ID   GIP1_PHYSO              Reviewed;         257 AA.
AC   Q945U0;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Glucanase inhibitor protein 1 {ECO:0000303|PubMed:12084830};
DE   Flags: Precursor;
GN   Name=GIP1 {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], PROTEIN SEQUENCE OF 29-55; 96-101; 131-135;
RP   136-151; 152-157; 213-221 AND 236-242, SUBCELLULAR LOCATION, INDUCTION,
RP   INTERACTION WITH HOST EGASEA, AND FUNCTION.
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).
RN   [2]
RP   INTERACTION WITH HOST EGASEA, AND FUNCTION.
RX   PubMed=15545660; DOI=10.1534/genetics.103.025098;
RA   Bishop J.G., Ripoll D.R., Bashir S., Damasceno C.M., Seeds J.D., Rose J.K.;
RT   "Selection on Glycine beta-1,3-endoglucanase genes differentially inhibited
RT   by a Phytophthora glucanase inhibitor protein.";
RL   Genetics 169:1009-1019(2005).
CC   -!- FUNCTION: Secreted effector that suppresses host plant glucan elicitor-
CC       mediated defense responses (PubMed:12084830, PubMed:15545660). Targets
CC       host endoglucanase EGaseA and inhibits the EGaseA-mediated release of
CC       elicitor-active glucan oligosaccharides from P.sojae cell walls
CC       (PubMed:12084830, PubMed:15545660). {ECO:0000269|PubMed:12084830,
CC       ECO:0000269|PubMed:15545660}.
CC   -!- SUBUNIT: Interacts with host endoglucanases EGaseA.
CC       {ECO:0000269|PubMed:12084830, ECO:0000269|PubMed:15545660}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12084830}.
CC   -!- INDUCTION: Expressed during pathogen infection.
CC       {ECO:0000269|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; AF406607; AAL11720.1; -; mRNA.
DR   RefSeq; XP_009538431.1; XM_009540136.1.
DR   RefSeq; XP_009538433.1; XM_009540138.1.
DR   RefSeq; XP_009538436.1; XM_009540141.1.
DR   AlphaFoldDB; Q945U0; -.
DR   SMR; Q945U0; -.
DR   GeneID; 20648150; -.
DR   GeneID; 20648153; -.
DR   GeneID; 20661580; -.
DR   KEGG; psoj:PHYSODRAFT_341789; -.
DR   KEGG; psoj:PHYSODRAFT_341794; -.
DR   KEGG; psoj:PHYSODRAFT_531224; -.
DR   VEuPathDB; FungiDB:PHYSODRAFT_341789; -.
DR   VEuPathDB; FungiDB:PHYSODRAFT_341794; -.
DR   VEuPathDB; FungiDB:PHYSODRAFT_531224; -.
DR   HOGENOM; CLU_006842_7_3_1; -.
DR   OrthoDB; 1314811at2759; -.
DR   PHI-base; PHI:652; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:12084830"
FT   CHAIN           29..257
FT                   /note="Glucanase inhibitor protein 1"
FT                   /id="PRO_5004320279"
FT   DOMAIN          29..256
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        213
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        181..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        201..232
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   257 AA;  26467 MW;  0BBB15E93BC48E53 CRC64;
     MKVFPALTSA LVALGTAGVE AEHVQRSLVM GGGTVPVGAK TYTVGLRTTA EGDTFCGGAL
     ISPTHVLTTA TCTASLGSGP AEWAAVGTHY LNGAKDGERL KVVSAQNHTL YNPNNFAYNF
     AVLTLEKPSK FSPVKLPAAD GSDIAPSMSS KLMGWGDTSY PNGARANELQ SVELRVVTSN
     CTYTVGPSEV CAGGEEGKDK CAGDTGGPLI KENGSGDADD ILIGLASWGM PCGHKDVASV
     YARVSAGLEW INSVIKK