RLP3_ARATH
ID RLP3_ARATH Reviewed; 756 AA.
AC Q9SHI4; Q0WVG4;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Receptor-like protein 3 {ECO:0000303|PubMed:18434605};
DE Short=AtRLP3 {ECO:0000303|PubMed:18434605};
DE AltName: Full=Protein RESISTANCE TO FUSARIUM OXYSPORUM 2 {ECO:0000303|PubMed:15965251};
DE Flags: Precursor;
GN Name=RLP3 {ECO:0000303|PubMed:18434605};
GN Synonyms=RFO2 {ECO:0000303|PubMed:15965251};
GN OrderedLocusNames=At1g17250 {ECO:0000312|Araport:AT1G17250};
GN ORFNames=F20D23.5 {ECO:0000312|EMBL:AAD50010.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] OF 1-647.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND GENE FAMILY.
RC STRAIN=cv. Columbia, and cv. Ty-0;
RX PubMed=15965251; DOI=10.1534/genetics.105.042218;
RA Diener A.C., Ausubel F.M.;
RT "RESISTANCE TO FUSARIUM OXYSPORUM 1, a dominant Arabidopsis disease-
RT resistance gene, is not race specific.";
RL Genetics 171:305-321(2005).
RN [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=19897604; DOI=10.1104/pp.109.148197;
RA Wang G., Long Y., Thomma B.P.H.J., de Wit P.J.G.M., Angenent G.C.,
RA Fiers M.;
RT "Functional analyses of the CLAVATA2-like proteins and their domains that
RT contribute to CLAVATA2 specificity.";
RL Plant Physiol. 152:320-331(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Ty-0;
RX PubMed=23717215; DOI=10.1371/journal.pgen.1003525;
RA Shen Y., Diener A.C.;
RT "Arabidopsis thaliana resistance to fusarium oxysporum 2 implicates
RT tyrosine-sulfated peptide signaling in susceptibility and resistance to
RT root infection.";
RL PLoS Genet. 9:E1003525-E1003525(2013).
CC -!- FUNCTION: Involved in the perception of CLV3 and CLV3-like peptides,
CC that act as extracellular signals regulating meristems maintenance (By
CC similarity). Contributes, with WAKL22/RFO1, to resistance to
CC F.oxysporum (f.) matthioli in cv. Columbia relative to cv. Ty-0
CC (PubMed:15965251, PubMed:23717215). {ECO:0000250|UniProtKB:Q9SHI3,
CC ECO:0000269|PubMed:15965251, ECO:0000269|PubMed:23717215}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at very low levels in the shoot apex.
CC {ECO:0000269|PubMed:19897604}.
CC -!- DISRUPTION PHENOTYPE: Normal resistance to F.oxysporum (f.) matthioli
CC in cv. Columbia. The double mutant rfo1 rfo2 is strongly susceptible to
CC F.oxysporum. {ECO:0000269|PubMed:23717215}.
CC -!- SIMILARITY: Belongs to the RLP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE98884.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AC007651; AAD50010.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29564.1; -; Genomic_DNA.
DR EMBL; AK226786; BAE98884.1; ALT_SEQ; mRNA.
DR PIR; G86308; G86308.
DR RefSeq; NP_173168.1; NM_101586.1.
DR AlphaFoldDB; Q9SHI4; -.
DR SMR; Q9SHI4; -.
DR STRING; 3702.AT1G17250.1; -.
DR PaxDb; Q9SHI4; -.
DR PRIDE; Q9SHI4; -.
DR EnsemblPlants; AT1G17250.1; AT1G17250.1; AT1G17250.
DR GeneID; 838296; -.
DR Gramene; AT1G17250.1; AT1G17250.1; AT1G17250.
DR KEGG; ath:AT1G17250; -.
DR Araport; AT1G17250; -.
DR TAIR; locus:2020382; AT1G17250.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_22_9_1; -.
DR InParanoid; Q9SHI4; -.
DR OMA; ISCHQED; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9SHI4; -.
DR PRO; PR:Q9SHI4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SHI4; differential.
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:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:TAIR.
DR GO; GO:0010073; P:meristem maintenance; ISS:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
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 Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR PROSITE; PS51450; LRR; 13.
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..50
FT /evidence="ECO:0000305|PubMed:23717215"
FT CHAIN 51..756
FT /note="Receptor-like protein 3"
FT /id="PRO_0000441618"
FT TOPO_DOM 51..725
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 747..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 95..119
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 120..143
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 145..169
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 174..199
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 201..225
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 226..250
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 252..274
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 275..298
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 299..322
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 323..346
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 348..370
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 371..395
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 397..419
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 420..443
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 445..471
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 474..498
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 499..521
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 522..546
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 548..569
FT /note="LRR 19; degenerate"
FT /evidence="ECO:0000305"
FT REPEAT 570..593
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 608..631
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT REPEAT 632..656
FT /note="LRR 22"
FT /evidence="ECO:0000255"
FT REPEAT 658..681
FT /note="LRR 23"
FT /evidence="ECO:0000255"
FT REGION 51..88
FT /note="N-cap"
FT /evidence="ECO:0000305|PubMed:23717215"
FT REGION 699..725
FT /note="C-cap/acidic domain"
FT /evidence="ECO:0000305|PubMed:23717215"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 381
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 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 756 AA; 83640 MW; 02163C8F404296FD CRC64;
MTNEGRFKAK GFVRTSSTTR PIQALSFHMI GILLQCVLFI SVLSIAVSEA LCNSQDRESL
LWFSGNVSSS VSPLNWNPSI DCCSWEGITC DDSPDSHITA ISLPFRALYG KLPLSVLRLH
HLSQLNLSHN RLSGHLPSGF LSALDQLKVL DLSYNSLDGE LPVEQTFRNG SNRCFPIRIV
DLSSNFLQGE ILPSSIFMQG TFDLISFNVS KNSFTGSIPS FMCKSSPQLS KLDFSYNDFT
GNIPQGLGRC LKLSVLQAGF NNISGEIPSD IYNLSELEQL FLPVNHLSGK INDDITHLTK
LKSLELYSNH LGGEIPMDIG QLSRLQSLQL HINNITGTVP PSLANCTNLV KLNLRLNRLE
GTLSELDFSR FQSLSILDLG NNSFSGDFPW RVHSCKSLSA MRFASNKLTG QISPHVLELE
SLSILSLSDN KLMNITGALG ILQGCRNLST LLIGKNFYNE TFPSDKDLIS SDGFPNLQIF
ASGGSGLRGE IPAWLIKLKS LAVIDLSHNQ LVGSIPGWLG TFPHLFYIDL SENLLSGELP
KDLFQLKALM SQKAYDATER NYLKLPVFVS PNNVTTHQQY NQLFSLPPGI YIRRNNLKGS
IPIEVGQLKV LHVLELSHNY LSGIIPHELS KLTSLERLDL SNNHLSGRIP WSLTSLHYMS
YFNVVNNSLD GPIPTGSQFD TFPQANFKGN PLLCGGILLT SCKASTKLPA TTTNKADTED
EEELKFIFIL GVATGFFVSY CFYWCFFARL DAFISK
