RPM1_ARATH
ID RPM1_ARATH Reviewed; 926 AA.
AC Q39214;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Disease resistance protein RPM1 {ECO:0000303|PubMed:7638602};
DE AltName: Full=Resistance to Pseudomonas syringae protein 3 {ECO:0000303|PubMed:9861059};
DE AltName: Full=Resistance to Pseudomonas syringae pv. Maculicola protein 1 {ECO:0000303|PubMed:7638602};
GN Name=RPM1 {ECO:0000303|PubMed:7638602};
GN Synonyms=RPS3 {ECO:0000303|PubMed:9861059};
GN OrderedLocusNames=At3g07040 {ECO:0000312|Araport:AT3G07040};
GN ORFNames=F17A9.20 {ECO:0000312|EMBL:AAF27008.1};
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 [GENOMIC DNA], AND MUTANTS RPS3-2 AND RPS3-4.
RC STRAIN=cv. Columbia;
RX PubMed=7638602; DOI=10.1126/science.7638602;
RA Grant M.R., Godiard L., Straube E., Ashfield T., Lewald J., Stattler A.,
RA Innes R.W., Dangl J.L.;
RT "Structure of the Arabidopsis RPM1 gene enabling dual specificity disease
RT resistance.";
RL Science 269:843-846(1995).
RN [2]
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 [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEGRADATION.
RX PubMed=9861059; DOI=10.1073/pnas.95.26.15849;
RA Boyes D.C., Nam J., Dangl J.L.;
RT "The Arabidopsis thaliana RPM1 disease resistance gene product is a
RT peripheral plasma membrane protein that is degraded coincident with the
RT hypersensitive response.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15849-15854(1998).
RN [5]
RP MUTAGENESIS OF SER-43; PRO-105; GLY-174; LEU-186; GLY-203; GLY-205;
RP ALA-211; VAL-219; GLU-247; VAL-269; LEU-272; THR-290; LEU-301; GLY-307;
RP THR-313; GLY-325; GLU-340; LEU-344; ALA-379; GLY-384; GLU-395; SER-439;
RP PRO-442; PRO-464; GLY-467; GLU-471; ALA-474; PRO-494; ARG-497; PRO-498;
RP SER-515; PRO-620; SER-738; GLY-766; LEU-778; LEU-781; ARG-787; ASN-812;
RP LEU-852 AND LEU-924.
RX PubMed=11884685; DOI=10.1105/tpc.010393;
RA Tornero P., Chao R.A., Luthin W.N., Goff S.A., Dangl J.L.;
RT "Large-scale structure-function analysis of the Arabidopsis RPM1 disease
RT resistance protein.";
RL Plant Cell 14:435-450(2002).
RN [6]
RP INTERACTION WITH TIP49A.
RX PubMed=12062092; DOI=10.1016/s1534-5807(02)00174-0;
RA Holt B.F. III, Boyes D.C., Ellerstroem M., Siefers N., Wiig A.,
RA Kauffman S., Grant M.R., Dangl J.L.;
RT "An evolutionarily conserved mediator of plant disease resistance gene
RT function is required for normal Arabidopsis development.";
RL Dev. Cell 2:807-817(2002).
RN [7]
RP INTERACTION WITH RIN4.
RX PubMed=11955429; DOI=10.1016/s0092-8674(02)00661-x;
RA Mackey D., Holt B.F. III, Wiig A., Dangl J.L.;
RT "RIN4 interacts with Pseudomonas syringae type III effector molecules and
RT is required for RPM1-mediated resistance in Arabidopsis.";
RL Cell 108:743-754(2002).
RN [8]
RP INTERACTION WITH RIN13.
RC STRAIN=cv. Col-5, and cv. Columbia;
RX PubMed=15722472; DOI=10.1105/tpc.104.028720;
RA Al-Daoude A., de Torres Zabala M., Ko J.-H., Grant M.;
RT "RIN13 is a positive regulator of the plant disease resistance protein
RT RPM1.";
RL Plant Cell 17:1016-1028(2005).
RN [9]
RP INTERACTION WITH RIN2 AND RIN3.
RX PubMed=16212605; DOI=10.1111/j.1365-313x.2005.02525.x;
RA Kawasaki T., Nam J., Boyes D.C., Holt B.F. III, Hubert D.A., Wiig A.,
RA Dangl J.L.;
RT "A duplicated pair of Arabidopsis RING-finger E3 ligases contribute to the
RT RPM1- and RPS2-mediated hypersensitive response.";
RL Plant J. 44:258-270(2005).
RN [10]
RP INTERACTION WITH MORC1/CRT1.
RX PubMed=20332379; DOI=10.1105/tpc.109.071662;
RA Kang H.-G., Oh C.-S., Sato M., Katagiri F., Glazebrook J., Takahashi H.,
RA Kachroo P., Martin G.B., Klessig D.F.;
RT "Endosome-associated CRT1 functions early in resistance gene-mediated
RT defense signaling in Arabidopsis and tobacco.";
RL Plant Cell 22:918-936(2010).
CC -!- FUNCTION: Disease resistance (R) protein that specifically recognizes
CC the AvrRpm1 type III effector avirulence protein from Pseudomonas
CC syringae (PubMed:9861059). Resistance proteins guard the plant against
CC pathogens that contain an appropriate avirulence protein via an
CC indirect interaction with this avirulence protein (PubMed:9861059).
CC That triggers a defense system including the hypersensitive response
CC (HR), which restricts the pathogen growth (PubMed:9861059). Acts via
CC its interaction with RIN4, and probably triggers the plant resistance
CC when RIN4 is phosphorylated by AvrRpm1. It is then degraded at the
CC onset of the hypersensitive response (PubMed:9861059).
CC {ECO:0000269|PubMed:9861059}.
CC -!- SUBUNIT: Interacts directly with RIN4 via its N-terminal region.
CC Interacts (via N-terminus) with RIN2 and RIN3 (via C-terminus).
CC Interacts with TIP49A, a protein known to interact with the TATA
CC binding protein complex (TBP) (PubMed:11955429, PubMed:12062092,
CC PubMed:16212605). Binds to MORC1/CRT1 (PubMed:20332379). Interacts, via
CC its NB-ARC domain, with RIN13 (PubMed:15722472).
CC {ECO:0000269|PubMed:11955429, ECO:0000269|PubMed:12062092,
CC ECO:0000269|PubMed:15722472, ECO:0000269|PubMed:16212605,
CC ECO:0000269|PubMed:20332379}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:9861059};
CC Peripheral membrane protein {ECO:0000269|PubMed:9861059}. Cell membrane
CC {ECO:0000269|PubMed:9861059}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9861059}.
CC -!- DOMAIN: The LRR repeats probably act as specificity determinant of
CC pathogen recognition.
CC -!- SIMILARITY: Belongs to the disease resistance 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; X87851; CAA61131.1; -; Genomic_DNA.
DR EMBL; AC016827; AAF27008.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74492.1; -; Genomic_DNA.
DR PIR; A57072; A57072.
DR RefSeq; NP_187360.1; NM_111584.3.
DR AlphaFoldDB; Q39214; -.
DR SMR; Q39214; -.
DR BioGRID; 5224; 7.
DR STRING; 3702.AT3G07040.1; -.
DR iPTMnet; Q39214; -.
DR PaxDb; Q39214; -.
DR PRIDE; Q39214; -.
DR ProteomicsDB; 228192; -.
DR EnsemblPlants; AT3G07040.1; AT3G07040.1; AT3G07040.
DR GeneID; 819889; -.
DR Gramene; AT3G07040.1; AT3G07040.1; AT3G07040.
DR KEGG; ath:AT3G07040; -.
DR Araport; AT3G07040; -.
DR TAIR; locus:2077572; AT3G07040.
DR eggNOG; KOG4658; Eukaryota.
DR HOGENOM; CLU_000837_25_4_1; -.
DR InParanoid; Q39214; -.
DR OMA; MWARHSI; -.
DR OrthoDB; 176572at2759; -.
DR PhylomeDB; Q39214; -.
DR PRO; PR:Q39214; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39214; baseline and differential.
DR Genevisible; Q39214; AT.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:CACAO.
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:0000166; F:nucleotide binding; ISS:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IDA:TAIR.
DR CDD; cd14798; RX-CC_like; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.8.430; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR042197; Apaf_helical.
DR InterPro; IPR044974; Disease_R_plants.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002182; NB-ARC.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038005; RX-like_CC.
DR InterPro; IPR041118; Rx_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR23155; PTHR23155; 1.
DR Pfam; PF00931; NB-ARC; 1.
DR Pfam; PF18052; Rx_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hypersensitive response; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Plant defense; Reference proteome; Repeat.
FT CHAIN 1..926
FT /note="Disease resistance protein RPM1"
FT /id="PRO_0000212717"
FT DOMAIN 153..467
FT /note="NB-ARC"
FT /evidence="ECO:0000255"
FT REPEAT 561..580
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 581..603
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 605..625
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 626..649
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 686..707
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 708..731
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 756..777
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 778..804
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 825..836
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 837..859
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 876..900
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REGION 10..45
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT BINDING 200..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT MUTAGEN 43
FT /note="S->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 105
FT /note="P->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 174
FT /note="G->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 186
FT /note="L->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 203
FT /note="G->D,S: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 205
FT /note="G->R,E: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 211
FT /note="A->V: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 219
FT /note="V->M: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 247
FT /note="E->K: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 269
FT /note="V->M: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 272
FT /note="L->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 290
FT /note="T->I: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 301
FT /note="L->F: In rps3-2; loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 307
FT /note="G->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 313
FT /note="T->I: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 325
FT /note="G->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 340
FT /note="E->K: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 341
FT /note="A->V: Loss of function."
FT MUTAGEN 344
FT /note="L->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 379
FT /note="A->V: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 384
FT /note="G->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 395
FT /note="E->K: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 439
FT /note="S->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 442
FT /note="P->L: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 464
FT /note="P->L: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 467
FT /note="G->R: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 471
FT /note="E->K: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 474
FT /note="A->T: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 494
FT /note="P->L: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 497
FT /note="R->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 498
FT /note="P->L,S: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 515
FT /note="S->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 620
FT /note="P->S,L: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 738
FT /note="S->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 766
FT /note="G->E: In rps3-4; loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 778
FT /note="L->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 781
FT /note="L->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 787
FT /note="R->H: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 812
FT /note="N->I: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 852
FT /note="L->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
FT MUTAGEN 924
FT /note="L->F: Loss of function."
FT /evidence="ECO:0000269|PubMed:11884685"
SQ SEQUENCE 926 AA; 106883 MW; E2B2D6613CB0FA0D CRC64;
MASATVDFGI GRILSVLENE TLLLSGVHGE IDKMKKELLI MKSFLEDTHK HGGNGSTTTT
TQLFQTFVAN TRDLAYQIED ILDEFGYHIH GYRSCAKIWR AFHFPRYMWA RHSIAQKLGM
VNVMIQSISD SMKRYYHSEN YQAALLPPID DGDAKWVNNI SESSLFFSEN SLVGIDAPKG
KLIGRLLSPE PQRIVVAVVG MGGSGKTTLS ANIFKSQSVR RHFESYAWVT ISKSYVIEDV
FRTMIKEFYK EADTQIPAEL YSLGYRELVE KLVEYLQSKR YIVVLDDVWT TGLWREISIA
LPDGIYGSRV MMTTRDMNVA SFPYGIGSTK HEIELLKEDE AWVLFSNKAF PASLEQCRTQ
NLEPIARKLV ERCQGLPLAI ASLGSMMSTK KFESEWKKVY STLNWELNNN HELKIVRSIM
FLSFNDLPYP LKRCFLYCSL FPVNYRMKRK RLIRMWMAQR FVEPIRGVKA EEVADSYLNE
LVYRNMLQVI LWNPFGRPKA FKMHDVIWEI ALSVSKLERF CDVYNDDSDG DDAAETMENY
GSRHLCIQKE MTPDSIRATN LHSLLVCSSA KHKMELLPSL NLLRALDLED SSISKLPDCL
VTMFNLKYLN LSKTQVKELP KNFHKLVNLE TLNTKHSKIE ELPLGMWKLK KLRYLITFRR
NEGHDSNWNY VLGTRVVPKI WQLKDLQVMD CFNAEDELIK NLGCMTQLTR ISLVMVRREH
GRDLCDSLNK IKRIRFLSLT SIDEEEPLEI DDLIATASIE KLFLAGKLER VPSWFNTLQN
LTYLGLRGSQ LQENAILSIQ TLPRLVWLSF YNAYMGPRLR FAQGFQNLKI LEIVQMKHLT
EVVIEDGAMF ELQKLYVRAC RGLEYVPRGI ENLINLQELH LIHVSNQLVE RIRGEGSVDR
SRVKHIPAIK HYFRTDNGSF YVSLSS
