ID   GIP2_PHYIN              Reviewed;         256 AA.
AC   B1AC87;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Glucanase inhibitor protein 2 {ECO:0000303|PubMed:18624645};
DE   Flags: Precursor;
GN   Name=GIP2 {ECO:0000303|PubMed:18624645};
OS   Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH HOST ENDOGLUCANASES.
RC   STRAIN=US970001;
RX   PubMed=18624645; DOI=10.1094/mpmi-21-6-0820;
RA   Damasceno C.M., Bishop J.G., Ripoll D.R., Win J., Kamoun S., Rose J.K.;
RT   "Structure of the glucanase inhibitor protein (GIP) family from
RT   phytophthora species suggests coevolution with plant endo-beta-1,3-
RT   glucanases.";
RL   Mol. Plant Microbe Interact. 21:820-830(2008).
CC   -!- FUNCTION: Secreted effector that suppresses host plant glucan elicitor-
CC       mediated defense responses (PubMed:18624645). Targets host
CC       endoglucanases and inhibits the endoglucanase-mediated release of
CC       elicitor-active glucan oligosaccharides from P.infestans cell walls
CC       (PubMed:18624645). {ECO:0000269|PubMed:18624645}.
CC   -!- SUBUNIT: Forms an apoplastic complex with host endoglucanases in tomato
CC       leaves during P.infestans infection. {ECO:0000269|PubMed:18624645}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18624645}.
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:18624645}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU443392; ACA23210.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1AC87; -.
DR   SMR; B1AC87; -.
DR   VEuPathDB; FungiDB:PITG_13641; -.
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   Disulfide bond; Glycoprotein; Secreted; Signal; Virulence.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..256
FT                   /note="Glucanase inhibitor protein 2"
FT                   /id="PRO_0000448095"
FT   DOMAIN          27..254
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        54..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        177..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        199..230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   256 AA;  26763 MW;  76AC5D2FF60B426F CRC64;
     MKLISTIAAA TTAFGAPNAD HTSRQLIFGG GIIPSGTKTY TAGIRTSADG DTYCGGSLIS
     PTHVLTTSIC TGYKEPKFVS VGTHYLNGTQ DGEQIKVVSA QNHTSLNFSS GTYDFALLTL
     EKPSKFIPVK LPKADDSDIK PGMWSKAMGW GVTSYPNGSL SYELQGVSLE VWANDECSQV
     FNIGDTSVCA GGLPGKDACV ADTGGPLIKE NGLGDLDDIL IGLVNWGYGC GDAGSPTVYS
     RVSTATEWIN SVTKGQ