAAFLQL HMSLQEDRVQ KWKAAMSEIV SIGGHEWTKG
     SQFILAEEVV RNASLRLYLK SSKNLLGILA LLNHSQSTDV EIMGIWGIAG IGKTSIAREI
     FELHAPHYDF CYFLQDFHLM CQMKRPRQLR EDFISKLFGE EKGLGASDVK PSFMRDWFHK
     KTILLVLDDV SNARDAEAVI GGFGWFSHGH RIILTSRSKQ VLVQCKVKKP YEIQKLSDFE
     SFRLCKQYLD GENPVISELI SCSSGIPLAL KLLVSSVSKQ YITNMKDHLQ SLRKDPPTQI
     QEAFRRSFDG LDENEKNIFL DLACFFRGQS KDYAVLLLDA CGFFTYMGIC ELIDESLISL
     VDNKIEMPIP FQDMGRIIVH EEDEDPCERS RLWDSKDIVD VLTNNSGTEA IEGIFLDASD
     LTCELSPTVF GKMYNLRLLK FYCSTSGNQC KLTLPHGLDT LPDELSLLHW ENYPLVYLPQ
     KFNPVNLVEL NMPYSNMEKL WEGKKNLEKL KNIKLSHSRE LTDILMLSEA LNLEHIDLEG
     CTSLIDVSMS IPCCGKLVSL NMKDCSRLRS LPSMVDLTTL KLLNLSGCSE FEDIQDFAPN
     LEEIYLAGTS IRELPLSIRN LTELVTLDLE NCERLQEMPS LPVEIIRRT
//