PEP1_ARATH
ID PEP1_ARATH Reviewed; 92 AA.
AC Q9LV87; Q8LCK9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Elicitor peptide 1;
DE Flags: Precursor;
GN Name=PEP1; Synonyms=PROPEP1; OrderedLocusNames=At5g64900; ORFNames=MXK3.13;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 70-92, FUNCTION, PROTEOLYTIC PROCESSING, IDENTIFICATION
RP BY MASS SPECTROMETRY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16785434; DOI=10.1073/pnas.0603727103;
RA Huffaker A., Pearce G., Ryan C.A.;
RT "An endogenous peptide signal in Arabidopsis activates components of the
RT innate immune response.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10098-10103(2006).
RN [6]
RP INTERACTION WITH PEPR1.
RX PubMed=16785433; DOI=10.1073/pnas.0603729103;
RA Yamaguchi Y., Pearce G., Ryan C.A.;
RT "The cell surface leucine-rich repeat receptor for AtPep1, an endogenous
RT peptide elicitor in Arabidopsis, is functional in transgenic tobacco
RT cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10104-10109(2006).
RN [7]
RP INTERACTION WITH PEPR1, AND MUTAGENESIS OF ARG-78; GLY-79; LYS-80; GLU-81;
RP LYS-82; VAL-83; SER-84; SER-85; GLY-86; ARG-87; PRO-88; GLY-89; GLN-90;
RP HIS-91 AND ASN-92.
RX PubMed=18824048; DOI=10.1016/j.peptides.2008.08.019;
RA Pearce G., Yamaguchi Y., Munske G., Ryan C.A.;
RT "Structure-activity studies of AtPep1, a plant peptide signal involved in
RT the innate immune response.";
RL Peptides 29:2083-2089(2008).
CC -!- FUNCTION: Elicitor of plant defense. Induces the production of plant
CC defensin (PDF1.2) and of H(2)O(2). Promotes resistance to the root
CC fungal pathogen P.irregulare. {ECO:0000269|PubMed:16785434}.
CC -!- SUBUNIT: Interacts with its receptor PEPR1.
CC {ECO:0000269|PubMed:16785433, ECO:0000269|PubMed:18824048}.
CC -!- INDUCTION: By wounding, methyl jasmonate (MeJA), ethylene. The
CC expression of the peptide PEP1 precursor is induced by the mature
CC peptide PEP1.
CC -!- SIMILARITY: Belongs to the brassicaceae elicitor peptide family.
CC {ECO:0000305}.
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DR EMBL; AB019236; BAA97302.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97966.1; -; Genomic_DNA.
DR EMBL; AY062830; AAL32908.1; -; mRNA.
DR EMBL; AY081662; AAM10224.1; -; mRNA.
DR EMBL; AY086540; AAM63605.1; -; mRNA.
DR RefSeq; NP_569001.1; NM_125888.4.
DR PDB; 5GR8; X-ray; 2.59 A; J/P=76-92.
DR PDBsum; 5GR8; -.
DR AlphaFoldDB; Q9LV87; -.
DR SMR; Q9LV87; -.
DR BioGRID; 21855; 1.
DR DIP; DIP-61206N; -.
DR IntAct; Q9LV87; 1.
DR STRING; 3702.AT5G64900.1; -.
DR PaxDb; Q9LV87; -.
DR PRIDE; Q9LV87; -.
DR ProteomicsDB; 236682; -.
DR EnsemblPlants; AT5G64900.1; AT5G64900.1; AT5G64900.
DR GeneID; 836613; -.
DR Gramene; AT5G64900.1; AT5G64900.1; AT5G64900.
DR KEGG; ath:AT5G64900; -.
DR Araport; AT5G64900; -.
DR TAIR; locus:2177659; AT5G64900.
DR HOGENOM; CLU_174284_0_0_1; -.
DR InParanoid; Q9LV87; -.
DR OMA; EETYWWM; -.
DR OrthoDB; 1571343at2759; -.
DR PhylomeDB; Q9LV87; -.
DR PRO; PR:Q9LV87; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV87; baseline and differential.
DR Genevisible; Q9LV87; AT.
DR GO; GO:0045087; P:innate immune response; IDA:TAIR.
DR GO; GO:0009723; P:response to ethylene; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR InterPro; IPR035176; PEP.
DR Pfam; PF17232; Pep1_7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Plant defense; Reference proteome.
FT PROPEP 1..69
FT /evidence="ECO:0000269|PubMed:16785434"
FT /id="PRO_0000249079"
FT PEPTIDE 70..92
FT /note="Elicitor peptide 1"
FT /id="PRO_0000249080"
FT REGION 35..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 86
FT /note="Required for ligand-receptor interaction"
FT MUTAGEN 78
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 79
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 80
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 81
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 82
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 83
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 84
FT /note="S->A: Loss of binding to PEPR1 and of subsequent
FT signaling."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 85
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 86
FT /note="G->A,P: Loss of binding to PEPR1 and of subsequent
FT signaling."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 87
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 88
FT /note="P->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 89
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 90
FT /note="Q->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 91
FT /note="H->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT MUTAGEN 92
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:18824048"
FT CONFLICT 10
FT /note="E -> G (in Ref. 4; AAM63605)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="K -> E (in Ref. 4; AAM63605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 92 AA; 10389 MW; A21FA1697B8FDA65 CRC64;
MEKSDRRSEE SHLWIPLQCL DQTLRAILKC LGLFHQDSPT TSSPGTSKQP KEEKEDVTME
KEEVVVTSRA TKVKAKQRGK EKVSSGRPGQ HN
