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 27-MAR-2024, entry version 82. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; A7PW81; 6 sites, No reported glycans. DR PaxDb; 29760-VIT_08s0007g07690-t01; -. 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; 1216178at2759; -. 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; Ribonuclease Inhibitor; 1. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR013210; LRR_N_plant-typ. DR PANTHER; PTHR48059; POLYGALACTURONASE INHIBITOR 1; 1. DR PANTHER; PTHR48059:SF4; POLYGALACTURONASE INHIBITOR 2; 1. DR Pfam; PF00560; LRR_1; 3. DR Pfam; PF13855; LRR_8; 1. DR Pfam; PF08263; LRRNT_2; 1. DR PRINTS; PR00019; LEURICHRPT. DR SUPFAM; SSF52058; L domain-like; 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 //