ID XTH19_ARATH Reviewed; 277 AA. AC Q9M0D1; Q94A49; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 148. DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 19 {ECO:0000305}; DE Short=At-XTH19 {ECO:0000303|PubMed:12514239}; DE Short=XTH-19 {ECO:0000303|PubMed:12514239}; DE EC=2.4.1.207 {ECO:0000269|PubMed:20732879}; DE Flags: Precursor; GN Name=XTH19 {ECO:0000303|PubMed:25182467}; OrderedLocusNames=At4g30290; GN ORFNames=F17I23.370; 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 [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 [2] 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 [3] 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 [4] RP TISSUE SPECIFICITY, AND 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 [5] 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 [6] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=20732879; DOI=10.1093/jxb/erq263; RA Maris A., Kaewthai N., Ekloef J.M., Miller J.G., Brumer H., Fry S.C., RA Verbelen J.P., Vissenberg K.; RT "Differences in enzymic properties of five recombinant xyloglucan RT endotransglucosylase/hydrolase (XTH) proteins of Arabidopsis thaliana."; RL J. Exp. Bot. 62:261-271(2011). RN [7] RP FUNCTION. RX PubMed=23585673; DOI=10.1093/jxb/ert107; RA Miedes E., Suslov D., Vandenbussche F., Kenobi K., Ivakov A., RA Van Der Straeten D., Lorences E.P., Mellerowicz E.J., Verbelen J.P., RA Vissenberg K.; RT "Xyloglucan endotransglucosylase/hydrolase (XTH) overexpression affects RT growth and cell wall mechanics in etiolated Arabidopsis hypocotyls."; RL J. Exp. Bot. 64:2481-2497(2013). RN [8] RP FUNCTION. RX PubMed=25182467; DOI=10.1111/tpj.12654; RA Pitaksaringkarn W., Matsuoka K., Asahina M., Miura K., Sage-Ono K., Ono M., RA Yokoyama R., Nishitani K., Ishii T., Iwai H., Satoh S.; RT "XTH20 and XTH19 regulated by ANAC071 under auxin flow are involved in cell RT proliferation in incised Arabidopsis inflorescence stems."; RL Plant J. 80:604-614(2014). CC -!- FUNCTION: Possesses xyloglucan endotransglucosylase (XET) activity in CC vitro. Does not possess xyloglucan endohydrolysis (XEH) activity CC (PubMed:20732879). Cleaves and religates xyloglucan polymers, an CC essential constituent of the primary cell wall, and thereby CC participates in cell wall construction of growing tissues CC (PubMed:23585673). Involved in cell proliferation in the tissue reunion CC process of wounded inflorescence stems. Maybe a downstream target of CC NAC071 as a consequence of auxin action in wounded stems CC (PubMed:25182467). {ECO:0000269|PubMed:20732879, CC ECO:0000269|PubMed:25182467, ECO:0000305|PubMed:23585673}. 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:20732879}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:20732879}; CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted, CC extracellular space, apoplast {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Root specific. {ECO:0000269|PubMed:11673616}. CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:11673616}. CC -!- PTM: Contains at least one intrachain disulfide bond essential for its CC enzymatic activity. {ECO:0000250}. 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; AL161576; CAB81022.1; -; Genomic_DNA. DR EMBL; CP002687; AEE85747.1; -; Genomic_DNA. DR EMBL; AY050373; AAK91391.1; -; mRNA. DR EMBL; AY143887; AAN28826.1; -; mRNA. DR PIR; B85354; B85354. DR RefSeq; NP_194758.1; NM_119175.3. DR AlphaFoldDB; Q9M0D1; -. DR SMR; Q9M0D1; -. DR STRING; 3702.Q9M0D1; -. DR CAZy; GH16; Glycoside Hydrolase Family 16. DR GlyCosmos; Q9M0D1; 1 site, No reported glycans. DR PaxDb; 3702-AT4G30290-1; -. DR ProteomicsDB; 242516; -. DR EnsemblPlants; AT4G30290.1; AT4G30290.1; AT4G30290. DR GeneID; 829152; -. DR Gramene; AT4G30290.1; AT4G30290.1; AT4G30290. DR KEGG; ath:AT4G30290; -. DR Araport; AT4G30290; -. DR TAIR; AT4G30290; XTH19. DR eggNOG; ENOG502QQ71; Eukaryota. DR HOGENOM; CLU_048041_0_0_1; -. DR InParanoid; Q9M0D1; -. DR OMA; IVMASLW; -. DR OrthoDB; 643704at2759; -. DR PhylomeDB; Q9M0D1; -. DR BioCyc; ARA:AT4G30290-MONOMER; -. DR BRENDA; 2.4.1.207; 399. DR PRO; PR:Q9M0D1; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q9M0D1; baseline and differential. 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; IDA:TAIR. DR GO; GO:0051301; P:cell division; IMP:TAIR. DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0071365; P:cellular response to auxin stimulus; IEP:TAIR. DR GO; GO:0010411; P:xyloglucan metabolic process; IDA:TAIR. 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:SF157; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 19-RELATED; 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; Q9M0D1; 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..21 FT /evidence="ECO:0000255" FT CHAIN 22..277 FT /note="Xyloglucan endotransglucosylase/hydrolase protein FT 19" FT /id="PRO_0000011819" FT DOMAIN 22..213 FT /note="GH16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098" FT ACT_SITE 99 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT ACT_SITE 103 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064" FT BINDING 103 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 116..118 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 126..128 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 192..193 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 197 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT BINDING 267 FT /ligand="xyloglucan" FT /ligand_id="ChEBI:CHEBI:18233" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT SITE 101 FT /note="Important for catalytic activity" FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT CARBOHYD 107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 221..230 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT DISULFID 262..276 FT /evidence="ECO:0000250|UniProtKB:Q8GZD5" FT CONFLICT 112 FT /note="P -> T (in Ref. 3; AAK91391/AAN28826)" FT /evidence="ECO:0000305" SQ SEQUENCE 277 AA; 31563 MW; B801F67E0CD72E53 CRC64; MKSFTFLILF LFAAQSISVY AGSFHKDVKI HWGDGRGKIH DNQGKLLSLS LDKSSGSGFQ SNQEFLYGKA EVQMKLVPGN SAGTVTTFYL KSPGTTWDEI DFEFLGNISG HPYTLHTNVY TKGSGDKEQQ FHLWFDPTAN FHTYCITWNP QRIIFTVDGI PIREFMNAES RGVPFPTKQP MRLYASLWEA EHWATRGGLE KTDWSKAPFT AYYRNYNVEG CVWVNGKSVC PANSQWFTQK LDSNGQTRMK GVQSKYMVYN YCSDKKRFPR GVPPECS //