XTH20_ARATH
ID XTH20_ARATH Reviewed; 282 AA.
AC Q9FI31; Q56Y69;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 20 {ECO:0000305};
DE Short=At-XTH20 {ECO:0000303|PubMed:12514239};
DE Short=XTH-20 {ECO:0000303|PubMed:12514239};
DE EC=2.4.1.207 {ECO:0000305};
DE Flags: Precursor;
GN Name=XTH20 {ECO:0000303|PubMed:25182467}; OrderedLocusNames=At5g48070;
GN ORFNames=MDN11.15;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
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 [6]
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 [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: Catalyzes xyloglucan endohydrolysis (XEH) (By similarity).
CC Cleaves and religates xyloglucan polymers, an essential constituent of
CC the primary cell wall, and thereby participates in cell wall
CC construction of growing tissues (PubMed:23585673). Involved in cell
CC proliferation in the tissue reunion process of wounded inflorescence
CC stems. Maybe a downstream target of NAC071 as a consequence of auxin
CC action in wounded stems (PubMed:25182467).
CC {ECO:0000250|UniProtKB:Q9M0D1, ECO:0000269|PubMed:25182467,
CC 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 -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Root specific. {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; AB017064; BAB11071.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95616.1; -; Genomic_DNA.
DR EMBL; BT012361; AAS77486.1; -; mRNA.
DR EMBL; AK221454; BAD94531.1; -; mRNA.
DR RefSeq; NP_199618.1; NM_124181.4.
DR AlphaFoldDB; Q9FI31; -.
DR SMR; Q9FI31; -.
DR STRING; 3702.AT5G48070.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q9FI31; -.
DR PRIDE; Q9FI31; -.
DR ProteomicsDB; 243028; -.
DR EnsemblPlants; AT5G48070.1; AT5G48070.1; AT5G48070.
DR GeneID; 834859; -.
DR Gramene; AT5G48070.1; AT5G48070.1; AT5G48070.
DR KEGG; ath:AT5G48070; -.
DR Araport; AT5G48070; -.
DR TAIR; locus:2162652; AT5G48070.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q9FI31; -.
DR OMA; KNRVKWA; -.
DR OrthoDB; 934253at2759; -.
DR PhylomeDB; Q9FI31; -.
DR BioCyc; ARA:AT5G48070-MON; -.
DR BRENDA; 2.4.1.207; 399.
DR PRO; PR:Q9FI31; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FI31; baseline and differential.
DR Genevisible; Q9FI31; 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; 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:0071365; P:cellular response to auxin 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 2: Evidence at transcript level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..282
FT /note="Xyloglucan endotransglucosylase/hydrolase protein
FT 20"
FT /id="PRO_0000011820"
FT DOMAIN 27..218
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 108
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 121..123
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 131..133
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 197..198
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 202
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 106
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 226..235
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 267..281
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 282 AA; 32437 MW; FBB8C587F6C9A3C3 CRC64;
MVSFCGRRFA FLIIFLFAAQ YERVYAGSFH KDVQIHWGDG RGKILDNVGN LLSLSLDKFS
GSGFQSHQEF LYGKVEVQMK LVPGNSAGTV TTFYLKSPGT TWDEIDFEFL GNISGHPYTL
HTNVYTKGTG DKEQQFHLWF DPTVDFHTYC IIWNPQRVIF TIDGIPIREF KNSEALGVPF
PKHQPMRLYA SLWEAEHWAT RGGLEKTDWS KAPFTAFYRN YNVDACVWSN GKSSCSANSS
WFTQVLDFKG KNRVKWAQRK YMVYNYCTDK KRFPQGAPPE CS
