PGIP_PYRCO
ID PGIP_PYRCO Reviewed; 330 AA.
AC Q05091;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Polygalacturonase inhibitor;
DE AltName: Full=Polygalacturonase-inhibiting protein;
DE Short=PGIG;
DE Flags: Precursor;
GN Name=PGIP;
OS Pyrus communis (Pear) (Pyrus domestica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=23211;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SIGNAL, FUNCTION,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Bartlett;
RX PubMed=8108494; DOI=10.1104/pp.102.1.133;
RA Stotz H.U., Powell A.L., Damon S.E., Greve L.C., Bennett A.B.,
RA Labavitch J.M.;
RT "Molecular characterization of a polygalacturonase inhibitor from Pyrus
RT communis L. cv Bartlett.";
RL Plant Physiol. 102:133-138(1993).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=cv. Bartlett; TISSUE=Fruit;
RA Abu-Goukh A.A., Greve L.C., Labavitch J.M.;
RT "Purification and partial characterization of 'Bartlett' pear
RT polygalacturonase inhibitors.";
RL Physiol. Mol. Plant Pathol. 23:111-122(1983).
CC -!- FUNCTION: Inhibitor of fungal polygalacturonase. It is an important
CC factor for plant resistance to phytopathogenic fungi.
CC {ECO:0000269|PubMed:8108494}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast.
CC Secreted, cell wall {ECO:0000250|UniProtKB:P58822}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in fruits, and, to a lower extent,
CC in flowers and leaves. {ECO:0000269|PubMed:8108494}.
CC -!- PTM: N-linked glycosylated. {ECO:0000269|PubMed:8108494}.
CC -!- SIMILARITY: Belongs to the polygalacturonase-inhibiting protein family.
CC {ECO:0000305}.
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DR EMBL; L09264; AAA33865.1; -; mRNA.
DR PIR; JQ2262; JQ2262.
DR AlphaFoldDB; Q05091; -.
DR SMR; Q05091; -.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Leucine-rich repeat; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8108494"
FT CHAIN 25..330
FT /note="Polygalacturonase inhibitor"
FT /id="PRO_0000023888"
FT REPEAT 69..92
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 93..118
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 119..141
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 142..166
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 167..192
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 194..215
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 217..237
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 239..261
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 262..285
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 287..309
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 27..57
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT DISULFID 58..65
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT DISULFID 298..320
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT DISULFID 322..329
FT /evidence="ECO:0000250|UniProtKB:P58822"
SQ SEQUENCE 330 AA; 36505 MW; 36BA2BCF420393E3 CRC64;
MELKFSTFLS LTLLFSSVLN PALSDLCNPD DKKVLLQIKK AFGDPYVLAS WKSDTDCCDW
YCVTCDSTTN RINSLTIFAG QVSGQIPALV GDLPYLETLE FHKQPNLTGP IQPAIAKLKG
LKSLRLSWTN LSGSVPDFLS QLKNLTFLDL SFNNLTGAIP SSLSELPNLG ALRLDRNKLT
GHIPISFGQF IGNVPDLYLS HNQLSGNIPT SFAQMDFTSI DLSRNKLEGD ASVIFGLNKT
TQIVDLSRNL LEFNLSKVEF PTSLTSLDIN HNKIYGSIPV EFTQLNFQFL NVSYNRLCGQ
IPVGGKLQSF DEYSYFHNRC LCGAPLPSCK
