XIP_ORYSJ
ID XIP_ORYSJ Reviewed; 293 AA.
AC Q5WMW5;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Xylanase inhibitor protein XIP {ECO:0000305};
DE Short=OsXIP {ECO:0000303|PubMed:17379695};
DE AltName: Full=Class III chitinase homolog XIP {ECO:0000305};
DE Flags: Precursor;
GN Name=XIP {ECO:0000303|PubMed:17379695};
GN OrderedLocusNames=Os05g0247800 {ECO:0000312|EMBL:BAF16934.1},
GN LOC_Os05g15880 {ECO:0000305};
GN ORFNames=OJ1037_G10.8 {ECO:0000312|EMBL:AAV32103.1},
GN OsJ_17793 {ECO:0000312|EMBL:EEE62985.1};
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=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(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 GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
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 [7]
RP FUNCTION, AND 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).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18511458; DOI=10.1093/pcp/pcn080;
RA Tokunaga T., Miyata Y., Fujikawa Y., Esaka M.;
RT "RNAi-mediated knockdown of the XIP-type endoxylanase inhibitor gene,
RT OsXIP, has no effect on grain development and germination in rice.";
RL Plant Cell Physiol. 49:1122-1127(2008).
CC -!- FUNCTION: Fungal xylanase inhibitor (PubMed:17379695, PubMed:18511458).
CC Possesses competitive inhibiting activity against several fungal endo-
CC 1,4-beta-D-xylanases belonging to glycoside hydrolase family 10 (GH10)
CC and family 11 (GH11) (PubMed:17379695, PubMed:18511458). May function
CC in plant defense against secreted fungal pathogen xylanases
CC (PubMed:17379695, PubMed:18511458). Is similar to class III chitinases,
CC but does not exhibit chitinase activity (PubMed:17379695,
CC PubMed:18511458). {ECO:0000269|PubMed:17379695,
CC ECO:0000269|PubMed:18511458}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18511458}.
CC -!- TISSUE SPECIFICITY: Expressed in mature grain.
CC {ECO:0000269|PubMed:18511458}.
CC -!- INDUCTION: Induced by exogenous treatment with ascorbate,
CC dehydroascorbate, citrate, sodium chloride and methyl jasmonate in
CC roots (PubMed:17379695). Induced by wounding in roots
CC (PubMed:17379695). {ECO:0000269|PubMed:17379695}.
CC -!- MISCELLANEOUS: Plants silencing XIP do not exhibit visible phenotype
CC under normal growth conditions. {ECO:0000269|PubMed:18511458}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Xylanase
CC inhibitor subfamily. {ECO:0000305}.
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DR EMBL; AC104270; AAV32103.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16934.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS93008.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE62985.1; -; Genomic_DNA.
DR EMBL; AK073843; BAG93671.1; -; mRNA.
DR RefSeq; XP_015638416.1; XM_015782930.1.
DR AlphaFoldDB; Q5WMW5; -.
DR SMR; Q5WMW5; -.
DR STRING; 4530.OS05T0247800-01; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR PaxDb; Q5WMW5; -.
DR PRIDE; Q5WMW5; -.
DR EnsemblPlants; Os05t0247800-01; Os05t0247800-01; Os05g0247800.
DR GeneID; 4338211; -.
DR Gramene; Os05t0247800-01; Os05t0247800-01; Os05g0247800.
DR KEGG; osa:4338211; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_007818_0_1_1; -.
DR InParanoid; Q5WMW5; -.
DR OMA; DKEAYMS; -.
DR OrthoDB; 1087812at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW Disulfide bond; Plant defense; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..293
FT /note="Xylanase inhibitor protein XIP"
FT /id="PRO_5015098067"
FT DOMAIN 31..293
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT DISULFID 50..92
FT /evidence="ECO:0000250|UniProtKB:Q8L5C6"
FT DISULFID 189..218
FT /evidence="ECO:0000250|UniProtKB:Q8L5C6"
SQ SEQUENCE 293 AA; 32436 MW; B08E5B66FDD82B11 CRC64;
MALRRLAALL SLAVLLSAGL AAVSATSQNT GDTVIIWGRN KDEGSLREAC DAGRYTTVII
SFLSAFGYIP GTYKLDISGH QVSAVGPDIK YCQSKGKLIL LAIGGQGGEY SLPSSQAAVD
LHDHLWYSYL GGRRNGVYRP FGDANVNGID FFIDQGAREH YNELAKMLYD HNKDYRATVG
VMVTATTRCG YPDHRLDEAL ATGLFHRIHV KMFSDGRCPA WSRRQSFEKW AKTYPQSRVL
IGVVASPDVD KDAYMPPEAL NNLLQFINKQ PNFGGVMVWD RFYDKKTGFT AHL
