ID   GIP2_PHYSO              Reviewed;         289 AA.
AC   Q945T9;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Glucanase inhibitor protein 2 {ECO:0000303|PubMed:12084830};
DE   Flags: Precursor;
GN   Name=GIP2 {ECO:0000303|PubMed:12084830};
OS   Phytophthora sojae (Soybean stem and root rot agent) (Phytophthora
OS   megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=67593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   STRAIN=Race1;
RX   PubMed=12084830; DOI=10.1105/tpc.002253;
RA   Rose J.K., Ham K.S., Darvill A.G., Albersheim P.;
RT   "Molecular cloning and characterization of glucanase inhibitor proteins:
RT   coevolution of a counterdefense mechanism by plant pathogens.";
RL   Plant Cell 14:1329-1345(2002).
CC   -!- FUNCTION: Secreted effector that suppresses host plant glucan elicitor-
CC       mediated defense responses (Probable). Targets host endoglucanases and
CC       inhibits the endoglucanase-mediated release of elicitor-active glucan
CC       oligosaccharides from P.sojae cell walls (Probable).
CC       {ECO:0000305|PubMed:12084830}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12084830}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000305}.
CC   -!- CAUTION: None of the predicted glucanase inhibitor proteins (GIPS) has
CC       an intact catalytic triad, therefore, GIPs are proteolytically
CC       inactive. {ECO:0000305|PubMed:12084830}.
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DR   EMBL; AF406608; AAL11721.1; -; mRNA.
DR   RefSeq; XP_009538335.1; XM_009540040.1.
DR   RefSeq; XP_009538340.1; XM_009540045.1.
DR   AlphaFoldDB; Q945T9; -.
DR   SMR; Q945T9; -.
DR   GeneID; 20661700; -.
DR   GeneID; 20661745; -.
DR   KEGG; psoj:PHYSODRAFT_532115; -.
DR   KEGG; psoj:PHYSODRAFT_532438; -.
DR   VEuPathDB; FungiDB:PHYSODRAFT_532115; -.
DR   VEuPathDB; FungiDB:PHYSODRAFT_532438; -.
DR   HOGENOM; CLU_006842_7_3_1; -.
DR   OMA; QCEAAYP; -.
DR   OrthoDB; 1314811at2759; -.
DR   PHI-base; PHI:653; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Secreted; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..289
FT                   /note="Glucanase inhibitor protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004319475"
FT   DOMAIN          29..257
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        56..72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        180..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        202..233
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   289 AA;  30201 MW;  C71B0EC0F892F957 CRC64;
     MKVTATIAAA SMAIAAASAD ADTTSRQLIL GGSIIPSGQK TYSVGIRSTA GGDTYCGGAL
     ISPTHVLTTT MCTKHAKPDF VAVGTHYVNG TKDGEQLKVI QAQNHTDFNK TGNGEYDFAL
     LTLEKPSKFA PVKLPKADDS DIKPGMWSKA MGWGWTSFPN GSPSNEMQGV NLQVWSNEDC
     SQVYVINPTN VCAGGVAGKD ACVADTGGPL IKENGAGDKD DVLIGLVNWG YGCGDEGAPT
     VYSRVSSALK WVNPIIKTKQ VKTAVPVQQA ISGKHGVPIK QGMPGTVRN