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RPP2D_ARATH
ID   RPP2D_ARATH             Reviewed;        1189 AA.
AC   O49471; A0A1P8B4W0;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 2.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Probable disease resistance protein At4g19530 {ECO:0000305|PubMed:15165183};
DE            EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
GN   OrderedLocusNames=At4g19530 {ECO:0000312|Araport:AT4G19530};
GN   ORFNames=F24J7.90 {ECO:0000312|EMBL:CAA16930.1};
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   IDENTIFICATION, AND 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).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
CC   -!- FUNCTION: Probable disease resistance protein.
CC       {ECO:0000303|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=O49471-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O49471-2; Sequence=VSP_059610;
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   -!- 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; CAA16930.1; -; Genomic_DNA.
DR   EMBL; AL161551; CAB78955.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84195.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66629.1; -; Genomic_DNA.
DR   PIR; T06146; T06146.
DR   RefSeq; NP_001328514.1; NM_001341356.1. [O49471-1]
DR   RefSeq; NP_193688.1; NM_118073.2. [O49471-2]
DR   AlphaFoldDB; O49471; -.
DR   SMR; O49471; -.
DR   STRING; 3702.AT4G19530.1; -.
DR   PaxDb; O49471; -.
DR   PRIDE; O49471; -.
DR   ProteomicsDB; 228234; -. [O49471-1]
DR   EnsemblPlants; AT4G19530.1; AT4G19530.1; AT4G19530. [O49471-2]
DR   EnsemblPlants; AT4G19530.2; AT4G19530.2; AT4G19530. [O49471-1]
DR   GeneID; 827695; -.
DR   Gramene; AT4G19530.1; AT4G19530.1; AT4G19530. [O49471-2]
DR   Gramene; AT4G19530.2; AT4G19530.2; AT4G19530. [O49471-1]
DR   KEGG; ath:AT4G19530; -.
DR   Araport; AT4G19530; -.
DR   TAIR; locus:2122985; AT4G19530.
DR   eggNOG; ENOG502SI7S; Eukaryota.
DR   HOGENOM; CLU_001561_0_3_1; -.
DR   InParanoid; O49471; -.
DR   OMA; ECEPKEN; -.
DR   OrthoDB; 86802at2759; -.
DR   PhylomeDB; O49471; -.
DR   PRO; PR:O49471; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O49471; 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; IEP:TAIR.
DR   GO; GO:0002758; P:innate immune response-activating signal transduction; IDA:TAIR.
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; 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; PF20160; C-JID; 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   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..1189
FT                   /note="Probable disease resistance protein At4g19530"
FT                   /id="PRO_0000444559"
FT   DOMAIN          13..176
FT                   /note="TIR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   DOMAIN          225..478
FT                   /note="NB-ARC"
FT                   /evidence="ECO:0000255"
FT   REPEAT          641..664
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          666..685
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          698..721
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          733..754
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          755..777
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          779..800
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          801..825
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          826..849
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          850..868
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REGION          1134..1189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1172
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT   VAR_SEQ         938..959
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_059610"
SQ   SEQUENCE   1189 AA;  135143 MW;  761FC8822C015B76 CRC64;
     MATSSSVVSS VPQQHQVFLN FRGDELRNNF VSHLDKALRG KQINVFIDEA VEKGENLDNL
     FKEIEKSRIA LAIISQKYTE SKWCLNELVK MKELEGKLVT IPIFYNVEPA TVRYQKEAFG
     AALTKTQEND SDGQMKKWKE ALTYVSLLVG FPFNSKSKEK ETTLIDKIVD AVLQKLSKIS
     SEESTSGSVD QGRGEEVEEA KADKISGLNQ RLKELEEKVA ITGDKRDETR IVEVVGMPGI
     GKSTLLKAFY ETWKTRFLSS ALLQNISELV KAMGLGRLTG MLLKELLPDE NIDEETYEPY
     KEKLLKNTVF IVLDGISDET HIQKLLKDHR KWAKKGSKIV IARRAVTRDL LHEDSMVRYT
     YFVPLLSHRD GLNHFCHYAF RHFAAHQNNK EAFMKESKEF VRYARGHPLI LKLLGEELRE
     KSLSYWEEKL KSLPKSLSQN IRDRVLQVTY DELSQVQKDA FLDIACFRSH DLVYVKSLLD
     SSGPAFSKAT VTIDALKDMF MIYISDSRVE MHDLLYTFAM ELGPEARDDD GRGRHRIWHH
     HNQDNKGRLN RLLKRPGGST SVRSFFLDMY VMKTDVTLGT DYLKNMRNLR YLKFYSSHCP
     QECTPKENIH IPGELELPLE EVRCLHWLNF PKDELPQDFI PKNLVDLKLP YSKIRQIWRE
     EKDAPKLRWV DLNHSSKLEN LSGLSQALNL ERLNLEGCTA LKTLLLGPEN MASLVFLNLK
     GCTGLESLPK INLRSLKTLI LSNCSNLEEF WVISETLYTL YLDGTAIKTL PQDMVKLTSL
     VKLYMKDCEM LVKLPEEFDK LKVLQELVCS GCKRLSSLPD VMKNMQCLQI LLLDGTAITK
     IPHISSLERL CLSRNEKISC LSNDIRLLSQ LKWLDLKYCT KLVSIPELPT NLQCLDANGC
     ESLTTVANPL ATHLPTEQIH STFIFTNCDK LDRTAKEVIT TYAQRKCQML SDALKRWNEG
     FVPEALFSTC FPGCEVPSWF CHEAVGSVLK LNLLPHWNEN RFVGIALCAV VGSLPNCQEQ
     TNSCSVTCTF NIASKDSKKG DPYKISFDRL VGRWNKHGNK LDKKGNKLKK TESDHVFICY
     TRCSNSIKCL QDQHSGTCTP TEAFLEFGVT DKESRLEVLK CGLRLVYASD EPQKTNSDMD
     LSLSSSDSTP TRNGSSNTTT SSGSVSTNTI REEDSNILHE AQSQNGRGL
 
 
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