ID RPP1_ARATH Reviewed; 1194 AA.
AC F4J339; Q9LXN9;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Probable disease resistance protein RPP1 {ECO:0000305};
DE AltName: Full=Probable NAD(+) hydrolase RPP1;
DE EC=3.2.2.6 {ECO:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
DE AltName: Full=Protein RECOGNITION OF PERONOSPORA PARASITICA 1 {ECO:0000305};
GN Name=RPP1 {ECO:0000305};
GN OrderedLocusNames=At3g44480 {ECO:0000312|Araport:AT3G44480};
GN ORFNames=F14L2_30 {ECO:0000312|EMBL:CAB88530.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 INDUCTION.
RX PubMed=20831409; DOI=10.1094/mpmi-01-10-0022;
RA Mohr T.J., Mammarella N.D., Hoff T., Woffenden B.J., Jelesko J.G.,
RA McDowell J.M.;
RT "The Arabidopsis downy mildew resistance gene RPP8 is induced by pathogens
RT and salicylic acid and is regulated by W box cis elements.";
RL Mol. Plant Microbe Interact. 23:1303-1315(2010).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439792; DOI=10.1126/science.aax1911;
RA Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA Dodds P.N., Kobe B.;
RT "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT pathways.";
RL Science 365:793-799(2019).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439793; DOI=10.1126/science.aax1771;
RA Wan L., Essuman K., Anderson R.G., Sasaki Y., Monteiro F., Chung E.H.,
RA Osborne Nishimura E., DiAntonio A., Milbrandt J., Dangl J.L.,
RA Nishimura M.T.;
RT "TIR domains of plant immune receptors are NAD+-cleaving enzymes that
RT promote cell death.";
RL Science 365:799-803(2019).
CC -!- FUNCTION: TIR-NB-LRR receptor-like protein that confers resistance to
CC the pathogen Hyaloperonospora arabidopsis (By similarity). Probably
CC acts as a NAD(+) hydrolase (NADase): in response to activation,
CC catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide;
CC NAD(+) cleavage triggering a defense system that promotes cell death
CC (PubMed:31439792, PubMed:31439793). {ECO:0000250|UniProtKB:F4JNA9,
CC ECO:0000269|PubMed:31439792, ECO:0000269|PubMed:31439793}.
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:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000305|PubMed:31439792, ECO:0000305|PubMed:31439793};
CC -!- INDUCTION: By infection with Hyaloperonospora arabidopsidis isolate
CC Emco5. {ECO:0000269|PubMed:20831409}.
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=CAB88530.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353818; CAB88530.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77906.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64388.1; -; Genomic_DNA.
DR PIR; T48928; T48928.
DR RefSeq; NP_001326419.1; NM_001339143.1.
DR RefSeq; NP_190034.2; NM_114316.3.
DR AlphaFoldDB; F4J339; -.
DR SMR; F4J339; -.
DR STRING; 3702.F4J339; -.
DR iPTMnet; F4J339; -.
DR PaxDb; 3702-AT3G44480-1; -.
DR ProteomicsDB; 226511; -.
DR EnsemblPlants; AT3G44480.1; AT3G44480.1; AT3G44480.
DR EnsemblPlants; AT3G44480.4; AT3G44480.4; AT3G44480.
DR GeneID; 823573; -.
DR Gramene; AT3G44480.1; AT3G44480.1; AT3G44480.
DR Gramene; AT3G44480.4; AT3G44480.4; AT3G44480.
DR KEGG; ath:AT3G44480; -.
DR Araport; AT3G44480; -.
DR TAIR; AT3G44480; RPP1.
DR eggNOG; ENOG502SUNR; Eukaryota.
DR HOGENOM; CLU_001561_0_1_1; -.
DR InParanoid; F4J339; -.
DR PRO; PR:F4J339; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4J339; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140376; F:innate immune receptor activity; EXP:PHI-base.
DR GO; GO:0030275; F:LRR domain binding; ISS:TAIR.
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; TAS:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0002758; P:innate immune response-activating signaling pathway; IMP:PHI-base.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:PHI-base.
DR GO; GO:0002239; P:response to oomycetes; IDA:TAIR.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 1.10.8.430; Helical domain of apoptotic protease-activating factors; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR045344; C-JID.
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:SF411; ADP-RIBOSYL CYCLASE_CYCLIC ADP-RIBOSE HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11017; LEUCINE-RICH REPEAT-CONTAINING PROTEIN; 1.
DR Pfam; PF20160; C-JID; 1.
DR Pfam; PF07725; LRR_3; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF01582; TIR; 1.
DR PRINTS; PR00364; DISEASERSIST.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Leucine-rich repeat; NAD; Nucleotide-binding;
KW Plant defense; Reference proteome; Repeat.
FT CHAIN 1..1194
FT /note="Probable disease resistance protein RPP1"
FT /id="PRO_0000433378"
FT DOMAIN 96..260
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 280..535
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 623..647
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 658..681
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 690..713
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 714..737
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 739..760
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 761..784
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 786..807
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 808..831
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 832..855
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 866..878
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 879..899
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 900..922
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 943..965
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 966..991
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 105..110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:V9M398"
SQ SEQUENCE 1194 AA; 136132 MW; 8A09D6203D35DA1A CRC64;
MGSVMSLGCS KRKATNQDVD SESRKRRKIC STNDAENCRF IQDESSWKHP WSLCANRVIS
VAAVALTNFR FQQDNQESNS SSLSLPSPAT SVSRNWKHDV FPSFHGADVR RTFLSHIMES
FRRKGIDTFI DNNIERSKSI GPELKEAIKG SKIAIVLLSR KYASSSWCLD ELAEIMKCRQ
MVGQIVMTIF YEVDPTDIKK QTGEFGKAFT KTCRGKPKEQ VERWRKALED VATIAGYHSH
SWRNEADMIE KISTDVSNML NSFTPSRDFD GLVGMRAHMD MLEQLLRLDL DEVRMIGIWG
PPGIGKTTIA RFLFNQVSDR FQLSAIMVNI KGCYPRPCFD EYSAQLQLQN QMLSQMINHK
DIMISHLGVA QERLRDKKVF LVLDEVDQLG QLDALAKETR WFGPGSRIII TTEDLGVLKA
HGINHVYKVE YPSNDEAFQI FCMNAFGQKQ PHEGFDEIAW EVTCLAGELP LGLKVLGSAL
RGKSKREWER TLPRLKTSLD GKIGSIIQFS YDVLCDEDKY LFLYIACLFN GESTTKVKEL
LGKFLDVKQG LHLLAQKSLI SFDGERIHMH TLLEQFGRET SRKQFVHHGF TKRQLLVGAR
GICEVLDDDT TDSRRFIGIH LELSNTEEEL NISEKVLERV HDFHFVRIDA SFQPERLQLA
LQDLIYHSPK IRSLNWYGYE SLCLPSTFNP EFLVELDMRS SNLRKLWEGT KQLRNLKWMD
LSYSSYLKEL PNLSTATNLE ELKLRNCSSL VELPSSIEKL TSLQILDLEN CSSLEKLPAI
ENATKLRELK LQNCSSLIEL PLSIGTATNL KQLNISGCSS LVKLPSSIGD ITDLEVFDLS
NCSSLVTLPS SIGNLQNLCK LIMRGCSKLE ALPININLKS LDTLNLTDCS QLKSFPEIST
HISELRLKGT AIKEVPLSIM SWSPLADFQI SYFESLMEFP HAFDIITKLH LSKDIQEVPP
WVKRMSRLRD LSLNNCNNLV SLPQLSDSLD YIYADNCKSL ERLDCCFNNP EIRLYFPKCF
KLNQEARDLI MHTCIDAMFP GTQVPACFIH RATSGDSLKI KLKESPLPTT LRFKACIMLV
KVNEELMSYD QTPMIVDIVI RDEHNDLKEK IYPSIYPSIY PLLTEHIYTF ELDVEEVTST
ELVFEFPQLN KRNWKIGECG ILQRETRSLR RSSSPDLSPE SSRVSSYDHC LRGD
//
