XTH15_ARATH
ID XTH15_ARATH Reviewed; 289 AA.
AC Q38911; O23272; Q5M726;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 15 {ECO:0000303|PubMed:12514239};
DE Short=At-XTH15 {ECO:0000303|PubMed:12514239};
DE Short=XTH-15 {ECO:0000303|PubMed:12514239};
DE EC=2.4.1.207 {ECO:0000269|PubMed:25446234};
DE EC=3.2.1.151 {ECO:0000269|PubMed:25446234};
DE Flags: Precursor;
GN Name=XTH15 {ECO:0000303|PubMed:12514239};
GN Synonyms=XTR7 {ECO:0000303|PubMed:8696366};
GN OrderedLocusNames=At4g14130 {ECO:0000312|Araport:AT4G14130};
GN ORFNames=dl3105c {ECO:0000312|EMBL:CAB10192.1},
GN FCAALL.173 {ECO:0000312|EMBL:CAB78455.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8696366; DOI=10.1046/j.1365-313x.1996.9060879.x;
RA Xu W., Campbell P., Vargheese A.K., Braam J.;
RT "The Arabidopsis XET-related gene family: environmental and hormonal
RT regulation of expression.";
RL Plant J. 9:879-889(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INDUCTION.
RX PubMed=11673616; DOI=10.1093/pcp/pce154;
RA Yokoyama R., Nishitani K.;
RT "A comprehensive expression analysis of all members of a gene family
RT encoding cell-wall enzymes allowed us to predict cis-regulatory regions
RT involved in cell-wall construction in specific organs of Arabidopsis.";
RL Plant Cell Physiol. 42:1025-1033(2001).
RN [9]
RP NOMENCLATURE.
RX PubMed=12514239; DOI=10.1093/pcp/pcf171;
RA Rose J.K.C., Braam J., Fry S.C., Nishitani K.;
RT "The XTH family of enzymes involved in xyloglucan endotransglucosylation
RT and endohydrolysis: current perspectives and a new unifying nomenclature.";
RL Plant Cell Physiol. 43:1421-1435(2002).
RN [10]
RP REGULATION BY FAR-RED LIGHT.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14645728; DOI=10.1104/pp.103.028480;
RA Hare P.D., Moller S.G., Huang L.-F., Chua N.-H.;
RT "LAF3, a novel factor required for normal phytochrome A signaling.";
RL Plant Physiol. 133:1592-1604(2003).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=16830179; DOI=10.1007/s11103-006-0021-z;
RA Becnel J., Natarajan M., Kipp A., Braam J.;
RT "Developmental expression patterns of Arabidopsis XTH genes reported by
RT transgenes and Genevestigator.";
RL Plant Mol. Biol. 61:451-467(2006).
RN [12]
RP INDUCTION BY ALUMINUM.
RX PubMed=21285327; DOI=10.1104/pp.111.172221;
RA Yang J.L., Zhu X.F., Peng Y.X., Zheng C., Li G.X., Liu Y., Shi Y.Z.,
RA Zheng S.J.;
RT "Cell wall hemicellulose contributes significantly to aluminum adsorption
RT and root growth in Arabidopsis.";
RL Plant Physiol. 155:1885-1892(2011).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=23776189; DOI=10.1104/pp.113.219147;
RA Zhu X.F., Lei G.J., Wang Z.W., Shi Y.Z., Braam J., Li G.X., Zheng S.J.;
RT "Coordination between apoplastic and symplastic detoxification confers
RT plant aluminum resistance.";
RL Plant Physiol. 162:1947-1955(2013).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=25446234; DOI=10.1016/j.phytochem.2014.09.020;
RA Shi Y.Z., Zhu X.F., Miller J.G., Gregson T., Zheng S.J., Fry S.C.;
RT "Distinct catalytic capacities of two aluminium-repressed Arabidopsis
RT thaliana xyloglucan endotransglucosylase/hydrolases, XTH15 and XTH31,
RT heterologously produced in Pichia.";
RL Phytochemistry 112:160-169(2015).
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. Has
CC a high XET activity, but little or no XEH activity in vitro. Acceptor
CC preferences are XXXGol > XLLGol = XLFGol > XXLGol > XXFGol.
CC {ECO:0000269|PubMed:25446234}.
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 Evidence={ECO:0000269|PubMed:25446234};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC Evidence={ECO:0000269|PubMed:25446234};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for XXXGol {ECO:0000269|PubMed:25446234};
CC Note=KM for xyloglucan as donor substrate is 2.87 mg/ml. KM is quoted
CC in mg/ml, not uM, because XTHs are able to utilise any segment of the
CC polysaccharide chain equally well, not just one site per molecule as
CC with the acceptor. {ECO:0000269|PubMed:25446234};
CC pH dependence:
CC Optimum pH is 6 for the XET activity. {ECO:0000269|PubMed:25446234};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in roots, hypocotyls and
CC cotyledons. Aslo detected in inflorescence stems and in the carpels and
CC styles in flowers. {ECO:0000269|PubMed:16830179}.
CC -!- INDUCTION: Down-regulated by auxin (PubMed:11673616). Down-regulated by
CC aluminum (PubMed:21285327). Repressed by far-red light (FRc)
CC (PubMed:14645728). {ECO:0000269|PubMed:11673616,
CC ECO:0000269|PubMed:14645728, ECO:0000269|PubMed:21285327}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible growth defects, but increased aluminum
CC resistance. {ECO:0000269|PubMed:23776189}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2
CC subfamily. {ECO:0000305}.
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DR EMBL; U43489; AAB18368.1; -; mRNA.
DR EMBL; Z97335; CAB10192.1; -; Genomic_DNA.
DR EMBL; AL161538; CAB78455.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83378.1; -; Genomic_DNA.
DR EMBL; AY045865; AAK76539.1; -; mRNA.
DR EMBL; BT020422; AAW28549.1; -; mRNA.
DR EMBL; AY087282; AAM64835.1; -; mRNA.
DR PIR; F71402; F71402.
DR RefSeq; NP_193149.2; NM_117490.4.
DR AlphaFoldDB; Q38911; -.
DR SMR; Q38911; -.
DR BioGRID; 12348; 1.
DR IntAct; Q38911; 1.
DR STRING; 3702.AT4G14130.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q38911; -.
DR PRIDE; Q38911; -.
DR ProteomicsDB; 242515; -.
DR EnsemblPlants; AT4G14130.1; AT4G14130.1; AT4G14130.
DR GeneID; 827051; -.
DR Gramene; AT4G14130.1; AT4G14130.1; AT4G14130.
DR KEGG; ath:AT4G14130; -.
DR Araport; AT4G14130; -.
DR TAIR; locus:2129445; AT4G14130.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q38911; -.
DR OMA; RPKIFKG; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q38911; -.
DR BioCyc; ARA:AT4G14130-MON; -.
DR BRENDA; 2.4.1.207; 399.
DR BRENDA; 3.2.1.151; 399.
DR SABIO-RK; Q38911; -.
DR PRO; PR:Q38911; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q38911; baseline and differential.
DR Genevisible; Q38911; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0030247; F:polysaccharide binding; ISS:UniProtKB.
DR GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase activity; IEA:UniProtKB-EC.
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:0010218; P:response to far red light; IEP:UniProtKB.
DR GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR CDD; cd02176; GH16_XET; 1.
DR InterPro; IPR044791; Beta-glucanase/XTH.
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 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; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..289
FT /note="Xyloglucan endotransglucosylase/hydrolase protein
FT 15"
FT /id="PRO_0000011815"
FT DOMAIN 26..216
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 106
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 119..121
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 129..131
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 195..196
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 200
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 275
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 104
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 224..230
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 270..284
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CONFLICT 70
FT /note="F -> V (in Ref. 2; CAB10192 and 3; CAB78455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 32687 MW; 3222ECF640792EF9 CRC64;
MGPSSSLTTI VATVLLVTLF GSAYASNFFD EFDLTWGDHR GKIFNGGNML SLSLDQVSGS
GFKSKKEYLF GRIDMQLKLV AGNSAGTVTA YYLSSQGATH DEIDFEFLGN ETGKPYVLHT
NVFAQGKGDR EQQFYLWFDP TKNFHTYSIV WRPQHIIFLV DNLPIRVFNN AEKLGVPFPK
SQPMRIYSSL WNADDWATRG GLVKTDWSKA PFTAYYRGFN AAACTASSGC DPKFKSSFGD
GKLQVATELN AYGRRRLRWV QKYFMIYNYC SDLKRFPRGF PPECKKSRV
