PGIP_VITVI
ID PGIP_VITVI Reviewed; 333 AA.
AC A7PW81; Q8LKV2; Q9AXP4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Polygalacturonase inhibitor {ECO:0000250|UniProtKB:P58822};
DE AltName: Full=Polygalacturonase-inhibiting protein {ECO:0000250|UniProtKB:P58822, ECO:0000312|EMBL:AAM74142.1};
DE Short=PGIG;
DE Flags: Precursor;
GN Name=pgip; ORFNames=GSVIVT00025506001, LOC100232865;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAK14075.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Chardonnay {ECO:0000269|Ref.1};
RC TISSUE=Leaf {ECO:0000312|EMBL:AAK14075.1};
RA Bezier A., Lambert B., Baillieul F.;
RT "Molecular cloning of a grapevine gene coding for polygalacturonase
RT inhibiting protein.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK14075.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Pinotage {ECO:0000269|Ref.2};
RA De Ascensao A.R., Pretorius I.S., Bellstedt D.U., Burger J.T., Vivier M.A.;
RT "The isolation and characterization of a gene encoding a polygalacturonase-
RT inhibiting protein (PGIP) from Vitis vinifera L.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000269|PubMed:17721507};
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAK14075.1}
RP PROTEIN SEQUENCE OF 172-179.
RA Almagro L., Belchi-Navarro S., Pedreno M.A.;
RL Submitted (JUL-2008) to UniProtKB.
CC -!- FUNCTION: Inhibitor of fungal polygalacturonase. It is an important
CC factor for plant resistance to phytopathogenic fungi. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:P58822}. Membrane
CC {ECO:0000250|UniProtKB:P58822}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P58822}.
CC -!- SIMILARITY: Belongs to the polygalacturonase-inhibiting protein family.
CC {ECO:0000255}.
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DR EMBL; AF305093; AAK14075.1; -; mRNA.
DR EMBL; AF499451; AAM74142.1; -; Genomic_DNA.
DR RefSeq; NP_001268106.1; NM_001281177.1.
DR AlphaFoldDB; A7PW81; -.
DR SMR; A7PW81; -.
DR STRING; 29760.VIT_08s0007g07690.t01; -.
DR PRIDE; A7PW81; -.
DR EnsemblPlants; Vitvi08g01844_t001; Vitvi08g01844_P001; Vitvi08g01844.
DR GeneID; 100232865; -.
DR Gramene; Vitvi08g01844_t001; Vitvi08g01844_P001; Vitvi08g01844.
DR KEGG; vvi:100232865; -.
DR eggNOG; ENOG502QRQP; Eukaryota.
DR OrthoDB; 1111550at2759; -.
DR ExpressionAtlas; A7PW81; baseline and differential.
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; 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.
DR PROSITE; PS51450; LRR; 4.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..333
FT /note="Polygalacturonase inhibitor"
FT /evidence="ECO:0000255"
FT /id="PRO_0000363745"
FT REPEAT 72..96
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 97..120
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 121..144
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 145..169
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 170..192
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 194..220
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 221..240
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 241..263
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 264..288
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 290..312
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 30..60
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT DISULFID 61..68
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT DISULFID 301..323
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT DISULFID 325..332
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT CONFLICT 47
FT /note="N -> T (in Ref. 1; AAK14075)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="S -> F (in Ref. 1; AAK14075)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="L -> I (in Ref. 1; AAK14075)"
FT /evidence="ECO:0000305"
FT CONFLICT 199..201
FT /note="GLH -> YLY (in Ref. 2; AAM74142)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="N -> T (in Ref. 2; AAM74142)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="L -> P (in Ref. 2; AAM74142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36929 MW; 0D4C502A6B93EF2D CRC64;
METSKLFLLS SSLLLVLLAT RPCPSLSERC NPKDKKVLLQ IKKALDNPYI LASWNPNTDC
CGWYCVECDL TTHRINSLTI FSGQLSGQIP DAVGDLPFLE TLIFRKLSNL TGQIPPAIAK
LKHLKMVRLS WTNLSGPVPA FFSELKNLTY LDLSFNNLSG PIPGSLSLLP NLGALHLDRN
HLTGPIPDSF GKFAGSTPGL HLSHNQLSGK IPYSFRGFDP NVMDLSRNKL EGDLSIFFNA
NKSTQIVDFS RNLFQFDLSR VEFPKSLTSL DLSHNKIAGS LPEMMTSLDL QFLNVSYNRL
CGKIPVGGKL QSFDYDSYFH NRCLCGAPLQ SCK
