PP914_SOYBN
ID PP914_SOYBN Reviewed; 52 AA.
AC K7LSB9;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Protein PROPEP914;
DE Short=GmPROPEP914;
DE Contains:
DE RecName: Full=Peptide GmPep914;
DE Flags: Precursor;
GN Name=PROPEP914; OrderedLocusNames=Glyma12g00991;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP MUTAGENESIS OF ASP-45; HIS-46; PRO-47; ARG-48; GLY-49; GLY-50; ASN-51 AND
RP TYR-52, INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. A3525;
RX PubMed=21478368; DOI=10.1104/pp.111.173096;
RA Yamaguchi Y., Barona G., Ryan C.A., Pearce G.;
RT "GmPep914, an eight-amino acid peptide isolated from soybean leaves,
RT activates defense-related genes.";
RL Plant Physiol. 156:932-942(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
CC -!- FUNCTION: [Peptide GmPep914]: Produces a rapid alkalinization of the
CC cellular media and the induction of defense-related genes, including
CC chitinase 1b, chalcone synthase and CYP93A1. Not active in tobacco or
CC Arabidopsis. The receptor for GmPep914 is probably different from the
CC receptor for GmSubPep. {ECO:0000269|PubMed:21478368}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. Barely detected in flowers.
CC {ECO:0000269|PubMed:21478368}.
CC -!- INDUCTION: Up-regulated by the GmPep914 peptide, ethephon, methyl
CC jasmonate and methyl salicylate. {ECO:0000269|PubMed:21478368}.
CC -!- CAUTION: The full-length coding region in cv. A3525 has been amplified
CC by RT-PCR and sequenced, but not submitted to the EMBL/GenBank/DDBJ
CC databases (PubMed:21478368). {ECO:0000305|PubMed:21478368}.
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DR AlphaFoldDB; K7LSB9; -.
DR PRIDE; K7LSB9; -.
DR EnsemblPlants; KRH23857; KRH23857; GLYMA_12G007400.
DR Gramene; KRH23857; KRH23857; GLYMA_12G007400.
DR HOGENOM; CLU_3091147_0_0_1; -.
DR Proteomes; UP000008827; Chromosome 12.
DR Genevisible; K7LSB9; GM.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Plant defense; Reference proteome.
FT CHAIN 1..52
FT /note="Protein PROPEP914"
FT /id="PRO_0000430191"
FT PEPTIDE 45..52
FT /note="Peptide GmPep914"
FT /id="PRO_0000430192"
FT REGION 25..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 45
FT /note="D->A: No effect on alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
FT MUTAGEN 46
FT /note="H->A: No effect on alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
FT MUTAGEN 47
FT /note="P->A: No effect on alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
FT MUTAGEN 48
FT /note="R->A: No effect on alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
FT MUTAGEN 49
FT /note="G->A: No effect on alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
FT MUTAGEN 50
FT /note="G->A: No effect on alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
FT MUTAGEN 51
FT /note="N->A: Loss of alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
FT MUTAGEN 52
FT /note="Y->A: Loss of alkalinization activity."
FT /evidence="ECO:0000269|PubMed:21478368"
SQ SEQUENCE 52 AA; 6061 MW; 1E6A2DF14B44CE91 CRC64;
MVKCFDFFLS LNFGKMTKLL VWRTDKPQDD MPQTPNSQVT IVSRDHPRGG NY
