XTH17_ARATH
ID XTH17_ARATH Reviewed; 282 AA.
AC O80803;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 17 {ECO:0000303|PubMed:12514239};
DE Short=At-XTH17 {ECO:0000303|PubMed:12514239};
DE Short=XTH-17 {ECO:0000303|PubMed:12514239};
DE EC=2.4.1.207 {ECO:0000305|PubMed:24948835};
DE Flags: Precursor;
GN Name=XTH17 {ECO:0000303|PubMed:12514239};
GN Synonyms=XTR1 {ECO:0000303|PubMed:11673616};
GN OrderedLocusNames=At1g65310 {ECO:0000312|Araport:AT1G65310};
GN ORFNames=T8F5.9 {ECO:0000312|EMBL:AAC27142.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 TISSUE SPECIFICITY.
RX PubMed=15659443; DOI=10.1093/pcp/pci013;
RA Vissenberg K., Oyama M., Osato Y., Yokoyama R., Verbelen J.P.,
RA Nishitani K.;
RT "Differential expression of AtXTH17, AtXTH18, AtXTH19 and AtXTH20 genes in
RT Arabidopsis roots. Physiological roles in specification in cell wall
RT construction.";
RL Plant Cell Physiol. 46:192-200(2005).
RN [7]
RP FUNCTION, INTERACTION WITH XTH31, SUBCELLULAR LOCATION, AND INDUCTION BY
RP ALUMINUM.
RX PubMed=24948835; DOI=10.1104/pp.114.243790;
RA Zhu X.F., Wan J.X., Sun Y., Shi Y.Z., Braam J., Li G.X., Zheng S.J.;
RT "Xyloglucan endotransglucosylase-hydrolase17 interacts with xyloglucan
RT endotransglucosylase-hydrolase31 to confer xyloglucan endotransglucosylase
RT action and affect aluminum sensitivity in Arabidopsis.";
RL Plant Physiol. 165:1566-1574(2014).
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.
CC {ECO:0000269|PubMed:24948835}.
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:0000305|PubMed:24948835};
CC -!- SUBUNIT: Interacts with XTH31. The formation of an XTH17-XTH31 dimer
CC may be required for XET activity. {ECO:0000269|PubMed:24948835}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:24948835}.
CC -!- TISSUE SPECIFICITY: Root specific (PubMed:11673616). Expressed in all
CC cell types in the elongating and differentiating region of the root
CC (PubMed:15659443). {ECO:0000269|PubMed:11673616,
CC ECO:0000269|PubMed:15659443}.
CC -!- INDUCTION: Up-regulated by auxin and brassinolide (PubMed:11673616).
CC Down-regulated by aluminum. {ECO:0000269|PubMed:11673616,
CC ECO:0000269|PubMed:24948835}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: Knockdown mutants have shorter roots, decreased cell
CC wall xyloglucan content and increased aluminum resistance.
CC {ECO:0000269|PubMed:24948835}.
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; AC004512; AAC27142.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34357.1; -; Genomic_DNA.
DR EMBL; AF370621; AAK43940.1; -; mRNA.
DR PIR; T02354; T02354.
DR RefSeq; NP_176710.1; NM_105205.4.
DR AlphaFoldDB; O80803; -.
DR SMR; O80803; -.
DR BioGRID; 28060; 1.
DR STRING; 3702.AT1G65310.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; O80803; -.
DR PRIDE; O80803; -.
DR ProteomicsDB; 242560; -.
DR EnsemblPlants; AT1G65310.1; AT1G65310.1; AT1G65310.
DR GeneID; 842839; -.
DR Gramene; AT1G65310.1; AT1G65310.1; AT1G65310.
DR KEGG; ath:AT1G65310; -.
DR Araport; AT1G65310; -.
DR TAIR; locus:2206335; AT1G65310.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; O80803; -.
DR OMA; NHENNGI; -.
DR PhylomeDB; O80803; -.
DR BRENDA; 2.4.1.207; 399.
DR PRO; PR:O80803; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O80803; baseline and differential.
DR Genevisible; O80803; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; 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:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 membrane; Cell wall; Cell wall biogenesis/degradation;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..282
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 17"
FT /id="PRO_0000011817"
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 DISULFID 226..235
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 267..281
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 282 AA; 31992 MW; 00F9732C0C44172D CRC64;
MKLSCGTSFA FLLLFLLAAQ SVHVYAGSFH KDVQIHWGDG RGKIHDRDGK LLSLSLDKSS
GSGFQSNQEF LYGKAEVQMK LVPGNSAGTV TTFYLKSPGT TWDEIDFEFL GNISGHPYTL
HTNVYTKGTG DKEQQFHLWF DPTVNFHTYC ITWNPQRIIF TVDGIPIREF KNPEAIGVPF
PTRQPMRLYA SLWEAEHWAT RGGLEKTDWS KAPFTAFYRN YNVDGCVWAN GKSSCSANSP
WFTQKLDSNG QTRMKGVQSK YMIYNYCTDK RRFPRGVPAE CT
