ID   GIP2_NICBE              Reviewed;         439 AA.
AC   P0DO21;
DT   18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Probable aspartic proteinase GIP2 {ECO:0000305};
DE            EC=3.4.23.- {ECO:0000305};
DE   AltName: Full=Glucanase inhibitor protein 2 {ECO:0000303|PubMed:28082413};
DE            Short=NbGIP2 {ECO:0000303|PubMed:28082413};
DE   Flags: Precursor;
GN   Name=GIP2 {ECO:0000303|PubMed:28082413};
GN   ORFNames=Niben101Scf03191g04002 {ECO:0000305};
OS   Nicotiana benthamiana.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4100;
RN   [1]
RP   FUNCTION, INTERACTION WITH PHYTOPHTORA PARASITICA XYLOGLUCANASE XEG1 AND
RP   XLP1, AND SUBCELLULAR LOCATION.
RX   PubMed=28082413; DOI=10.1126/science.aai7919;
RA   Ma Z., Zhu L., Song T., Wang Y., Zhang Q., Xia Y., Qiu M., Lin Y., Li H.,
RA   Kong L., Fang Y., Ye W., Wang Y., Dong S., Zheng X., Tyler B.M., Wang Y.;
RT   "A paralogous decoy protects Phytophthora sojae apoplastic effector PsXEG1
RT   from a host inhibitor.";
RL   Science 355:710-714(2017).
CC   -!- FUNCTION: Involved in plant defense against Phytophtora parasitica
CC       (PubMed:28082413). Contributes positively to Nicotiana resistance
CC       against P.parasitica (PubMed:28082413). Binds the P.parasitica
CC       xyloglucanase XEG1 and inhibits its cell wall degrading enzyme activity
CC       and its contribution as P.parasitica virulence factor
CC       (PubMed:28082413). XEG1 acts as an important virulence factor during
CC       P.parasitica infection but also acts as a pathogen-associated molecular
CC       pattern (PAMP) in Nictotiana species, where it can trigger defense
CC       responses including cell death (PubMed:28082413).
CC       {ECO:0000269|PubMed:28082413}.
CC   -!- FUNCTION: (Microbial infection) Possesses stronger binding affinity
CC       with XLP1, a truncated paralog of P.parasitica XEG1 which has no enzyme
CC       activity. Is impaired in its inhibitor activity towards the
CC       P.parasitica xyloglucanase XEG1 when hijacked by XLP1 binding.
CC       {ECO:0000269|PubMed:28082413}.
CC   -!- SUBUNIT: Interacts with the Phytophtora parasitica xyloglucanase XEG1
CC       and xyloglucanase-like XLP1 (PubMed:28082413). Possesses stronger
CC       binding affinity with XLP1, a truncated paralog of P.parasitica XEG1
CC       which has no enzyme activity (PubMed:28082413).
CC       {ECO:0000269|PubMed:28082413}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305|PubMed:28082413}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103, ECO:0000305}.
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DR   AlphaFoldDB; P0DO21; -.
DR   SMR; P0DO21; -.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032799; TAXi_C.
DR   InterPro; IPR032861; TAXi_N.
DR   InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR   PANTHER; PTHR47965; PTHR47965; 1.
DR   Pfam; PF14541; TAXi_C; 1.
DR   Pfam; PF14543; TAXi_N; 1.
DR   SUPFAM; SSF50630; SSF50630; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   1: Evidence at protein level;
KW   Apoplast; Aspartyl protease; Glycoprotein; Hydrolase; Plant defense;
KW   Protease; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..439
FT                   /note="Probable aspartic proteinase GIP2"
FT                   /id="PRO_0000447892"
FT   DOMAIN          47..420
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        280
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        434
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   439 AA;  47214 MW;  6958435973D96D57 CRC64;
     MASSCCLHAI LLCSLLFITS TTAQSETSFR PKGLILPITK DALTLQYLTQ IQQRTPLVPV
     SLTLDLGGQF LWVDCDQGYV SSTYRPARCR SAQCSLAGAG SGCGQCFSPP KPGCNNNTCG
     LLPDNTITRT ATSGELASDT VQVQSSNGKN PGRHVSDKDF LFVCGSTFLL EGLASGVKGM
     AGLGRTRISL PSQFSAEFSF PRKFAVCLSS STNSKGVVLF GDGPYTFLPN REFANNDFSY
     TPLFINPVST ASAFSSREPS SEYFIGVKSI KINEKVVPIN TTLLSIDNQG VGGTKISTVN
     PYTILETSIY NAVTNFFVKE LVNITRVASV APFRACFDSR NIASTRVGPA VPSIDLVLQN
     ENVFWRIFGA NSMVQVSENV LCLGFVDGGV SPRTSIVVGG YTIEDNLLQF DLARSRLGFT
     SSILFRQTTC ANFNFTSIA