PGIP2_PHAVU
ID PGIP2_PHAVU Reviewed; 342 AA.
AC P58822;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Polygalacturonase inhibitor 2;
DE AltName: Full=Polygalacturonase-inhibiting protein 2;
DE Short=PGIP-2;
DE Flags: Precursor;
GN Name=PGIP2;
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, FUNCTION, AND MUTAGENESIS OF LEU-89; VAL-181; SER-207;
RP GLN-253; HIS-300; GLN-320; ALA-326 AND ALA-340.
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 [2]
RP STRUCTURE OF CARBOHYDRATES ON ASN-64 AND ASN-141, GLYCOSYLATION AT ASN-64
RP AND ASN-141, AND DISULFIDE BONDS.
RX PubMed=11148052; DOI=10.1021/bi0017632;
RA Mattei B., Bernalda M.S., Federici L., Roepstorff P., Cervone F., Boffi A.;
RT "Secondary structure and posttranslational modifications of the leucine-
RT rich repeat protein PGIP (polygalacturonase-inhibiting protein) from
RT Phaseolus vulgaris.";
RL Biochemistry 40:569-576(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 30-342, DISULFIDE BONDS,
RP LEUCINE-RICH REPEATS, AND GLYCOSYLATION AT ASN-64; ASN-141 AND ASN-303.
RX PubMed=12904578; DOI=10.1073/pnas.1733690100;
RA Di Matteo A., Federici L., Mattei B., Salvi G., Johnson K.A., Savino C.,
RA De Lorenzo G., Tsernoglou D., Cervone F.;
RT "The crystal structure of polygalacturonase-inhibiting protein (PGIP), a
RT leucine-rich repeat protein involved in plant defense.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10124-10128(2003).
CC -!- FUNCTION: Inhibitor of fungal polygalacturonase. It is an important
CC factor for plant resistance to phytopathogenic fungi. Inhibits all
CC polygalacturonases (PG) tested, with the exception of PG from
CC F.oxysporum which was only inhibited at 60%.
CC {ECO:0000269|PubMed:10228150}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000305|PubMed:10228150}. Membrane; Peripheral membrane protein.
CC -!- PTM: Asn-303 is not glycosylated. {ECO:0000269|PubMed:11148052}.
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 PDB; 1OGQ; X-ray; 1.70 A; A=30-342.
DR PDBsum; 1OGQ; -.
DR AlphaFoldDB; P58822; -.
DR SMR; P58822; -.
DR STRING; 3885.XP_007159022.1; -.
DR GlyConnect; 507; 1 N-Linked glycan.
DR iPTMnet; P58822; -.
DR EnsemblPlants; ESW31016; ESW31016; PHAVU_002G201800g.
DR Gramene; ESW31016; ESW31016; PHAVU_002G201800g.
DR eggNOG; ENOG502QRQP; Eukaryota.
DR EvolutionaryTrace; P58822; -.
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 3D-structure; Cell wall; Disulfide bond; Glycoprotein; Leucine-rich repeat;
KW Membrane; Plant defense; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..342
FT /note="Polygalacturonase inhibitor 2"
FT /id="PRO_0000023886"
FT REPEAT 82..107
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 108..132
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 133..156
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 157..180
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 181..205
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 206..228
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 229..252
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 253..275
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 276..299
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:12904578"
FT REPEAT 300..319
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:12904578"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:11148052, ECO:0000269|PubMed:12904578,
FT ECO:0007744|PDB:1OGQ"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:11148052, ECO:0000269|PubMed:12904578,
FT ECO:0007744|PDB:1OGQ"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:12904578, ECO:0007744|PDB:1OGQ"
FT DISULFID 32..62
FT /evidence="ECO:0000269|PubMed:11148052,
FT ECO:0000269|PubMed:12904578, ECO:0007744|PDB:1OGQ"
FT DISULFID 63..72
FT /evidence="ECO:0000269|PubMed:11148052,
FT ECO:0000269|PubMed:12904578, ECO:0007744|PDB:1OGQ"
FT DISULFID 310..332
FT /evidence="ECO:0000269|PubMed:11148052,
FT ECO:0000269|PubMed:12904578, ECO:0007744|PDB:1OGQ"
FT DISULFID 334..341
FT /evidence="ECO:0000269|PubMed:11148052,
FT ECO:0000269|PubMed:12904578, ECO:0007744|PDB:1OGQ"
FT MUTAGEN 89
FT /note="L->H: No effect."
FT /evidence="ECO:0000269|PubMed:10228150"
FT MUTAGEN 181
FT /note="V->G: No effect. Loss of activity; when associated
FT with K-253. No effect; when associated with S-326."
FT /evidence="ECO:0000269|PubMed:10228150"
FT MUTAGEN 207
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:10228150"
FT MUTAGEN 253
FT /note="Q->K: 70% decrease of activity. Loss of activity;
FT when associated with G-181 or S-326."
FT /evidence="ECO:0000269|PubMed:10228150"
FT MUTAGEN 300
FT /note="H->Q: No effect."
FT /evidence="ECO:0000269|PubMed:10228150"
FT MUTAGEN 320
FT /note="Q->K: No effect."
FT /evidence="ECO:0000269|PubMed:10228150"
FT MUTAGEN 326
FT /note="A->S: No effect. No effect; when associated with G-
FT 181. Loss of activity; when associated with K-253."
FT /evidence="ECO:0000269|PubMed:10228150"
FT MUTAGEN 340
FT /note="A->S: No effect."
FT /evidence="ECO:0000269|PubMed:10228150"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1OGQ"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:1OGQ"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1OGQ"
FT STRAND 329..335
FT /evidence="ECO:0007829|PDB:1OGQ"
SQ SEQUENCE 342 AA; 37068 MW; 8B93E4AEB4A6477E CRC64;
MTQFNIPVTM SSSLSIILVI LVSLSTAHSE LCNPQDKQAL LQIKKDLGNP TTLSSWLPTT
DCCNRTWLGV LCDTDTQTYR VNNLDLSGLN LPKPYPIPSS LANLPYLNFL YIGGINNLVG
PIPPAIAKLT QLHYLYITHT NVSGAIPDFL SQIKTLVTLD FSYNALSGTL PPSISSLPNL
VGITFDGNRI SGAIPDSYGS FSKLFTSMTI SRNRLTGKIP PTFANLNLAF VDLSRNMLEG
DASVLFGSDK NTQKIHLAKN SLAFDLGKVG LSKNLNGLDL RNNRIYGTLP QGLTQLKFLH
SLNVSFNNLC GEIPQGGNLQ RFDVSAYANN KCLCGSPLPA CT
