PEPR2_ARATH
ID PEPR2_ARATH Reviewed; 1088 AA.
AC Q9FZ59;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Leucine-rich repeat receptor-like protein kinase PEPR2;
DE EC=2.7.11.1;
DE AltName: Full=Elicitor peptide 1 receptor 2;
DE Short=PEP1 receptor 2;
DE Flags: Precursor;
GN Name=PEPR2; OrderedLocusNames=At1g17750; ORFNames=F11A6.9;
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].
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [4]
RP INTERACTION WITH BAK1.
RX PubMed=20018402; DOI=10.1016/j.ejcb.2009.11.001;
RA Postel S., Kuefner I., Beuter C., Mazzotta S., Schwedt A., Borlotti A.,
RA Halter T., Kemmerling B., Nuernberger T.;
RT "The multifunctional leucine-rich repeat receptor kinase BAK1 is implicated
RT in Arabidopsis development and immunity.";
RL Eur. J. Cell Biol. 89:169-174(2010).
RN [5]
RP INTERACTION WITH CLE14.
RX PubMed=28586647; DOI=10.1016/j.devcel.2017.05.009;
RA Gutierrez-Alanis D., Yong-Villalobos L., Jimenez-Sandoval P.,
RA Alatorre-Cobos F., Oropeza-Aburto A., Mora-Macias J., Sanchez-Rodriguez F.,
RA Cruz-Ramirez A., Herrera-Estrella L.;
RT "Phosphate starvation-dependent iron mobilization induces CLE14 expression
RT to trigger root meristem differentiation through CLV2/PEPR2 signaling.";
RL Dev. Cell 41:555-570(2017).
CC -!- FUNCTION: Acts as a receptor for PEP defense peptides. Unlike typical
CC immune receptors, senses an endogenous elicitor that potentiates PAMP-
CC inducible plant responses (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with BAK1 (PubMed:20018402). Interacts with CLE14
CC (PubMed:28586647). {ECO:0000269|PubMed:20018402,
CC ECO:0000269|PubMed:28586647}.
CC -!- INTERACTION:
CC Q9FZ59; Q9M9S4: At1g14390; NbExp=2; IntAct=EBI-20652612, EBI-16954682;
CC Q9FZ59; Q9M9C5: At1g68400; NbExp=3; IntAct=EBI-20652612, EBI-1238661;
CC Q9FZ59; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-20652612, EBI-20651541;
CC Q9FZ59; Q9SUQ3: At4g23740; NbExp=2; IntAct=EBI-20652612, EBI-16912451;
CC Q9FZ59; C0LGR9: At4g31250; NbExp=2; IntAct=EBI-20652612, EBI-16955262;
CC Q9FZ59; C0LGU5: At5g45780; NbExp=3; IntAct=EBI-20652612, EBI-16964970;
CC Q9FZ59; Q8W4S5: At5g63710; NbExp=2; IntAct=EBI-20652612, EBI-16934827;
CC Q9FZ59; C0LGQ5: GSO1; NbExp=2; IntAct=EBI-20652612, EBI-16905069;
CC Q9FZ59; C0LGU7: MDIS1; NbExp=2; IntAct=EBI-20652612, EBI-16196163;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC034257; AAF99817.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29632.1; -; Genomic_DNA.
DR EMBL; FJ708635; ACN59231.1; -; mRNA.
DR PIR; E86312; E86312.
DR RefSeq; NP_173217.1; NM_101638.3.
DR AlphaFoldDB; Q9FZ59; -.
DR SMR; Q9FZ59; -.
DR BioGRID; 23592; 36.
DR IntAct; Q9FZ59; 42.
DR STRING; 3702.AT1G17750.1; -.
DR iPTMnet; Q9FZ59; -.
DR PaxDb; Q9FZ59; -.
DR PRIDE; Q9FZ59; -.
DR ProteomicsDB; 236810; -.
DR EnsemblPlants; AT1G17750.1; AT1G17750.1; AT1G17750.
DR GeneID; 838353; -.
DR Gramene; AT1G17750.1; AT1G17750.1; AT1G17750.
DR KEGG; ath:AT1G17750; -.
DR Araport; AT1G17750; -.
DR TAIR; locus:2007918; AT1G17750.
DR eggNOG; ENOG502QUAH; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9FZ59; -.
DR OMA; NITMIKW; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9FZ59; -.
DR PRO; PR:Q9FZ59; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ59; baseline and differential.
DR Genevisible; Q9FZ59; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042277; F:peptide binding; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 16.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1088
FT /note="Leucine-rich repeat receptor-like protein kinase
FT PEPR2"
FT /id="PRO_0000389460"
FT TOPO_DOM 27..739
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 75..99
FT /note="LRR 1"
FT REPEAT 100..122
FT /note="LRR 2"
FT REPEAT 123..146
FT /note="LRR 3"
FT REPEAT 147..170
FT /note="LRR 4"
FT REPEAT 172..194
FT /note="LRR 5"
FT REPEAT 195..219
FT /note="LRR 6"
FT REPEAT 221..243
FT /note="LRR 7"
FT REPEAT 244..267
FT /note="LRR 8"
FT REPEAT 269..291
FT /note="LRR 9"
FT REPEAT 292..315
FT /note="LRR 10"
FT REPEAT 316..339
FT /note="LRR 11"
FT REPEAT 341..363
FT /note="LRR 12"
FT REPEAT 365..387
FT /note="LRR 13"
FT REPEAT 388..411
FT /note="LRR 14"
FT REPEAT 412..435
FT /note="LRR 15"
FT REPEAT 436..459
FT /note="LRR 16"
FT REPEAT 460..485
FT /note="LRR 17"
FT REPEAT 487..506
FT /note="LRR 18"
FT REPEAT 507..529
FT /note="LRR 19"
FT REPEAT 530..554
FT /note="LRR 20"
FT REPEAT 556..577
FT /note="LRR 21"
FT REPEAT 578..602
FT /note="LRR 22"
FT REPEAT 603..627
FT /note="LRR 23"
FT REPEAT 629..651
FT /note="LRR 24"
FT REPEAT 652..676
FT /note="LRR 25"
FT REPEAT 678..698
FT /note="LRR 26"
FT DOMAIN 794..1080
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 921
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 800..808
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 822
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 791
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 868
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 908
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 962
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 969
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 698
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1088 AA; 119177 MW; 7BE349BC5711BD17 CRC64;
MRNLGLLEIT LLCSLFVYFR IDSVSSLNSD GLALLSLLKH FDKVPLEVAS TWKENTSETT
PCNNNWFGVI CDLSGNVVET LNLSASGLSG QLGSEIGELK SLVTLDLSLN SFSGLLPSTL
GNCTSLEYLD LSNNDFSGEV PDIFGSLQNL TFLYLDRNNL SGLIPASVGG LIELVDLRMS
YNNLSGTIPE LLGNCSKLEY LALNNNKLNG SLPASLYLLE NLGELFVSNN SLGGRLHFGS
SNCKKLVSLD LSFNDFQGGV PPEIGNCSSL HSLVMVKCNL TGTIPSSMGM LRKVSVIDLS
DNRLSGNIPQ ELGNCSSLET LKLNDNQLQG EIPPALSKLK KLQSLELFFN KLSGEIPIGI
WKIQSLTQML VYNNTLTGEL PVEVTQLKHL KKLTLFNNGF YGDIPMSLGL NRSLEEVDLL
GNRFTGEIPP HLCHGQKLRL FILGSNQLHG KIPASIRQCK TLERVRLEDN KLSGVLPEFP
ESLSLSYVNL GSNSFEGSIP RSLGSCKNLL TIDLSQNKLT GLIPPELGNL QSLGLLNLSH
NYLEGPLPSQ LSGCARLLYF DVGSNSLNGS IPSSFRSWKS LSTLVLSDNN FLGAIPQFLA
ELDRLSDLRI ARNAFGGKIP SSVGLLKSLR YGLDLSANVF TGEIPTTLGA LINLERLNIS
NNKLTGPLSV LQSLKSLNQV DVSYNQFTGP IPVNLLSNSS KFSGNPDLCI QASYSVSAII
RKEFKSCKGQ VKLSTWKIAL IAAGSSLSVL ALLFALFLVL CRCKRGTKTE DANILAEEGL
SLLLNKVLAA TDNLDDKYII GRGAHGVVYR ASLGSGEEYA VKKLIFAEHI RANQNMKREI
ETIGLVRHRN LIRLERFWMR KEDGLMLYQY MPNGSLHDVL HRGNQGEAVL DWSARFNIAL
GISHGLAYLH HDCHPPIIHR DIKPENILMD SDMEPHIGDF GLARILDDST VSTATVTGTT
GYIAPENAYK TVRSKESDVY SYGVVLLELV TGKRALDRSF PEDINIVSWV RSVLSSYEDE
DDTAGPIVDP KLVDELLDTK LREQAIQVTD LALRCTDKRP ENRPSMRDVV KDLTDLESFV
RSTSGSVH
