ID   XTH3_ARATH              Reviewed;         290 AA.
AC   Q9LJR7; Q1PEM0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 3;
DE            Short=At-XTH3;
DE            Short=XTH-3;
DE            EC=2.4.1.207;
DE   Flags: Precursor;
GN   Name=XTH3; OrderedLocusNames=At3g25050; ORFNames=K3G3.6;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
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).
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   -!- TISSUE SPECIFICITY: Predominantly expressed in flower buds.
CC       {ECO:0000269|PubMed:11673616}.
CC   -!- INDUCTION: By auxin and brassinolide. {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 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AP000412; BAB01890.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76972.1; -; Genomic_DNA.
DR   EMBL; DQ446697; ABE65966.1; -; mRNA.
DR   RefSeq; NP_189141.1; NM_113409.4.
DR   AlphaFoldDB; Q9LJR7; -.
DR   SMR; Q9LJR7; -.
DR   STRING; 3702.Q9LJR7; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q9LJR7; 1 site, No reported glycans.
DR   PaxDb; 3702-AT3G25050-1; -.
DR   ProteomicsDB; 242427; -.
DR   EnsemblPlants; AT3G25050.1; AT3G25050.1; AT3G25050.
DR   GeneID; 822096; -.
DR   Gramene; AT3G25050.1; AT3G25050.1; AT3G25050.
DR   KEGG; ath:AT3G25050; -.
DR   Araport; AT3G25050; -.
DR   TAIR; AT3G25050; XTH3.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_048041_0_0_1; -.
DR   InParanoid; Q9LJR7; -.
DR   OMA; WGQSHVS; -.
DR   OrthoDB; 337487at2759; -.
DR   PhylomeDB; Q9LJR7; -.
DR   BioCyc; ARA:AT3G25050-MONOMER; -.
DR   PRO; PR:Q9LJR7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LJR7; 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; IDA:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030243; P:cellulose metabolic process; IDA:TAIR.
DR   GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR   GO; GO:0009832; P:plant-type cell wall biogenesis; ISS:TAIR.
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; IPR008264; Beta_glucanase.
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:SF194; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 3; 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; PS51762; GH16_2; 1.
DR   Genevisible; Q9LJR7; 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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..290
FT                   /note="Xyloglucan endotransglucosylase/hydrolase protein 3"
FT                   /id="PRO_0000011803"
FT   DOMAIN          22..220
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        109
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         113
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         126..128
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         136..138
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         199..200
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   BINDING         204
FT                   /ligand="xyloglucan"
FT                   /ligand_id="ChEBI:CHEBI:18233"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   SITE            111
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        228..240
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT   DISULFID        276..289
FT                   /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ   SEQUENCE   290 AA;  33259 MW;  5139E94737955AF0 CRC64;
     MDYMRIFSVF VVTLWIIRVD ARVFGGRGIE KFVTFGQNYI VTWGQSHVST LHSGEEVDLY
     MDQSSGGGFE SKDAYGSGLF EMRIKVPSGN TGGIVTAFYL TSKGGGHDEI DFEFLGNNNG
     KPVTLQTNLF LNGEGNREER FLLWFNPTKH YHTYGLLWNP YQIVFYVDNI PIRVYKNENG
     VSYPSKPMQV EASLWNGDDW ATDGGRTKVN WSYSPFIAHF RDFALSGCNI DGRSNNVGAC
     ESSNYWWNAG NYQRLSGNEQ KLYEHVRSKY MNYDYCTDRS KYQTPPRECY
//