ID   XTH8_ORYSJ              Reviewed;         290 AA.
AC   Q76BW5; Q0J732; Q7M1Y6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Xyloglucan endotransglycosylase/hydrolase protein 8;
DE            EC=2.4.1.207;
DE   AltName: Full=End-xyloglucan transferase;
DE   AltName: Full=OsXRT5;
DE   AltName: Full=OsXTH8;
DE   Flags: Precursor;
GN   Name=XTH8; Synonyms=XRT5;
GN   OrderedLocusNames=Os08g0237000, LOC_Os08g13920; ORFNames=P0682A06.17;
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 [MRNA].
RC   STRAIN=cv. Koshihikari;
RA   Aoki T., Kameya N., Nakamura I.;
RT   "A cDNA clone from rice accelerated overgrowth (ao) mutant encoding
RT   xyloglucanrelated protein homolog.";
RL   Rice Genet. Newsl. 14:133-136(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Gimbozu, and cv. Nipponbare;
RX   PubMed=15516498; DOI=10.1104/pp.104.052274;
RA   Jan A., Yang G., Nakamura H., Ichikawa H., Kitano H., Matsuoka M.,
RA   Matsumoto H., Komatsu S.;
RT   "Characterization of a xyloglucan endotransglucosylase gene that is up-
RT   regulated by gibberellin in rice.";
RL   Plant Physiol. 136:3670-3681(2004).
RN   [3]
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   [4]
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   [5]
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   [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   PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 26-32, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16758443; DOI=10.1002/pmic.200600043;
RA   Nozu Y., Tsugita A., Kamijo K.;
RT   "Proteomic analysis of rice leaf, stem and root tissues during growth
RT   course.";
RL   Proteomics 6:3665-3670(2006).
RN   [8]
RP   GENE FAMILY, AND LEVEL OF PROTEIN EXPRESSION.
RX   PubMed=14988479; DOI=10.1104/pp.103.035261;
RA   Yokoyama R., Rose J.K.C., Nishitani K.;
RT   "A surprising diversity and abundance of xyloglucan
RT   endotransglucosylase/hydrolases in rice. Classification and expression
RT   analysis.";
RL   Plant Physiol. 134:1088-1099(2004).
CC   -!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
CC       endotransglycosylation (XET). Cleaves and religates xyloglucan
CC       polymers, an essential constituent of the primary cell wall, and
CC       thereby participates in cell wall construction of growing tissues (By
CC       similarity). May promote elongation of three internodes (II, III and
CC       IV) and may be involved in cell elongation processes. {ECO:0000250,
CC       ECO:0000269|PubMed:15516498}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=breaks a beta-(1->4) bond in the backbone of a xyloglucan and
CC         transfers the xyloglucanyl segment on to O-4 of the non-reducing
CC         terminal glucose residue of an acceptor, which can be a xyloglucan or
CC         an oligosaccharide of xyloglucan.; EC=2.4.1.207;
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC       extracellular space, apoplast {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Transcript strongly detected in leaf sheaths.
CC       Weakly or not expressed in leaf blades, roots and calli. Accumulation
CC       of transcript detected in shoot apex meristem, vascular tissues, young
CC       leaves, vascular bundles of leaf sheaths, and peripheral cylinder of
CC       the vascular bundles and fibers in the nodal region.
CC       {ECO:0000269|PubMed:15516498}.
CC   -!- INDUCTION: By gibberellic acid (GA3). Accumulation continues to
CC       increase throughout 24 hours of GA3 treatment. Very little effect by
CC       other plant hormones like brassinolide (BL), 6-benzyladenine (BA),
CC       indole-3-acetic acid (IAA), and abscisic acid (ABA). Inhibitory effect
CC       from uniconazole, a potent GA biosynthesis inhibitor.
CC       {ECO:0000269|PubMed:15516498}.
CC   -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC       enzymatic activity. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Plants exhibit up to 50% growth reduction when
CC       they reach maturity. {ECO:0000269|PubMed:15516498}.
CC   -!- MISCELLANEOUS: Lower level of XTH8 transcript detected in Tanginbozu, a
CC       GA-deficient semidwarf mutant, and higher level detected in Slender
CC       rice 1 (slr1), a GA-insensitive mutant showing a constitutive GA-
CC       response phenotype.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB110604; BAD06579.1; -; mRNA.
DR   EMBL; AP004705; BAD05469.1; -; Genomic_DNA.
DR   EMBL; AP008214; BAF23233.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT04470.1; -; Genomic_DNA.
DR   EMBL; AK060654; BAG87527.1; -; mRNA.
DR   EMBL; AK104451; BAG96694.1; -; mRNA.
DR   PIR; JE0156; JE0156.
DR   RefSeq; XP_015650689.1; XM_015795203.1.
DR   AlphaFoldDB; Q76BW5; -.
DR   SMR; Q76BW5; -.
DR   STRING; 39947.Q76BW5; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q76BW5; 1 site, No reported glycans.
DR   PaxDb; 39947-Q76BW5; -.
DR   EnsemblPlants; Os08t0237000-01; Os08t0237000-01; Os08g0237000.
DR   GeneID; 4345019; -.
DR   Gramene; Os08t0237000-01; Os08t0237000-01; Os08g0237000.
DR   KEGG; osa:4345019; -.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_048041_0_1_1; -.
DR   InParanoid; Q76BW5; -.
DR   OMA; CPAGANE; -.
DR   OrthoDB; 339493at2759; -.
DR   BRENDA; 2.4.1.207; 4460.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; ISS:UniProtKB.
DR   GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR   CDD; cd02176; GH16_XET; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR008264; Beta_glucanase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   InterPro; IPR010713; XET_C.
DR   InterPro; IPR016455; XTH.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF45; XYLOGLUCAN ENDOTRANSGLYCOSYLASE_HYDROLASE PROTEIN 8; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF06955; XET_C; 1.
DR   PIRSF; PIRSF005604; XET; 1.
DR   PRINTS; PR00737; GLHYDRLASE16.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
DR   Genevisible; Q76BW5; OS.
PE   1: Evidence at protein level;
KW   Apoplast; Cell wall; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Reference proteome; Secreted; Signal; Transferase.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:16758443"
FT   CHAIN           26..290
FT                   /note="Xyloglucan endotransglycosylase/hydrolase protein 8"
FT                   /id="PRO_0000011836"
FT   DOMAIN          26..218
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        110
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   BINDING         110
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         123..125
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         133..135
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         197..198
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         278
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            108
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        226..240
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   DISULFID        273..287
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CONFLICT        249..290
FT                   /note="HRELDGAELGTVAWAERNYMSYNYCADGWRFPQGFPAECYRK -> KKKKTK
FT                   TKTKTRTRSNYKSLPRTHQWRRI (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   290 AA;  32097 MW;  26F294BA0E0AC11B CRC64;
     MAKHLALSVA AAVAVSWLAA SSAAAAGFYE KFDVVGAGDH VRVVSDDGKT QQVALTLDRS
     SGSGFTSKDT YLFGEFSVQM KLVGGNSAGT VTSFYLSSGE GDGHDEIDIE FMGNLSGNPY
     VMNTNVWANG DGKKEHQFYL WFDPTADFHT YKIIWNPQNI IFQVDDVPVR TFKKYDDLAY
     PQSKPMRLHA TLWDGSYWAT RHGDVKIDWS GAPFVVSYRG YSTNACVNNN PAGGWSSSWC
     PEGTSAWIHR ELDGAELGTV AWAERNYMSY NYCADGWRFP QGFPAECYRK
//