XTH8_ORYSJ
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 03-AUG-2022, entry version 112.
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; OrderedLocusNames=Os08g0237000, LOC_Os08g13920;
GN 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; 4530.OS08T0237000-01; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q76BW5; -.
DR PRIDE; 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; GSDAWMS; -.
DR OrthoDB; 1209387at2759; -.
DR BRENDA; 2.4.1.207; 4460.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; Q76BW5; OS.
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 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; PTHR31062; 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; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
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
