ID   PGIP3_PHAVU             Reviewed;         342 AA.
AC   P58823;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Polygalacturonase inhibitor 3;
DE   AltName: Full=Polygalacturonase-inhibiting protein 3;
DE            Short=PGIP-3;
DE   Flags: Precursor;
GN   Name=PGIP3;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Pinto; TISSUE=Hypocotyl;
RX   PubMed=1303801; DOI=10.1111/j.1365-313x.1992.00367.x;
RA   Toubart P., Desiderio A., Salvi G., Cervone F., Daroda L., de Lorenzo G.,
RA   Bergmann C., Darvill A.G., Albersheim P.;
RT   "Cloning and characterization of the gene encoding the
RT   endopolygalacturonase-inhibiting protein (PGIP) of Phaseolus vulgaris L.";
RL   Plant J. 2:367-373(1992).
CC   -!- FUNCTION: Inhibitor of fungal polygalacturonase. It is an important
CC       factor for plant resistance to phytopathogenic fungi.
CC       {ECO:0000250|UniProtKB:P35334}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P58822}. Membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Found in suspension-cultured cells and to a lesser
CC       extent in hypocotyls, leaves and flowers. {ECO:0000269|PubMed:1303801}.
CC   -!- SIMILARITY: Belongs to the polygalacturonase-inhibiting protein family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P58823; -.
DR   SMR; P58823; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   Pfam; PF08263; LRRNT_2; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Leucine-rich repeat; Membrane; Plant defense; Repeat; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:1303801"
FT   CHAIN           30..342
FT                   /note="Polygalacturonase inhibitor 3"
FT                   /id="PRO_0000023887"
FT   REPEAT          82..107
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          108..132
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          133..156
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          157..180
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          181..205
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          206..228
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          229..252
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          253..275
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          276..299
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          300..319
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        32..62
FT                   /evidence="ECO:0000250|UniProtKB:P58822"
FT   DISULFID        63..72
FT                   /evidence="ECO:0000250|UniProtKB:P58822"
FT   DISULFID        310..332
FT                   /evidence="ECO:0000250|UniProtKB:P58822"
FT   DISULFID        334..341
FT                   /evidence="ECO:0000250|UniProtKB:P58822"
SQ   SEQUENCE   342 AA;  37252 MW;  980AEF1D3A28F27D CRC64;
     MTQFNIPVTM SSSLSIILVI LVSLRTALSE LCNPQDKQAL LQIKKDLGNP TTLSSWLPTT
     DCCNRTWLGV LCDTDTQTYR VNNLDLSGHN LPKPYPIPSS LANLPYLNFL YIGGINNLVG
     PIPPAIAKLT QLHYLYITHT NVSGAIPDFL SQIKTLVTLD FSYNALSGTL PPSISSLPNL
     VGITFDGNRI SGAIPDSYGS FSKLFTSMTI SRNRLTGKIP PTFANLNLAF VDLSRNMLQG
     DASVLFGSDK NTQKIHLAKN SLDFDLEKVG LSKNLNGLDL RNNRIYGTLP QGLTQLKFLH
     SLNVSFNNLC GEIPQGGNLQ RFDVSAYANN KCLCGSPLPA CT