XTH19_ARATH
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 03-AUG-2022, entry version 142.
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}.
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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.AT4G30290.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q9M0D1; -.
DR PRIDE; Q9M0D1; -.
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; locus:2118751; AT4G30290.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q9M0D1; -.
DR OMA; IVMASLW; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q9M0D1; -.
DR BioCyc; ARA:AT4G30290-MON; -.
DR BRENDA; 2.4.1.207; 399.
DR PRO; PR:Q9M0D1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0D1; baseline and differential.
DR Genevisible; Q9M0D1; AT.
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 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; 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
