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 27-MAR-2024, entry version 163. 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}, FCAALL.173 GN {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q38911; -. DR CAZy; GH16; Glycoside Hydrolase Family 16. DR GlyCosmos; Q38911; 1 site, No reported glycans. DR PaxDb; 3702-AT4G14130-1; -. 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; AT4G14130; XTH15. DR eggNOG; ENOG502QQ71; Eukaryota. DR HOGENOM; CLU_048041_0_0_1; -. DR InParanoid; Q38911; -. DR OMA; EWHTNAL; -. DR OrthoDB; 337487at2759; -. DR PhylomeDB; Q38911; -. DR BioCyc; ARA:AT4G14130-MONOMER; -. 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 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 Gene3D; 2.60.120.200; -; 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; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1. DR PANTHER; PTHR31062:SF176; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 15; 1. DR Pfam; PF00722; Glyco_hydro_16; 1. DR Pfam; PF06955; XET_C; 1. DR PIRSF; PIRSF005604; XET; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS01034; GH16_1; 1. DR PROSITE; PS51762; GH16_2; 1. DR Genevisible; Q38911; AT. 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 //