GIP1_SOYBN
ID GIP1_SOYBN Reviewed; 427 AA.
AC I1JNS6;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Probable aspartic proteinase GIP1 {ECO:0000305};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Glucanase inhibitor protein 1 {ECO:0000303|PubMed:28082413};
DE Short=GmGIP1 {ECO:0000303|PubMed:28082413};
DE Flags: Precursor;
GN Name=GIP1 {ECO:0000303|PubMed:28082413};
GN ORFNames=GLYMA_03G151900 {ECO:0000312|EMBL:KRH67173.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82;
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2]
RP FUNCTION.
RX PubMed=26163574; DOI=10.1105/tpc.15.00390;
RA Ma Z., Song T., Zhu L., Ye W., Wang Y., Shao Y., Dong S., Zhang Z., Dou D.,
RA Zheng X., Tyler B.M., Wang Y.;
RT "A Phytophthora sojae glycoside hydrolase 12 protein is a major virulence
RT factor during soybean infection and is recognized as a PAMP.";
RL Plant Cell 27:2057-2072(2015).
RN [3]
RP FUNCTION, INTERACTION WITH PHYTOPHTORA SOJAE XYLOGLUCANASE XEG1 AND XLP1,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-408; LEU-409; ASP-411;
RP LYS-413; SER-415 AND ASN-416.
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 sojae
CC (PubMed:28082413). Contributes positively to soybean resistance against
CC P.sojae (PubMed:28082413). Binds the P.sojae xyloglucanase XEG1 and
CC inhibits its cell wall degrading enzyme activity and its contribution
CC as P.sojae virulence factor (PubMed:28082413). XEG1 acts as an
CC important virulence factor during P.sojae infection but also acts as a
CC pathogen-associated molecular pattern (PAMP) in soybean and solanaceous
CC species, where it can trigger defense responses including cell death
CC (PubMed:26163574). {ECO:0000269|PubMed:26163574,
CC ECO:0000269|PubMed:28082413}.
CC -!- FUNCTION: (Microbial infection) Possesses stronger binding affinity
CC with XLP1, a truncated paralog of P.sojae XEG1 which has no enzyme
CC activity. Is impaired in its inhibitor activity towards the P.sojae
CC xyloglucanase XEG1 when hijacked by XLP1 binding.
CC {ECO:0000269|PubMed:28082413}.
CC -!- SUBUNIT: Interacts with the Phytophtora sojae xyloglucanase XEG1 and
CC xyloglucanase-like XLP1 (PubMed:28082413). Possesses stronger binding
CC affinity with XLP1, a truncated paralog of P.sojae XEG1 which has no
CC enzyme activity (PubMed:28082413). {ECO:0000269|PubMed:28082413}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000305|PubMed:28082413}.
CC -!- MISCELLANEOUS: Plants silencing GIP1 display significantly increased
CC susceptibility to infection by Phytophtora sojae, and plants over-
CC expressing GIP1 show increased resistance.
CC {ECO:0000269|PubMed:28082413}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103, ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Lure - Issue 218 of October
CC 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/218/";
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DR EMBL; CM000836; KRH67173.1; -; Genomic_DNA.
DR RefSeq; XP_003520561.1; XM_003520513.3.
DR AlphaFoldDB; I1JNS6; -.
DR SMR; I1JNS6; -.
DR STRING; 3847.GLYMA03G30860.1; -.
DR PRIDE; I1JNS6; -.
DR EnsemblPlants; KRH67173; KRH67173; GLYMA_03G151900.
DR GeneID; 100800584; -.
DR Gramene; KRH67173; KRH67173; GLYMA_03G151900.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_032185_0_0_1; -.
DR InParanoid; I1JNS6; -.
DR OMA; TYQHIPC; -.
DR OrthoDB; 584584at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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 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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..427
FT /note="Probable aspartic proteinase GIP1"
FT /id="PRO_5014577186"
FT DOMAIN 41..404
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 408
FT /note="L->A: Almost abolishes the interaction with XEG1;
FT when associated with A-409; A-411; A-413; A-415 and A-416."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 409
FT /note="L->A: Almost abolishes the interaction with XEG1;
FT when associated with A-408; A-411; A-413; A-415 and A-416."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 411
FT /note="D->A: Almost abolishes the interaction with XEG1;
FT when associated with A-408; A-409; A-413; A-415 and A-416."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 413
FT /note="K->A: Almost abolishes the interaction with XEG1;
FT when associated with A-408; A-409; A-411; A-415 and A-416."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 415
FT /note="S->A: Almost abolishes the interaction with XEG1;
FT when associated with A-408; A-409; A-411; A-413 and A-416."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 416
FT /note="N->A: Almost abolishes the interaction with XEG1;
FT when associated with A-408; A-409; A-411; A-413 and A-415."
FT /evidence="ECO:0000269|PubMed:28082413"
SQ SEQUENCE 427 AA; 45958 MW; 524375CD09E61D72 CRC64;
MPPPLPSLCN FNLAILFLFL TPTFQIPLIA PISKDDTTQL YTLSVFLKTP LQPTKLHLHL
GSSLSWVLCD STYTSSSSHH IPCNTPLCNS FPSNACSNNS SLCALFPENP VTRNTLLDTA
LIDSLALPTY DASSSLVLIS DFIFSCATAH LLQGLAANAL GLASLGRSNY SLPAQISTSL
TSPRSFTLCL PASSANTGAA IFASTASSFL FSSKIDLTYT QLIVNPVADT VVTDNPQPSD
EYFINLTSIK INGKPLYINS SILTVDQTGF GGTKISTAEP YTVLETSIYR LFVQRFVNES
SAFNLTVTEA VEPFGVCYPA GDLTETRVGP AVPTVDLVMH SEDVFWRIFG GNSMVRVAKG
GVDVWCLGFV DGGTRGRTPI VIGGHQLEDN LMQFDLDSNR FGFTSTLLLQ DAKCSNLKVN
NFANGIK
