RPS6R_ARATH
ID RPS6R_ARATH Reviewed; 1127 AA.
AC P0DKH6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Disease resistance protein RPS6 {ECO:0000303|PubMed:19525323};
DE EC=3.2.2.6 {ECO:0000255|PROSITE-ProRule:PRU00204};
DE AltName: Full=Resistance to Pseudomonas syringae 6 {ECO:0000303|PubMed:19525323};
GN Name=RPS6 {ECO:0000303|PubMed:19525323};
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 [MRNA], FUNCTION, ALTERNATIVE SPLICING, AND MUTAGENESIS
RP OF GLY-220 AND HIS-490.
RC STRAIN=cv. RLD;
RX PubMed=19525323; DOI=10.1104/pp.109.139238;
RA Kim S.H., Kwon S.I., Saha D., Anyanwu N.C., Gassmann W.;
RT "Resistance to the Pseudomonas syringae effector HopA1 is governed by the
RT TIR-NBS-LRR protein RPS6 and is enhanced by mutations in SRFR1.";
RL Plant Physiol. 150:1723-1732(2009).
RN [2]
RP INTERACTION WITH EDS1.
RX PubMed=22158819; DOI=10.1126/science.1211592;
RA Bhattacharjee S., Halane M.K., Kim S.H., Gassmann W.;
RT "Pathogen effectors target Arabidopsis EDS1 and alter its interactions with
RT immune regulators.";
RL Science 334:1405-1408(2011).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the hopA1 type III effector avirulence protein from Pseudomonas
CC syringae. Resistance proteins guard the plant against pathogens that
CC contain an appropriate avirulence protein via an indirect interaction
CC with this avirulence protein. That triggers a defense system including
CC the hypersensitive response, which restricts the pathogen growth.
CC {ECO:0000269|PubMed:19525323}.
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 -!- SUBUNIT: Interacts with EDS1. {ECO:0000269|PubMed:22158819}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.
CC {ECO:0000269|PubMed:19525323};
CC Name=1;
CC IsoId=P0DKH6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000305|PubMed:19525323}.
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 -!- MISCELLANEOUS: Ecotype cv. Columbia does not respond with a
CC hypersensitive response to hopA1. {ECO:0000305|PubMed:19525323}.
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DR AlphaFoldDB; P0DKH6; -.
DR SMR; P0DKH6; -.
DR ExpressionAtlas; P0DKH6; baseline and differential.
DR GO; GO:0043531; F:ADP binding; 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; 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; 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; 3.
DR Pfam; PF07725; LRR_3; 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; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Hydrolase; Leucine-rich repeat; NAD;
KW Plant defense; Repeat.
FT CHAIN 1..1127
FT /note="Disease resistance protein RPS6"
FT /id="PRO_0000431369"
FT DOMAIN 12..176
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REPEAT 197..221
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 540..563
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 587..609
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 610..632
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 633..656
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 658..679
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 680..704
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 766..790
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 791..813
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 814..834
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 835..857
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT ACT_SITE 87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O23530"
FT MUTAGEN 220
FT /note="G->D: In rps6-2; loss of resistance."
FT /evidence="ECO:0000269|PubMed:19525323"
FT MUTAGEN 490
FT /note="H->R: In rps6-1; loss of resistance."
FT /evidence="ECO:0000269|PubMed:19525323"
SQ SEQUENCE 1127 AA; 128230 MW; 5AB3D5484CDDB21E CRC64;
MASSSSSSSR NWSYHVFPSF SGEDVRNTFL SHFLKELDRK LIISFKDNEI ERSQSLDPEL
KHGIRNSRIA VVVFSKTYAS SSWCLNELLE IVKCKKEFGQ LVIPIFYNLD PSHVRKQTGD
FGKIFEKTCR NKTVDEKIRW KEALTDVANI LGYHIVTWDN EASMIEEIAN DILGKMNISP
SNDFEDLVGI EDHITKMSSL LHLESEEVRM VGIWGPSGIG KTTISRALFS RLSCQFQSSV
FIDKVFISKS MEVYSGANLV DYNMKLHLQR AFLAEIFDKK DIKIHVGAME KMVKHRKALI
VIDDLDDQDV LDALAGQTQW FGSGSRIIVV TENKHFLRAN RIDHIYKVCL PSNALALEMF
CRSAFKKNSP PDDFLELSSE VALRAGNLPL GLNVLGSNLR GINKGYWIDM LPRLQGLDGK
IGKTLRVSYD GLNNRKDEAI FRHIACIFNG EKVSDIKLLL ANSNLDVNIG LKNLVDRSLI
CERFNTLEMH SLLQELGKEI VRTESNQPGE REFLVDLKDI CDVLEHNTGT KKVLGITLDI
DETDELHIHE SSFKGMHNLL FLKIYTKKLD QKKKVRWHLP ERFDYLPSRL RLLRFDRYPS
KCLPSNFHPE NLVKLQMQQS KLEKLWDGVH SLAGLRNMDL RGSRNLKEIP DLSMATNLET
LKLSSCSSLV ELPSSIQYLN KLNDLDMSYC DHLETIPSGV NLKSLDRLNL SGCSRLKSFL
DIPTNISWLD IGQTADIPSN LRLQNLDELI LCERVQLRTP LMTMLSPTLT RLTFSNNPSF
VEVPSSIQNL YQLEHLEIMN CRNLVTLPTG INLDSLISLD LSHCSQLKTF PDISTNISDL
NLSYTAIEEV PLSIEKLSLL CYLDMNGCSN LLCVSPNISK LKHLERADFS DCVELTEASW
NGSSSEMVKL LPADNFSTVK LNFINCFKLD LTALIQNQTF FMQLILTGEE VPSYFTHRTS
GDSISLPHIS VCQSFFSFRG CTVIDVDSFS TISVSFDIEV CCRFIDRFGN HFDSTDFPGY
FITTKLGGHL VVFDCYFPFN EEFTTFLDGQ FNYDHVDIQF RLTNDNSQLK LKGCGILLSE
DVPSLDNRPC SPNILPGVCE DSALERRSFR TKMRMMRMRL LKKLLNR
