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   27-MAR-2024, entry version 157.
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}.
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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.O80803; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; O80803; 1 site, No reported glycans.
DR   PaxDb; 3702-AT1G65310-1; -.
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; AT1G65310; XTH17.
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   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   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; O80803; AT.
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
//