RLP30_ARATH
ID RLP30_ARATH Reviewed; 786 AA.
AC Q9MA83;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Receptor-like protein 30 {ECO:0000303|PubMed:18434605};
DE Short=AtRLP30 {ECO:0000303|PubMed:18434605};
DE Flags: Precursor;
GN Name=RLP30 {ECO:0000303|PubMed:18434605};
GN OrderedLocusNames=At3g05360 {ECO:0000312|Araport:AT3G05360};
GN ORFNames=T12H1.33 {ECO:0000312|EMBL:AAF27042.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY.
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY MAMPS,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=24104566; DOI=10.1105/tpc.113.117010;
RA Zhang W., Fraiture M., Kolb D., Loeffelhardt B., Desaki Y., Boutrot F.F.,
RA Toer M., Zipfel C., Gust A.A., Brunner F.;
RT "Arabidopsis receptor-like protein30 and receptor-like kinase suppressor of
RT BIR1-1/EVERSHED mediate innate immunity to necrotrophic fungi.";
RL Plant Cell 25:4227-4241(2013).
RN [7]
RP REVIEW.
RX PubMed=25064074; DOI=10.1016/j.pbi.2014.07.007;
RA Gust A.A., Felix G.;
RT "Receptor like proteins associate with SOBIR1-type of adaptors to form
RT bimolecular receptor kinases.";
RL Curr. Opin. Plant Biol. 21:104-111(2014).
RN [8]
RP INDUCTION BY FUSARIUM OXYSPORUM.
RC STRAIN=cv. Columbia;
RX PubMed=24283937; DOI=10.1094/mpmi-06-13-0160-r;
RA Gupta K.J., Mur L.A., Brotman Y.;
RT "Trichoderma asperelloides suppresses nitric oxide generation elicited by
RT Fusarium oxysporum in Arabidopsis roots.";
RL Mol. Plant Microbe Interact. 27:307-314(2014).
RN [9]
RP INDUCTION BY NACL AND MANNITOL.
RX PubMed=27099374; DOI=10.1093/jxb/erw152;
RA Wu J., Liu Z., Zhang Z., Lv Y., Yang N., Zhang G., Wu M., Lv S., Pan L.,
RA Joosten M.H., Wang G.;
RT "Transcriptional regulation of receptor-like protein genes by environmental
RT stresses and hormones and their overexpression activities in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 67:3339-3351(2016).
CC -!- FUNCTION: Receptor for microbe-associated molecular patterns (MAMPs)
CC that induces a BAK1-dependent basal immune response to necrotrophic
CC fungi (e.g. S.sclerotiorum) in the presence of MAMPs (e.g. flg22 and
CC SCLEROTINIA CULTURE FILTRATE ELICITOR1 (SCFE1) from the necrotrophic
CC fungal pathogen S. sclerotiorum). Functionality seems to depend on the
CC presence of the receptor kinase SOBIR1 as an adapter protein
CC (PubMed:24104566). Required for full non-host resistance to bacterial
CC pathogens (e.g. P.syringae pv phaseolicola) (PubMed:18434605).
CC {ECO:0000269|PubMed:18434605, ECO:0000269|PubMed:24104566}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18434605};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- INDUCTION: Induced by microbe-associated molecular patterns (MAMPs)
CC such as LPS, HrpZ, flg22 and oomycete-(NPP1) (PubMed:18434605).
CC Accumulates upon infection by the soil-borne necrotrophic pathogen
CC F.oxysporum f. sp. lentis and associated with nitric oxide (NO)
CC production; this induction is prevented by the plant growth promoting
CC saprophytic fungus T.asperelloides (PubMed:24283937). Induced by NaCl
CC and mannitol (PubMed:27099374). {ECO:0000269|PubMed:18434605,
CC ECO:0000269|PubMed:24283937, ECO:0000269|PubMed:27099374}.
CC -!- DISRUPTION PHENOTYPE: Reduced basal defense leading to an increased
CC susceptibility to the non-host bacteria such as P.syringae pv
CC phaseolicola (Psp 1448A) (PubMed:18434605). Increased susceptibility to
CC S.sclerotiorum strain 1980 and to the related fungus B.cinerea.
CC Impaired SCLEROTINIA CULTURE FILTRATE ELICITOR1- (SCFE1) and flg22-
CC dependent ethylene production (PubMed:24104566).
CC {ECO:0000269|PubMed:18434605, ECO:0000269|PubMed:24104566}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
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DR EMBL; AC009177; AAF27042.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74225.1; -; Genomic_DNA.
DR EMBL; AY091056; AAM13877.1; -; mRNA.
DR EMBL; AY117362; AAM51437.1; -; mRNA.
DR RefSeq; NP_187187.1; NM_111409.3.
DR AlphaFoldDB; Q9MA83; -.
DR SMR; Q9MA83; -.
DR IntAct; Q9MA83; 49.
DR STRING; 3702.AT3G05360.1; -.
DR PaxDb; Q9MA83; -.
DR PRIDE; Q9MA83; -.
DR ProteomicsDB; 228106; -.
DR EnsemblPlants; AT3G05360.1; AT3G05360.1; AT3G05360.
DR GeneID; 819700; -.
DR Gramene; AT3G05360.1; AT3G05360.1; AT3G05360.
DR KEGG; ath:AT3G05360; -.
DR Araport; AT3G05360; -.
DR TAIR; locus:2096339; AT3G05360.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_3_1; -.
DR InParanoid; Q9MA83; -.
DR OMA; NIENNHI; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9MA83; -.
DR PRO; PR:Q9MA83; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MA83; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0032491; P:detection of molecule of fungal origin; IMP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0010555; P:response to mannitol; IMP:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IEP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
DR GO; GO:0002240; P:response to molecule of oomycetes origin; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR045273; RLP23-like.
DR PANTHER; PTHR27004; PTHR27004; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR PROSITE; PS51450; LRR; 11.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane; Plant defense;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..786
FT /note="Receptor-like protein 30"
FT /id="PRO_0000436182"
FT TOPO_DOM 31..739
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..786
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 110..133
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 134..158
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 159..181
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 183..204
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 207..231
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 233..255
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 257..279
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 280..304
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 305..328
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 329..352
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 354..375
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 376..399
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 400..423
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 425..447
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 448..472
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 474..496
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 497..524
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 526..546
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 596..621
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 622..645
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 646..669
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 671..694
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 786 AA; 87527 MW; 6C078E0DE03E3968 CRC64;
MIPSQSNSFS GSVITLYFFL LGSLVLRTLA SSRLHYCRHD QRDALLEFKH EFPVSESKPS
PSLSSWNKTS DCCFWEGVTC DDESGEVVSL DLSYVLLNNS LKPTSGLFKL QQLQNLTLSD
CHLYGEVTSS LGNLSRLTHL DLSSNQLTGE VLASVSKLNQ LRDLLLSENS FSGNIPTSFT
NLTKLSSLDI SSNQFTLENF SFILPNLTSL SSLNVASNHF KSTLPSDMSG LHNLKYFDVR
ENSFVGTFPT SLFTIPSLQI VYLEGNQFMG PIKFGNISSS SRLWDLNLAD NKFDGPIPEY
ISEIHSLIVL DLSHNNLVGP IPTSISKLVN LQHLSLSNNT LEGEVPGCLW GLMTVTLSHN
SFNSFGKSSS GALDGESMQE LDLGSNSLGG PFPHWICKQR FLKYLDLSNN LFNGSIPPCL
KNSTYWLKGL VLRNNSFSGF LPDVFVNASM LLSLDVSYNR LEGKLPKSLI NCTGMELLNV
GSNIIKDTFP SWLVSLPSLR VLILRSNAFY GSLYYDHISF GFQHLRLIDI SQNGFSGTLS
PLYFSNWREM VTSVLEENGS NIGTEDWYMG EKGPEFSHSN SMTMIYKGVE TDFLRIPYFF
RAIDFSGNRF FGNIPESVGL LKELRLLNLS GNSFTSNIPQ SLANLTNLET LDLSRNQLSG
HIPRDLGSLS FLSTMNFSHN LLEGPVPLGT QFQSQHCSTF MDNLRLYGLE KICGKAHAPS
STPLESEEFS EPEEQVINWI AAAIAYGPGV FCGLVIGHIF FTAHKHEWFM EKFHRNKRRV
VTTSAR
