XIP2_ORYSJ
ID XIP2_ORYSJ Reviewed; 290 AA.
AC Q53NL5; A0A0P0Y5Q2; Q2QZ66; Q9SXY5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Xylanase inhibitor protein 2 {ECO:0000303|PubMed:15895691};
DE AltName: Full=Class III chitinase homolog h {ECO:0000305};
DE Flags: Precursor;
GN Name=Chib3H-h {ECO:0000305};
GN OrderedLocusNames=Os11g0701100 {ECO:0000312|EMBL:BAT15365.1},
GN LOC_Os11g47520 {ECO:0000312|EMBL:ABA95475.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-147.
RC STRAIN=cv. Nipponbare; TISSUE=Callus;
RX PubMed=9501993; DOI=10.1093/dnares/4.6.379;
RA Nagasaki H., Yamamoto K., Shomura A., Koga-Ban Y., Takasuga A., Yano M.,
RA Minobe Y., Sasaki T.;
RT "Rice class III chitinase homologues isolated by random cloning of rice
RT cDNAs.";
RL DNA Res. 4:379-385(1997).
RN [7]
RP PROTEIN SEQUENCE OF 28-57, AND FUNCTION.
RX PubMed=15895691; DOI=10.1080/14756360400002080;
RA Goesaert H., Gebruers K., Courtin C.M., Delcour J.A.;
RT "Purification and characterization of a XIP-type endoxylanase inhibitor
RT from rice (Oryza sativa).";
RL J. Enzym. Inhib. Med. Chem. 20:95-101(2005).
RN [8]
RP INDUCTION.
RX PubMed=17379695; DOI=10.1093/pcp/pcm038;
RA Tokunaga T., Esaka M.;
RT "Induction of a novel XIP-type xylanase inhibitor by external ascorbic acid
RT treatment and differential expression of XIP-family genes in rice.";
RL Plant Cell Physiol. 48:700-714(2007).
CC -!- FUNCTION: Fungal xylanase inhibitor. Possesses competitive inhibiting
CC activity against several fungal endo-1,4-beta-D-xylanases belonging to
CC glycoside hydrolase family 10 (GH10) and family 11 (GH11). May function
CC in plant defense against secreted fungal pathogen xylanases. Is similar
CC to class III chitinases, but does not exhibit chitinase activity.
CC {ECO:0000269|PubMed:15895691}.
CC -!- SUBUNIT: Binds to fungal GH10 xylanases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- INDUCTION: Induced by wounding and methyl jasmonate in roots.
CC {ECO:0000269|PubMed:17379695}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Xylanase
CC inhibitor subfamily. {ECO:0000305}.
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DR EMBL; AC134045; AAX95330.1; -; Genomic_DNA.
DR EMBL; DP000010; ABA95475.1; -; Genomic_DNA.
DR EMBL; AP008217; BAF28883.1; -; Genomic_DNA.
DR EMBL; AP014967; BAT15365.1; -; Genomic_DNA.
DR EMBL; AK064356; BAG89082.1; -; mRNA.
DR EMBL; AB027427; BAA77780.1; -; mRNA.
DR RefSeq; XP_015617733.1; XM_015762247.1.
DR AlphaFoldDB; Q53NL5; -.
DR SMR; Q53NL5; -.
DR STRING; 4530.OS11T0701100-01; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; Q53NL5; -.
DR PRIDE; Q53NL5; -.
DR EnsemblPlants; Os11t0701100-01; Os11t0701100-01; Os11g0701100.
DR GeneID; 4351187; -.
DR Gramene; Os11t0701100-01; Os11t0701100-01; Os11g0701100.
DR KEGG; osa:4351187; -.
DR eggNOG; KOG4701; Eukaryota.
DR InParanoid; Q53NL5; -.
DR OMA; CTMSPRY; -.
DR OrthoDB; 923272at2759; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR ExpressionAtlas; Q53NL5; baseline and differential.
DR Genevisible; Q53NL5; OS.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Plant defense;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:15895691"
FT CHAIN 28..290
FT /note="Xylanase inhibitor protein 2"
FT /id="PRO_0000011992"
FT DOMAIN 30..290
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 49..89
FT /evidence="ECO:0000250|UniProtKB:Q8L5C6"
FT DISULFID 187..216
FT /evidence="ECO:0000250|UniProtKB:Q8L5C6"
FT CONFLICT 145..147
FT /note="DGI -> ELQ (in Ref. 6; BAA77780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31654 MW; 0BA3E44427A9E4FF CRC64;
MGLVHALLPF AAAAALLLLA APPPATADDP GLAVYWGRHK EEGSLREACD TGRYTTVIIT
FYNAFGHGRY SLDISGHPLA AVGADIKHCQ SRGITVLLSI GGQGGAYSLP TNASAADVAD
NLWNAYLGGH RAGVARPFGD DAAVDGIDFF IDQGGADHYD DLARRLDGYN KYYRGRVGVL
LTATTRCSYP DHRLEKALAT GVFARIHVRM FGDEQCTMSP RYSWEKWAAA FPGSKVYIGL
VASPEQDSAW MFQKDLYYEM LQFVRSLPNY GGLAIYDRYF DKKANYTGEG
