XTH22_ARATH
ID XTH22_ARATH Reviewed; 284 AA.
AC Q38857; Q8H783;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 22;
DE Short=At-XTH22;
DE Short=XTH-22;
DE EC=2.4.1.207;
DE AltName: Full=Touch protein 4;
DE Flags: Precursor;
GN Name=XTH22; Synonyms=TCH4; OrderedLocusNames=At5g57560; ORFNames=MUA2.13;
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7580251; DOI=10.2307/3870019;
RA Xu W., Purugganan M.M., Polisensky D.H., Antosiewicz D.M., Fry S.C.,
RA Braam J.;
RT "Arabidopsis TCH4, regulated by hormones and the environment, encodes a
RT xyloglucan endotransglycosylase.";
RL Plant Cell 7:1555-1567(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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] OF 1-121.
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ACTIVITY REGULATION.
RX PubMed=9306698; DOI=10.1104/pp.115.1.181;
RA Purugganan M.M., Braam J., Fry S.C.;
RT "The Arabidopsis TCH4 xyloglucan endotransglycosylase. Substrate
RT specificity, pH optimum, and cold tolerance.";
RL Plant Physiol. 115:181-190(1997).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=9414546; DOI=10.1104/pp.115.4.1319;
RA Antosiewicz D.M., Purugganan M.M., Polisensky D.H., Braam J.;
RT "Cellular localization of Arabidopsis xyloglucan endotransglycosylase-
RT related proteins during development and after wind stimulation.";
RL Plant Physiol. 115:1319-1328(1997).
RN [9]
RP GLYCOSYLATION, DISULFIDE BOND, AND MUTAGENESIS OF GLU-97.
RX PubMed=9753780; DOI=10.1046/j.1365-313x.1998.00239.x;
RA Campbell P., Braam J.;
RT "Co- and/or post-translational modifications are critical for TCH4 XET
RT activity.";
RL Plant J. 15:553-561(1998).
RN [10]
RP ENZYME ACTIVITY, AND GLYCOSYLATION.
RX PubMed=10406121; DOI=10.1046/j.1365-313x.1999.00459.x;
RA Campbell P., Braam J.;
RT "In vitro activities of four xyloglucan endotransglycosylases from
RT Arabidopsis.";
RL Plant J. 18:371-382(1999).
RN [11]
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 [12]
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).
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. Its
CC induction in case of mechanical stress, suggests that it may contribute
CC in the adaptive changes in morphogenesis by being recruited to alter
CC tissues tensil strength, or flexibility, enabling adaptation to
CC mechanically stressful environments. {ECO:0000269|PubMed:7580251}.
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:10406121};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0-6.5.;
CC Temperature dependence:
CC Optimum temperature from 12 to 18 degrees Celsius. Cold tolerant.;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed. Predominantly expressed in green
CC siliques. Expressed in young expanding leaves, trichomes, lateral root
CC primordia, vascular tissue, abscission zones and elongating hypocols.
CC Following wind stimulation, it decreases in the leaves of wind-
CC stimulated plants, while it strongly increases in sites around cells of
CC the pith parenchyma, between the vascular elements, and within the
CC epidermis. {ECO:0000269|PubMed:11673616, ECO:0000269|PubMed:7580251,
CC ECO:0000269|PubMed:9414546}.
CC -!- INDUCTION: In response to mechanical perturbations such as wind or
CC touch. Induced by auxin and brassinolide. {ECO:0000269|PubMed:11673616,
CC ECO:0000269|PubMed:7580251, ECO:0000269|PubMed:8696366}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity.
CC -!- PTM: N-glycosylated; essential for its enzymatic activity.
CC {ECO:0000269|PubMed:10406121, ECO:0000269|PubMed:9753780}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 2
CC subfamily. {ECO:0000305}.
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DR EMBL; U27609; AAA92363.1; -; Genomic_DNA.
DR EMBL; AF051338; AAC05572.1; -; mRNA.
DR EMBL; AB011482; BAB08791.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96915.1; -; Genomic_DNA.
DR EMBL; AF367262; AAK56251.1; -; mRNA.
DR EMBL; AF446881; AAL38614.1; -; mRNA.
DR EMBL; AY052712; AAK96616.1; -; mRNA.
DR EMBL; AY055102; AAL05902.1; -; mRNA.
DR EMBL; AF083792; AAN60350.1; -; mRNA.
DR PIR; T52097; T52097.
DR RefSeq; NP_200564.1; NM_125137.4.
DR AlphaFoldDB; Q38857; -.
DR SMR; Q38857; -.
DR BioGRID; 21104; 4.
DR STRING; 3702.AT5G57560.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q38857; -.
DR PRIDE; Q38857; -.
DR ProteomicsDB; 242791; -.
DR EnsemblPlants; AT5G57560.1; AT5G57560.1; AT5G57560.
DR GeneID; 835860; -.
DR Gramene; AT5G57560.1; AT5G57560.1; AT5G57560.
DR KEGG; ath:AT5G57560; -.
DR Araport; AT5G57560; -.
DR TAIR; locus:2174497; AT5G57560.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q38857; -.
DR OMA; GKIMNNG; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q38857; -.
DR BioCyc; ARA:AT5G57560-MON; -.
DR PRO; PR:Q38857; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38857; baseline and differential.
DR Genevisible; Q38857; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
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:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; TAS:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009741; P:response to brassinosteroid; IEP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR.
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; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..284
FT /note="Xyloglucan endotransglucosylase/hydrolase protein
FT 22"
FT /id="PRO_0000011822"
FT DOMAIN 22..211
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 97
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 101
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 101
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 114..116
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 124..126
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 190..191
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 195
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 272
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 99
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 219..228
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 267..281
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT MUTAGEN 97
FT /note="E->D: Induces mislocalization."
FT /evidence="ECO:0000269|PubMed:9753780"
FT MUTAGEN 97
FT /note="E->Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:9753780"
SQ SEQUENCE 284 AA; 32093 MW; E5FCAA8C673530F7 CRC64;
MAITYLLPLF LSLIITSSVS ANFQRDVEIT WGDGRGQIKN NGELLTLSLD KSSGSGFQSK
NEYLFGKVSM QMKLVPGNSA GTVTTLYLKS PGTTWDEIDF EFLGNSSGEP YTLHTNVYTQ
GKGDKEQQFK LWFDPTANFH TYTILWNPQR IIFTVDGTPI REFKNMESLG TLFPKNKPMR
MYSSLWNADD WATRGGLVKT DWSKAPFTAS YRGFQQEACV WSNGKSSCPN ASKQGTTTGS
WLSQELDSTA QQRMRWVQRN YMIYNYCTDA KRFPQGLPKE CLAA
