RPP2A_ARATH
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 03-AUG-2022, entry version 81.
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 STRING; 3702.AT4G19500.1; -.
DR PaxDb; F4JT78; -.
DR PRIDE; F4JT78; -.
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; locus:2122955; AT4G19500.
DR HOGENOM; CLU_260879_0_0_1; -.
DR InParanoid; F4JT78; -.
DR OrthoDB; 339372at2759; -.
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: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; 3.40.50.10140; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.80.10.10; -; 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; PTHR11017; 2.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 2.
DR Pfam; PF01582; TIR; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00255; TIR; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52200; SSF52200; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
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
