ID   XTH10_ARATH             Reviewed;         299 AA.
AC   Q9ZVK1;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 10;
DE            Short=At-XTH10;
DE            Short=XTH-10;
DE            EC=2.4.1.207;
DE   Flags: Precursor;
GN   Name=XTH10; Synonyms=XTR14; OrderedLocusNames=At2g14620;
GN   ORFNames=T6B13.14;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   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 (By
CC       similarity). {ECO:0000250}.
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   -!- 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 1
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; AC005398; AAC69380.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06315.1; -; Genomic_DNA.
DR   EMBL; AY070415; AAL49911.1; -; mRNA.
DR   EMBL; AY096596; AAM20246.1; -; mRNA.
DR   PIR; D84519; D84519.
DR   RefSeq; NP_179069.1; NM_127026.4.
DR   AlphaFoldDB; Q9ZVK1; -.
DR   SMR; Q9ZVK1; -.
DR   STRING; 3702.Q9ZVK1; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q9ZVK1; 2 sites, No reported glycans.
DR   PaxDb; 3702-AT2G14620-1; -.
DR   ProteomicsDB; 242495; -.
DR   EnsemblPlants; AT2G14620.1; AT2G14620.1; AT2G14620.
DR   GeneID; 815950; -.
DR   Gramene; AT2G14620.1; AT2G14620.1; AT2G14620.
DR   KEGG; ath:AT2G14620; -.
DR   Araport; AT2G14620; -.
DR   TAIR; AT2G14620; XTH10.
DR   eggNOG; ENOG502QQ71; Eukaryota.
DR   HOGENOM; CLU_048041_0_0_1; -.
DR   InParanoid; Q9ZVK1; -.
DR   OMA; IDACVWN; -.
DR   OrthoDB; 337487at2759; -.
DR   PhylomeDB; Q9ZVK1; -.
DR   BioCyc; ARA:AT2G14620-MONOMER; -.
DR   PRO; PR:Q9ZVK1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZVK1; baseline and differential.
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:0010411; P:xyloglucan metabolic process; IEA:InterPro.
DR   CDD; cd02176; GH16_XET; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR044791; Beta-glucanase/XTH.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR010713; XET_C.
DR   InterPro; IPR016455; XTH.
DR   PANTHER; PTHR31062; XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN 8-RELATED; 1.
DR   PANTHER; PTHR31062:SF120; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 10-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF06955; XET_C; 1.
DR   PIRSF; PIRSF005604; XET; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51762; GH16_2; 1.
DR   Genevisible; Q9ZVK1; AT.
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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..299
FT                   /note="Probable xyloglucan endotransglucosylase/hydrolase
FT                   protein 10"
FT                   /id="PRO_0000011810"
FT   DOMAIN          30..225
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        111
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         115
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         128..130
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         138..140
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         204..205
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         209
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         285
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            113
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        51
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        233..242
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   DISULFID        280..294
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ   SEQUENCE   299 AA;  34687 MW;  C8A688EFB7E910A5 CRC64;
     MTLINRSKPF VLLVGFSIIS SLLLWVSQAS VVSSGDFNKD FFVTWSPTHV NTSNDGRSRT
     LKLDQESGAS FSSIQTFLFG QIDMKIKLIR GSSQGTVVAY YMSSDQPNRD EIDFEFLGNV
     NGQPYILQTN VYAEGLDNRE ERIHLWFDPA KDFHTYSILW NIHQIVFMVD QIPIRLYRNH
     GEKGVAYPRL QPMSVQASLW NGESWATRGG HDKIDWSKGP FVASFGDYKI DACIWIGNTS
     FCNGESTENW WNKNEFSSLT RVQKRWFKWV RKYHLIYDYC QDYGRFNNKL PKECSLPKY
//