PGIP1_ARATH
ID PGIP1_ARATH Reviewed; 330 AA.
AC Q9M5J9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Polygalacturonase inhibitor 1;
DE AltName: Full=Polygalacturonase-inhibiting protein 1;
DE Short=PGIP-1;
DE Flags: Precursor;
GN Name=PGIP1; OrderedLocusNames=At5g06860; ORFNames=MOJ9_3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Park B., Jin Y., Nam S., Kim H.;
RT "Arabidopsis thaliana polygalacturonase inhibiting protein 1 (PGIP1)
RT gene.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
CC -!- FUNCTION: Inhibitor of fungal polygalacturonase. It is an important
CC factor for plant resistance to phytopathogenic fungi.
CC {ECO:0000250|UniProtKB:P58822}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:P58822}. Membrane; Peripheral membrane protein.
CC -!- SIMILARITY: Belongs to the polygalacturonase-inhibiting protein family.
CC {ECO:0000305}.
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DR EMBL; AF229249; AAF69827.1; -; mRNA.
DR EMBL; AB010697; BAB11144.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91076.1; -; Genomic_DNA.
DR EMBL; AY048295; AAK82557.1; -; mRNA.
DR EMBL; AY133567; AAM91397.1; -; mRNA.
DR RefSeq; NP_196304.1; NM_120769.2.
DR AlphaFoldDB; Q9M5J9; -.
DR SMR; Q9M5J9; -.
DR BioGRID; 15856; 1.
DR STRING; 3702.AT5G06860.1; -.
DR PaxDb; Q9M5J9; -.
DR PRIDE; Q9M5J9; -.
DR ProteomicsDB; 235097; -.
DR EnsemblPlants; AT5G06860.1; AT5G06860.1; AT5G06860.
DR GeneID; 830577; -.
DR Gramene; AT5G06860.1; AT5G06860.1; AT5G06860.
DR KEGG; ath:AT5G06860; -.
DR Araport; AT5G06860; -.
DR TAIR; locus:2169389; AT5G06860.
DR eggNOG; ENOG502QRQP; Eukaryota.
DR HOGENOM; CLU_000288_18_22_1; -.
DR InParanoid; Q9M5J9; -.
DR OMA; APLEICK; -.
DR OrthoDB; 1111550at2759; -.
DR PhylomeDB; Q9M5J9; -.
DR PRO; PR:Q9M5J9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9M5J9; baseline and differential.
DR Genevisible; Q9M5J9; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0090353; F:polygalacturonase inhibitor activity; IDA:TAIR.
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; PF00560; LRR_1; 1.
DR Pfam; PF08263; LRRNT_2; 1.
PE 1: Evidence at protein level;
KW Cell wall; Disulfide bond; Glycoprotein; Leucine-rich repeat; Membrane;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..330
FT /note="Polygalacturonase inhibitor 1"
FT /id="PRO_0000023882"
FT REPEAT 69..93
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 94..117
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 118..142
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 143..166
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 167..189
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 191..215
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 217..237
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 238..260
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 261..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 238
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 25..55
FT /evidence="ECO:0000250|UniProtKB:P58822"
FT DISULFID 56..63
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; 36689 MW; 223C0252796F18D9 CRC64;
MDKTATLCLL FLFTFLTTCL SKDLCNQNDK NTLLKIKKSL NNPYHLASWD PQTDCCSWYC
LECGDATVNH RVTALTIFSG QISGQIPAEV GDLPYLETLV FRKLSNLTGT IQPTIAKLKN
LRMLRLSWTN LTGPIPDFIS QLKNLEFLEL SFNDLSGSIP SSLSTLPKIL ALELSRNKLT
GSIPESFGSF PGTVPDLRLS HNQLSGPIPK SLGNIDFNRI DLSRNKLQGD ASMLFGSNKT
TWSIDLSRNM FQFDISKVDI PKTLGILDLN HNGITGNIPV QWTEAPLQFF NVSYNKLCGH
IPTGGKLQTF DSYSYFHNKC LCGAPLEICK
