ID   GIP3_PHYSP              Reviewed;         261 AA.
AC   G5AE35;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Glucanase inhibitor protein 3 {ECO:0000303|PubMed:12084830};
DE   Flags: Precursor;
GN   Name=GIP3; ORFNames=PHYSODRAFT_532326;
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497;
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.-K.,
RA   McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K.C., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W.S., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
RN   [2]
RP   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; JH159164; EGZ06437.1; -; Genomic_DNA.
DR   RefSeq; XP_009538334.1; XM_009540039.1.
DR   AlphaFoldDB; G5AE35; -.
DR   SMR; G5AE35; -.
DR   EnsemblProtists; EGZ06437; EGZ06437; PHYSODRAFT_532326.
DR   GeneID; 20661728; -.
DR   KEGG; psoj:PHYSODRAFT_532326; -.
DR   InParanoid; G5AE35; -.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
KW   Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..261
FT                   /note="Glucanase inhibitor protein 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5003473302"
FT   DOMAIN          29..260
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        108
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        183..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        205..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   261 AA;  27446 MW;  6323EB3C4DCCD3A3 CRC64;
     MKVLSSLAAA LIALSAVDVE AEHVQRSLIL GGGKVPVGSK TYTVGLRTTP EGDTFCGGAL
     ISPTHVLTTA SCTAYEEGSS IPHWVAVGTH YLNGKKDGEQ LKIVSAQNHT LYDASSFSYN
     LAVLTLEKPS KFAPIKLPKA DGSDIFPRVW SKVMGWGVTS YPNGKPSNEL QSVDVRVWGD
     NACENKLGVD KSSLCAGGEA GKDSCVGDTG DPLIKENGRG DADDILLGLS GWGTGCGDKD
     MPSVYSRVSA GIEWINSVIK K