RLP42_ARATH
ID RLP42_ARATH Reviewed; 890 AA.
AC Q9LJS0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Receptor-like protein 42 {ECO:0000303|PubMed:18434605};
DE Short=AtRLP42 {ECO:0000303|PubMed:18434605};
DE AltName: Full=Protein RESPONSIVENESS TO BOTRYTIS POLYGALACTURONASES 1 {ECO:0000303|PubMed:24259685};
DE Flags: Precursor;
GN Name=RLP42 {ECO:0000303|PubMed:18434605};
GN Synonyms=RBPG1 {ECO:0000303|PubMed:24259685};
GN OrderedLocusNames=At3g25020 {ECO:0000312|Araport:AT3G25020};
GN ORFNames=K3G3.4 {ECO:0000312|EMBL:BAB01887.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [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 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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH BCPG3.
RC STRAIN=cv. Br-0, and cv. Columbia;
RX PubMed=24259685; DOI=10.1104/pp.113.230698;
RA Zhang L., Kars I., Essenstam B., Liebrand T.W.H., Wagemakers L.,
RA Elberse J., Tagkalaki P., Tjoitang D., van den Ackerveken G.,
RA van Kan J.A.L.;
RT "Fungal endopolygalacturonases are recognized as microbe-associated
RT molecular patterns by the arabidopsis receptor-like protein RESPONSIVENESS
RT TO BOTRYTIS POLYGALACTURONASES1.";
RL Plant Physiol. 164:352-364(2014).
CC -!- FUNCTION: Recognizes fungal (e.g. B.cinerea and A.niger)
CC endopolygalacturonases (PGs, e.g. BcPG3, BcPG2, BcPG4, BcPG6 and AnPGB)
CC and acts as a microbe-associated molecular pattern (MAMP) receptor to
CC mediate defense response against fungi (e.g. B.cinerea) and oomycetes
CC (e.g. H.arabidopsidis). Functionality seems to depend on the presence
CC of the receptor kinase SOBIR1 as an adapter protein.
CC {ECO:0000269|PubMed:24259685}.
CC -!- SUBUNIT: Interacts with BcPG3. {ECO:0000269|PubMed:24259685}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Impaired perception of fungal
CC endopolygalacturonases (e.g. BcPG3) leading to absence of necrosis upon
CC B.cinerea BcPG3, BcPG2, BcPG4, and BcPG6 or A.niger AnPGB treatments.
CC {ECO:0000269|PubMed:24259685}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP000412; BAB01887.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76968.1; -; Genomic_DNA.
DR RefSeq; NP_189138.1; NM_113406.2.
DR AlphaFoldDB; Q9LJS0; -.
DR SMR; Q9LJS0; -.
DR STRING; 3702.AT3G25020.1; -.
DR PaxDb; Q9LJS0; -.
DR PRIDE; Q9LJS0; -.
DR ProteomicsDB; 228007; -.
DR EnsemblPlants; AT3G25020.1; AT3G25020.1; AT3G25020.
DR GeneID; 822093; -.
DR Gramene; AT3G25020.1; AT3G25020.1; AT3G25020.
DR KEGG; ath:AT3G25020; -.
DR Araport; AT3G25020; -.
DR TAIR; locus:2086979; AT3G25020.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_18_3_1; -.
DR InParanoid; Q9LJS0; -.
DR OMA; NCASLEF; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9LJS0; -.
DR PRO; PR:Q9LJS0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:1902288; P:regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; 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; IPR045273; RLP23-like.
DR PANTHER; PTHR27004; PTHR27004; 1.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 7.
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..890
FT /note="Receptor-like protein 42"
FT /evidence="ECO:0000255"
FT /id="PRO_5010847994"
FT TOPO_DOM 22..844
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 866..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 97..121
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 122..143
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 146..169
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 170..195
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 197..219
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 220..244
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 246..267
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 268..291
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 293..316
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 317..339
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 341..363
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 364..389
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 390..411
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 412..436
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 438..461
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 462..485
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 486..505
FT /note="LRR 17; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 506..527
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 528..551
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 553..575
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 577..598
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 599..623
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 626..650
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REPEAT 700..723
FT /note="LRR 24"
FT /evidence="ECO:0000255"
FT REPEAT 724..747
FT /note="LRR 25"
FT /evidence="ECO:0000255"
FT REPEAT 748..771
FT /note="LRR 26"
FT /evidence="ECO:0000255"
FT REPEAT 773..796
FT /note="LRR 27"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 730
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 890 AA; 98439 MW; 5570A724C9EFC013 CRC64;
MSKSLLRLTF LLLLLLSCVS PSSFFTFNNP AEGPGACGPH QIQAFTQFKN EFDTRACNHS
DPWNGVWCDN STGAVTMLQL RACLSGTLKP NSSLFQFHHL RSLLLPHNNF TSSSISSKFG
MLNNLEVLSL SSSGFLAQVP FSFSNLSMLS ALDLSKNELT GSLSFVRNLR KLRVLDVSYN
HFSGILNPNS SLFELHHLIY LNLRYNNFTS SSLPYEFGNL NKLEVLDVSS NSFFGQVPPT
ISNLTQLTEL YLPLNDFTGS LPLVQNLTKL SILHLFGNHF SGTIPSSLFT MPFLSSIYLN
KNNLSGSIEV PNSSSSSRLE HLYLGKNHLG KILEPIAKLV NLKELDLSFL NTSHPIDLSL
FSSLKSLLLL DLSGDWISKA SLTLDSYIPS TLEVLRLEHC DISEFPNVFK TLHNLEYIAL
SNNRISGKFP EWLWSLPRLS SVFITDNLLT GFEGSSEVLV NSSVQILSLD TNSLEGALPH
LPLSINYFSA IDNRFGGDIP LSICNRSSLD VLDLSYNNFS GQIPPCLSNL LYLKLRKNNL
EGSIPDKYYV DTPLRSFDVG YNRLTGKLPR SLINCSALQF LSVDHNGIKD TFPFYLKALP
KLQVLLLSSN EFYGPLSPPN QGPLGFPELR ILEIAGNKLT GSLPPDFFVN WKASSHTMNE
DLGLYMVYSK VIFGNYHLTY YETIDLRYKG LSMEQENVLT SSATIDLSGN RLEGEIPESL
GLLKALIALN LSNNAFTGHI PLSLANLKKI ESLDLSSNQL SGTIPNGLGT LSFLAYMNVS
HNQLNGEIPQ GTQITGQPKS SFEGNAGLCG FPLQESCFGT NAPPAQKPKE EEEAEEDEQE
LNWKAVAIGY GVGVLLGLAI AQLIASYKPE WLVCLVKSRN PLRSFFGFEY
