RLP51_ARATH
ID RLP51_ARATH Reviewed; 431 AA.
AC Q9SN38;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Receptor-like protein 51 {ECO:0000303|PubMed:18434605};
DE Short=AtRLP51 {ECO:0000303|PubMed:18434605};
DE AltName: Full=Protein PUTATIVE DEVELOPMENTAL ORTHOLOG 1 {ECO:0000303|PubMed:15955925};
DE Short=AtPDO1 {ECO:0000303|PubMed:15955925};
DE AltName: Full=Protein SUPPRESSOR OF NPR1-1, CONSTITUTIVE 2 {ECO:0000303|PubMed:20841424};
DE Flags: Precursor;
GN Name=RLP51 {ECO:0000303|PubMed:18434605};
GN Synonyms=PDO1 {ECO:0000303|PubMed:15955925},
GN SNC2 {ECO:0000303|PubMed:20841424};
GN OrderedLocusNames=At4g18760 {ECO:0000312|Araport:AT4G18760};
GN ORFNames=F28A21.170 {ECO:0000312|EMBL:CAB37461.1};
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [4]
RP INDUCTION BY PSEUDOMONAS FLUORESCENS.
RX PubMed=15305611; DOI=10.1094/mpmi.2004.17.8.895;
RA Verhagen B.W., Glazebrook J., Zhu T., Chang H.S., van Loon L.C.,
RA Pieterse C.M.;
RT "The transcriptome of rhizobacteria-induced systemic resistance in
RT arabidopsis.";
RL Mol. Plant Microbe Interact. 17:895-908(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [6]
RP GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=15955925; DOI=10.1104/pp.104.054452;
RA Fritz-Laylin L.K., Krishnamurthy N., Toer M., Sjoelander K.V., Jones J.D.;
RT "Phylogenomic analysis of the receptor-like proteins of rice and
RT Arabidopsis.";
RL Plant Physiol. 138:611-623(2005).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=18434605; DOI=10.1104/pp.108.119487;
RA Wang G., Ellendorff U., Kemp B., Mansfield J.W., Forsyth A., Mitchell K.,
RA Bastas K., Liu C.-M., Woods-Toer A., Zipfel C., de Wit P.J.G.M.,
RA Jones J.D.G., Toer M., Thomma B.P.H.J.;
RT "A genome-wide functional investigation into the roles of receptor-like
RT proteins in Arabidopsis.";
RL Plant Physiol. 147:503-517(2008).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-108; PRO-137; GLY-204;
RP PRO-277; PRO-402 AND GLY-412, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=20841424; DOI=10.1105/tpc.110.074120;
RA Zhang Y., Yang Y., Fang B., Gannon P., Ding P., Li X., Zhang Y.;
RT "Arabidopsis snc2-1D activates receptor-like protein-mediated immunity
RT transduced through WRKY70.";
RL Plant Cell 22:3153-3163(2010).
CC -!- FUNCTION: Involved in plant defense. Required for basal resistance
CC against P.syringae pv. tomato DC3000. {ECO:0000269|PubMed:20841424}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20841424};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced locally in roots by the nonpathogenic, root-
CC colonizing rhizobacterium P.fluorescens WCS417r.
CC {ECO:0000269|PubMed:15305611}.
CC -!- DISRUPTION PHENOTYPE: In snc2-5 and snc2-8 mutants, impaired basal
CC resistance to P.syringae pv. tomato DC3000 leading to increased
CC susceptibility. {ECO:0000269|PubMed:20841424}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
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DR EMBL; AL035526; CAB37461.1; -; Genomic_DNA.
DR EMBL; AL161549; CAB78878.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84087.1; -; Genomic_DNA.
DR PIR; T04868; T04868.
DR RefSeq; NP_193611.1; NM_117992.2.
DR AlphaFoldDB; Q9SN38; -.
DR SMR; Q9SN38; -.
DR STRING; 3702.AT4G18760.1; -.
DR iPTMnet; Q9SN38; -.
DR SwissPalm; Q9SN38; -.
DR PaxDb; Q9SN38; -.
DR PRIDE; Q9SN38; -.
DR ProteomicsDB; 228162; -.
DR EnsemblPlants; AT4G18760.1; AT4G18760.1; AT4G18760.
DR GeneID; 827610; -.
DR Gramene; AT4G18760.1; AT4G18760.1; AT4G18760.
DR KEGG; ath:AT4G18760; -.
DR Araport; AT4G18760; -.
DR TAIR; locus:2124147; AT4G18760.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_034697_0_0_1; -.
DR InParanoid; Q9SN38; -.
DR OMA; SHGPSKV; -.
DR OrthoDB; 1167047at2759; -.
DR PhylomeDB; Q9SN38; -.
DR PRO; PR:Q9SN38; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SN38; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane; Plant defense;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..431
FT /note="Receptor-like protein 51"
FT /evidence="ECO:0000255"
FT /id="PRO_5005706115"
FT TOPO_DOM 22..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 161..185
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 189..211
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 212..235
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 236..259
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 261..283
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 284..307
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 309..332
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REGION 23..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 108
FT /note="S->F: In snc2-7; reversion of the snc2-1D mutation
FT leading to the suppression of constitutive defense
FT responses and subsequent reduced resistance to
FT H.arabidopsidis NOCO2."
FT /evidence="ECO:0000269|PubMed:20841424"
FT MUTAGEN 137
FT /note="P->S: In snc2-6; reversion of the snc2-1D mutation
FT leading to the suppression of constitutive defense
FT responses and subsequent reduced resistance to
FT H.arabidopsidis NOCO2."
FT /evidence="ECO:0000269|PubMed:20841424"
FT MUTAGEN 204
FT /note="G->R: In snc2-2; reversion of the snc2-1D mutation
FT leading to the suppression of constitutive defense
FT responses and subsequent reduced resistance to
FT H.arabidopsidis NOCO2."
FT /evidence="ECO:0000269|PubMed:20841424"
FT MUTAGEN 277
FT /note="P->S: In snc2-4; reversion of the snc2-1D mutation
FT leading to the suppression of constitutive defense
FT responses and subsequent reduced resistance to
FT H.arabidopsidis NOCO2."
FT /evidence="ECO:0000269|PubMed:20841424"
FT MUTAGEN 402
FT /note="P->L: In snc2-3; reversion of the snc2-1D mutation
FT leading to the suppression of constitutive defense
FT responses and subsequent reduced resistance to
FT H.arabidopsidis NOCO2."
FT /evidence="ECO:0000269|PubMed:20841424"
FT MUTAGEN 412
FT /note="G->R: In snc2-1D; constitutive activation of defense
FT responses leading to enhanced resistance against
FT H.arabidopsidis NOCO2. Dwarf morphology and constitutive
FT defense responses in snc2-1D npr1-1 double mutant, thus
FT suppressing the npr1-1 susceptible phenotype."
FT /evidence="ECO:0000269|PubMed:20841424"
SQ SEQUENCE 431 AA; 46071 MW; 856164A75F332157 CRC64;
MKPPSLPLLL LLLHLSATIS AAPSLSPTPS PTTSPIPPHK PSSSSSPLDP KQLKALESLN
IPTVKDPCNH RPTTKSTSSS VVTCDTSSPF RLVTSISFTN CSTDLSISTT ALRALSPSLT
SLSFLNCPSL SPPPRLPDSL HSFTAVSSFL RRRNGLSGVF LARLVNLTDL TVSSVPVSTS
GLFVILGNMH EIVSLTISHA NLSGNIPKSF HSNLTFIDLS DNLLKGSIPT SITLLSNLKS
LNLSKNTISG DIPDSIGDLI SLKNLSLSSN KLSGPIPDSI SSIPELTHLD LSGNQLNGTI
PRFISKMKYL THLNLANNAF HGVLPFNASF IKNLEVFKIG GNSDLCYNHS VLSSKMKLGI
AQCDKHGLPL SPPPQKEDSN SDYDYGNEDD TSEKKKEEHH GPNKVVLGVA IGLSSLVFLI
IFMILLAKWC G
