ID   GIP3_PHYSO              Reviewed;         139 AA.
AC   Q945T8;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Glucanase inhibitor protein 3 {ECO:0000303|PubMed:12084830};
DE   Flags: Fragment;
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.
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; AF406609; AAL11722.1; -; mRNA.
DR   AlphaFoldDB; Q945T8; -.
DR   SMR; Q945T8; -.
DR   VEuPathDB; FungiDB:PHYSODRAFT_532326; -.
DR   HOGENOM; CLU_006842_7_3_1; -.
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   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
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; Secreted; Virulence.
FT   CHAIN           <1..139
FT                   /note="Glucanase inhibitor protein 3"
FT                   /id="PRO_0000448094"
FT   DOMAIN          <1..138
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        61..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        83..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   139 AA;  14715 MW;  E8EC422B9B9ED93B CRC64;
     VLTLEKPSKF APIKLPKADG SDIFPRVWSK VMGWGVTSYP NGKPSNELQS VDVRVWGDNA
     CENKLGVDKS SLCAGGEAGK DSCVGDTGDP LIKENGRGDA DDILLGLSGW GTGCGDKDMP
     SVYSRVSAGI EWINSVIKK