RLP55_ARATH
ID RLP55_ARATH Reviewed; 425 AA.
AC Q9FK66;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Receptor-like protein 55 {ECO:0000303|PubMed:18434605};
DE Short=AtRLP55 {ECO:0000303|PubMed:18434605};
DE AltName: Full=Protein SUPPRESSOR OF NPR1-1, CONSTITUTIVE 3 {ECO:0000303|PubMed:20841424};
DE Flags: Precursor;
GN Name=RLP55 {ECO:0000303|PubMed:18434605};
GN Synonyms=SNC3 {ECO:0000303|PubMed:20841424};
GN OrderedLocusNames=At5g45770 {ECO:0000312|Araport:AT5G45770};
GN ORFNames=MRA19.20 {ECO:0000312|EMBL:BAB09219.1};
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 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 [4]
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 [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-404.
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. {ECO:0000269|PubMed:20841424}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9SN38};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
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DR EMBL; AB012245; BAB09219.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95295.1; -; Genomic_DNA.
DR RefSeq; NP_199389.1; NM_123944.3.
DR AlphaFoldDB; Q9FK66; -.
DR SMR; Q9FK66; -.
DR IntAct; Q9FK66; 7.
DR STRING; 3702.AT5G45770.1; -.
DR PaxDb; Q9FK66; -.
DR PRIDE; Q9FK66; -.
DR ProteomicsDB; 226917; -.
DR EnsemblPlants; AT5G45770.1; AT5G45770.1; AT5G45770.
DR GeneID; 834616; -.
DR Gramene; AT5G45770.1; AT5G45770.1; AT5G45770.
DR KEGG; ath:AT5G45770; -.
DR Araport; AT5G45770; -.
DR TAIR; locus:2171963; AT5G45770.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_034697_0_0_1; -.
DR InParanoid; Q9FK66; -.
DR OMA; NSELCYN; -.
DR OrthoDB; 1167047at2759; -.
DR PhylomeDB; Q9FK66; -.
DR PRO; PR:Q9FK66; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK66; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13855; LRR_8; 1.
DR PROSITE; PS51450; LRR; 6.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..425
FT /note="Receptor-like protein 55"
FT /evidence="ECO:0000255"
FT /id="PRO_5006751748"
FT TOPO_DOM 26..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 144..169
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 170..193
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 195..216
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 217..240
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 242..264
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 265..287
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 288..313
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REGION 355..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 404
FT /note="G->R: Constitutive activation of defense responses
FT leading to enhanced resistance against Hyaloperonospora
FT arabidopsidis NOCO2. Dwarf morphology."
FT /evidence="ECO:0000269|PubMed:20841424"
SQ SEQUENCE 425 AA; 47174 MW; 3FCF13866B0D8EF1 CRC64;
MKPQQPQPPL LLLLLLPLLL TTVSSYPLNP KQLKALQSLN ISTPTNDPCN NNNNQSSSSS
ITCDDASPYR HITSISFTNC SSTLSLPSKT LKPLSKSLIS LSFTNCPSLS PPYHLPISLH
SFSAVSSFLQ NNRTKLSGLF LARLKNLKTL YISSTPIQTS RRLYVILGNM HKLTSLTISN
SNLTGLIPKS FHSNLRYIDL SNNSLKGSIR ISITRLKNLK SLNLSHNSLS GQIPNKIKSL
TFLKNLSLAS NKLSGTIPNS LSSISELTHL DLSMNQLNGT VPSFFSEMKN LKHLNLADNS
FHGVLPFNES FIKNLNFFEI GRNSELCYNK TVLSSNLKLE GLAPCDKYGF PLWSPSQKEE
SLSGENDYDV EGGNEEKTEN LKTKEEEEEE HKGSNKTLFG LGIGLFSLVF LILFLFYLAK
RCRLI
