XTH21_ARATH
ID XTH21_ARATH Reviewed; 305 AA.
AC Q9ZV40;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 21;
DE Short=At-XTH21;
DE Short=XTH-21;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH21; Synonyms=XTR17; OrderedLocusNames=At2g18800; ORFNames=MSF3.18;
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 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 [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 -!- TISSUE SPECIFICITY: Predominantly expressed in green siliques.
CC {ECO:0000269|PubMed:11673616}.
CC -!- INDUCTION: Down-regulated by auxin. {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; AC005724; AAD08949.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06809.1; -; Genomic_DNA.
DR PIR; G84568; G84568.
DR RefSeq; NP_179470.1; NM_127436.2.
DR AlphaFoldDB; Q9ZV40; -.
DR SMR; Q9ZV40; -.
DR STRING; 3702.AT2G18800.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q9ZV40; -.
DR PRIDE; Q9ZV40; -.
DR ProteomicsDB; 242403; -.
DR EnsemblPlants; AT2G18800.1; AT2G18800.1; AT2G18800.
DR GeneID; 816395; -.
DR Gramene; AT2G18800.1; AT2G18800.1; AT2G18800.
DR KEGG; ath:AT2G18800; -.
DR Araport; AT2G18800; -.
DR TAIR; locus:2053967; AT2G18800.
DR eggNOG; ENOG502R75F; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q9ZV40; -.
DR OMA; ASFMNYN; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q9ZV40; -.
DR BioCyc; ARA:AT2G18800-MON; -.
DR BRENDA; 2.4.1.207; 399.
DR PRO; PR:Q9ZV40; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV40; baseline and differential.
DR Genevisible; Q9ZV40; 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; IDA:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
DR GO; GO:0042545; P:cell wall modification; IMP:TAIR.
DR GO; GO:0080022; P:primary root development; IMP: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; 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 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..305
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 21"
FT /id="PRO_0000011821"
FT DOMAIN 26..216
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 236..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 106
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 119..121
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 129..131
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 195..196
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 200
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 287
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 104
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 225..239
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 282..296
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 305 AA; 34145 MW; 9B4BD59F25FA6DC7 CRC64;
MVSSTLLVMS ISLFLGLSIL LVVHGKDFNQ DIDITWGDGR GNILNNGTLL NLGLDQSSGS
GFQSKAEYLY GKVDMQIKLV PGNSAGTVTT FYLKSQGLTW DEIDFEFLGN VSGDPYIVHT
NVYTQGKGDR EQQFYLWFDP TAAFHNYSIL WNPSHIVFYI DGKPIREFKN LEVLGVAYPK
NQPMRMYGSL WNADDWATRG GLVKTNWSQG PFVASFMNYN SENACVWSIV NGTTTTSPCS
PGDSTSSSSS STSEWFSQRG MDSSSKKVLR WVQRKFMVYN YCKDKKRFSN GLPVECTAKN
KNTKS
