PGIP1_PHAVU
ID PGIP1_PHAVU Reviewed; 342 AA.
AC P35334;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Polygalacturonase inhibitor 1;
DE AltName: Full=Polygalacturonase-inhibiting protein 1;
DE Short=PGIP-1;
DE Flags: Precursor;
GN Name=PGIP1;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 30-49; 190-201;
RP 204-208; 255-259 AND 285-297, AND SIGNAL.
RC STRAIN=cv. Saxa; 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).
RN [2]
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND MUTAGENESIS OF LYS-253.
RC STRAIN=cv. Pinto; TISSUE=Hypocotyl;
RX PubMed=10228150; DOI=10.1093/emboj/18.9.2352;
RA Leckie F., Mattei B., Capodicasa C., Hemmings A., Nuss L., Aracri B.,
RA De Lorenzo G., Cervone F.;
RT "The specificity of polygalacturonase-inhibiting protein (PGIP): a single
RT amino acid substitution in the solvent-exposed beta-strand/beta-turn region
RT of the leucine-rich repeats (LRRs) confers a new recognition capability.";
RL EMBO J. 18:2352-2363(1999).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9304859; DOI=10.1094/mpmi.1997.10.7.852;
RA Desiderio A., Aracri B., Leckie F., Mattei B., Salvi G., Tigelaar H.,
RA Van Roekel J.S., Baulcombe D.C., Melchers L.S., De Lorenzo G., Cervone F.;
RT "Polygalacturonase-inhibiting proteins (PGIPs) with different specificities
RT are expressed in Phaseolus vulgaris.";
RL Mol. Plant Microbe Interact. 10:852-860(1997).
CC -!- FUNCTION: Inhibitor of fungal polygalacturonase. It is an important
CC factor for plant resistance to phytopathogenic fungi. Substrate
CC preference is polygalacturonase (PG) from A.niger >> PG of F.oxysporum,
CC A.solani or B.cinerea. Not active on PG from F.moniliforme.
CC {ECO:0000269|PubMed:10228150, ECO:0000269|PubMed:9304859}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000303|PubMed:9304859}.
CC Membrane; Peripheral membrane protein.
CC -!- MISCELLANEOUS: Mutation of Lys-253 confers the ability to inhibit the
CC F.moniliforme PG. {ECO:0000269|PubMed:10228150}.
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 EMBL; X64769; CAA46016.1; -; Genomic_DNA.
DR EMBL; A23205; CAA01664.1; -; Unassigned_DNA.
DR PIR; S23764; S23764.
DR RefSeq; XP_007159023.1; XM_007158961.1.
DR AlphaFoldDB; P35334; -.
DR SMR; P35334; -.
DR STRING; 3885.XP_007159023.1; -.
DR EnsemblPlants; ESW31017; ESW31017; PHAVU_002G201900g.
DR GeneID; 18638549; -.
DR Gramene; ESW31017; ESW31017; PHAVU_002G201900g.
DR KEGG; pvu:PHAVU_002G201900g; -.
DR eggNOG; ENOG502QRQP; Eukaryota.
DR OMA; MLETIIV; -.
DR OrthoDB; 1111550at2759; -.
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 1"
FT /id="PRO_0000023885"
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"
FT MUTAGEN 253
FT /note="K->Q: Broader spectrum of action."
FT /evidence="ECO:0000269|PubMed:10228150"
SQ SEQUENCE 342 AA; 37102 MW; 950F94E0D2A39598 CRC64;
MTQFNIPVTM SSSLSIILVI LVSLRTALSE LCNPQDKQAL LQIKKDLGNP TTLSSWLPTT
DCCNRTWLGV LCDTDTQTYR VNNLDLSGHN LPKPYPIPSS LANLPYLNFL YIGGINNLVG
PIPPAIAKLT QLHYLYITHT NVSGAIPDFL SQIKTLVTLD FSYNALSGTL PPSISSLPNL
GGITFDGNRI SGAIPDSYGS FSKLFTAMTI SRNRLTGKIP PTFANLNLAF VDLSRNMLEG
DASVLFGSDK NTKKIHLAKN SLAFDLGKVG LSKNLNGLDL RNNRIYGTLP QGLTQLKFLQ
SLNVSFNNLC GEIPQGGNLK RFDVSSYANN KCLCGSPLPS CT
