WHW1_WHEAT
ID WHW1_WHEAT Reviewed; 146 AA.
AC O64392;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Wheatwin-1;
DE AltName: Full=Pathogenesis-related protein 4a;
DE AltName: Full=Protein 0.14;
DE AltName: Full=RNase;
DE EC=3.1.-.-;
DE Flags: Precursor;
GN Name=PR4A;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION TO 66.
RC STRAIN=cv. San Pastore; TISSUE=Endosperm;
RX PubMed=10727084; DOI=10.3109/10425179909033956;
RA Caruso C., Bertini L., Tucci M., Caporale C., Leonardi L., Saccardo F.,
RA Bressan R.A., Veronese P., Buonocore V.;
RT "Isolation and characterisation of wheat cDNA clones encoding PR4
RT proteins.";
RL DNA Seq. 10:301-307(1999).
RN [2]
RP PROTEIN SEQUENCE OF 22-146, PYROGLUTAMATE FORMATION AT GLN-22, AND VARIANT
RP ASP-109.
RC STRAIN=cv. San Pastore; TISSUE=Kernel;
RX PubMed=8251057; DOI=10.1007/bf01025037;
RA Caruso C., Caporale C., Poerio E., Facchiano A., Buonocore V.;
RT "The amino acid sequence of a protein from wheat kernel closely related to
RT proteins involved in the mechanisms of plant defence.";
RL J. Protein Chem. 12:379-386(1993).
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND 3D-STRUCTURE MODELING.
RC STRAIN=cv. San Pastore;
RX PubMed=10398366;
RX DOI=10.1002/(sici)1097-0134(19990801)36:2<192::aid-prot5>3.0.co;2-l;
RA Caporale C., Caruso C., Facchiano A., Nobile M., Leonardi L., Bertini L.,
RA Colonna G., Buonocore V.;
RT "Probing the modelled structure of wheatwin1 by controlled proteolysis and
RT sequence analysis of unfractionated digestion mixtures.";
RL Proteins 36:192-204(1999).
RN [4]
RP ANTIFUNGAL ACTIVITY.
RX PubMed=8838588; DOI=10.1007/bf01886809;
RA Caruso C., Caporale C., Chilosi G., Vacca F., Bertini L., Magro P.,
RA Poerio E., Buonocore V.;
RT "Structural and antifungal properties of a pathogenesis-related protein
RT from wheat kernel.";
RL J. Protein Chem. 15:35-44(1996).
RN [5]
RP INDUCTION.
RX DOI=10.1016/S0168-9452(03)00112-2;
RA Bertini L., Leonardi L., Caporale C., Tucci M., Cascone N.,
RA Di Berardino I., Buonocore V., Caruso C.;
RT "Pathogen-responsive wheat PR4 genes are induced by activators of systemic
RT acquired resistance and wounding.";
RL Plant Sci. 164:1067-1078(2003).
RN [6]
RP FUNCTION.
RX PubMed=15388335; DOI=10.1016/j.febslet.2004.07.091;
RA Caporale C., Di Berardino I., Leonardi L., Bertini L., Cascone A.,
RA Buonocore V., Caruso C.;
RT "Wheat pathogenesis-related proteins of class 4 have ribonuclease
RT activity.";
RL FEBS Lett. 575:71-76(2004).
RN [7]
RP FUNCTION, MUTAGENESIS OF HIS-32 AND HIS-134, AND ACTIVITY REGULATION.
RX PubMed=19647737; DOI=10.1016/j.febslet.2009.07.045;
RA Bertini L., Caporale C., Testa M., Proietti S., Caruso C.;
RT "Structural basis of the antifungal activity of wheat PR4 proteins.";
RL FEBS Lett. 583:2865-2871(2009).
CC -!- FUNCTION: Shows antifungal activity towards B.cinerea and towards the
CC wheat-specific pathogenic fungi F.culmorum and F.graminearum (groups 1
CC and 2). Has ribonuclease activity. {ECO:0000269|PubMed:15388335,
CC ECO:0000269|PubMed:19647737}.
CC -!- ACTIVITY REGULATION: Inhibited by 5'-ADP.
CC {ECO:0000269|PubMed:19647737}.
CC -!- SUBUNIT: Monomer.
CC -!- INDUCTION: Up-regulated by fungal infection, salicylic acid (SA), benzo
CC (1,2,3) thiodiazole-7-carbothioic acid S-methyl ester (BTH), methyl
CC jasmonate (MeJA) and wounding. {ECO:0000269|Ref.5}.
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DR EMBL; AJ006098; CAA06856.1; -; Genomic_DNA.
DR PIR; A53882; A53882.
DR PIR; T06485; T06485.
DR AlphaFoldDB; O64392; -.
DR SMR; O64392; -.
DR PRIDE; O64392; -.
DR EnsemblPlants; TraesCAD_scaffold_019321_01G000100.1; TraesCAD_scaffold_019321_01G000100.1; TraesCAD_scaffold_019321_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_022433_01G000100.1; TraesCLE_scaffold_022433_01G000100.1; TraesCLE_scaffold_022433_01G000100.
DR EnsemblPlants; TraesCS3A02G517100.1; TraesCS3A02G517100.1.cds1; TraesCS3A02G517100.
DR EnsemblPlants; TraesPAR_scaffold_024381_01G000100.1; TraesPAR_scaffold_024381_01G000100.1; TraesPAR_scaffold_024381_01G000100.
DR EnsemblPlants; TraesROB_scaffold_067620_01G000300.1; TraesROB_scaffold_067620_01G000300.1; TraesROB_scaffold_067620_01G000300.
DR EnsemblPlants; TraesWEE_scaffold_149922_01G000200.1; TraesWEE_scaffold_149922_01G000200.1; TraesWEE_scaffold_149922_01G000200.
DR Gramene; TraesCAD_scaffold_019321_01G000100.1; TraesCAD_scaffold_019321_01G000100.1; TraesCAD_scaffold_019321_01G000100.
DR Gramene; TraesCLE_scaffold_022433_01G000100.1; TraesCLE_scaffold_022433_01G000100.1; TraesCLE_scaffold_022433_01G000100.
DR Gramene; TraesCS3A02G517100.1; TraesCS3A02G517100.1.cds1; TraesCS3A02G517100.
DR Gramene; TraesPAR_scaffold_024381_01G000100.1; TraesPAR_scaffold_024381_01G000100.1; TraesPAR_scaffold_024381_01G000100.
DR Gramene; TraesROB_scaffold_067620_01G000300.1; TraesROB_scaffold_067620_01G000300.1; TraesROB_scaffold_067620_01G000300.
DR Gramene; TraesWEE_scaffold_149922_01G000200.1; TraesWEE_scaffold_149922_01G000200.1; TraesWEE_scaffold_149922_01G000200.
DR OMA; MAMTIMV; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; O64392; baseline and differential.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR Gene3D; 2.40.40.10; -; 1.
DR InterPro; IPR018226; Barwin_CS.
DR InterPro; IPR001153; Barwin_dom.
DR InterPro; IPR044301; PR4.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR46351; PTHR46351; 1.
DR Pfam; PF00967; Barwin; 1.
DR PRINTS; PR00602; BARWIN.
DR SUPFAM; SSF50685; SSF50685; 1.
DR PROSITE; PS00771; BARWIN_1; 1.
DR PROSITE; PS00772; BARWIN_2; 1.
DR PROSITE; PS51174; BARWIN_3; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Direct protein sequencing; Disulfide bond; Fungicide;
KW Hydrolase; Hypersensitive response; Nuclease; Pathogenesis-related protein;
KW Plant defense; Pyrrolidone carboxylic acid; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:8251057"
FT CHAIN 22..146
FT /note="Wheatwin-1"
FT /id="PRO_0000002793"
FT DOMAIN 22..146
FT /note="Barwin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00527"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8251057"
FT DISULFID 52..84
FT /evidence="ECO:0000250"
FT DISULFID 73..107
FT /evidence="ECO:0000250"
FT DISULFID 87..144
FT /evidence="ECO:0000250"
FT VARIANT 109
FT /note="N -> D"
FT /evidence="ECO:0000269|PubMed:8251057"
FT MUTAGEN 32
FT /note="H->G: Loss of antifungal activity. Reduces
FT ribonuclease activity 60%."
FT /evidence="ECO:0000269|PubMed:19647737"
FT MUTAGEN 32
FT /note="H->L: Loss of antifungal activity. Reduces
FT ribonuclease activity 62%. Reduces ribonuclease activity
FT 92%; when associated with L-134."
FT /evidence="ECO:0000269|PubMed:19647737"
FT MUTAGEN 134
FT /note="H->L: Loss of antifungal activity. Reduces
FT ribonuclease activity 92%; when associated with L-32."
FT /evidence="ECO:0000269|PubMed:19647737"
SQ SEQUENCE 146 AA; 15635 MW; F23B79E93CC2D7AA CRC64;
MAARPMLVVA LLCAAAAAAT AQQATNVRAT YHYYRPAQNN WDLGAPAVSA YCATWDASKP
LSWRSKYGWT AFCGPAGAHG QASCGKCLQV TNPATGAQIT ARIVDQCANG GLDLDWDTVF
TKIDTNGIGY QQGHLNVNYQ FVDCRD
