XTH12_ARATH
ID XTH12_ARATH Reviewed; 285 AA.
AC Q9FKL9;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable xyloglucan endotransglucosylase/hydrolase protein 12;
DE Short=At-XTH12;
DE Short=XTH-12;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH12; OrderedLocusNames=At5g57530; ORFNames=MUA2.10;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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).
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: Root specific. {ECO:0000269|PubMed:11673616}.
CC -!- INDUCTION: Strongly down-regulated by abscisic acid (ABA).
CC {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; AB011482; BAB08788.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96911.1; -; Genomic_DNA.
DR EMBL; AY057625; AAL15256.1; -; mRNA.
DR EMBL; AY113025; AAM47333.1; -; mRNA.
DR RefSeq; NP_200561.1; NM_125134.2.
DR AlphaFoldDB; Q9FKL9; -.
DR SMR; Q9FKL9; -.
DR STRING; 3702.AT5G57530.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR PaxDb; Q9FKL9; -.
DR PRIDE; Q9FKL9; -.
DR ProteomicsDB; 242410; -.
DR EnsemblPlants; AT5G57530.1; AT5G57530.1; AT5G57530.
DR GeneID; 835857; -.
DR Gramene; AT5G57530.1; AT5G57530.1; AT5G57530.
DR KEGG; ath:AT5G57530; -.
DR Araport; AT5G57530; -.
DR TAIR; locus:2174572; AT5G57530.
DR eggNOG; ENOG502QQ71; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q9FKL9; -.
DR OMA; FDITWGA; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q9FKL9; -.
DR BioCyc; ARA:AT5G57530-MON; -.
DR BRENDA; 2.4.1.207; 399.
DR PRO; PR:Q9FKL9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKL9; baseline and differential.
DR Genevisible; Q9FKL9; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
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; 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..285
FT /note="Probable xyloglucan endotransglucosylase/hydrolase
FT protein 12"
FT /id="PRO_0000011812"
FT DOMAIN 26..215
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT BINDING 105
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 118..120
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 194..195
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 199
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 273
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT SITE 103
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 224..235
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 268..282
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 285 AA; 32190 MW; 0544E8E568F5C543 CRC64;
MAAFATKQSP LLLASLLILI GVATGSFYDS FDITWGAGRA NIFESGQLLT CTLDKTSGSG
FQSKKEYLFG KIDMKIKLVP GNSAGTVTAY YLSSKGETWD EIDFEFLGNV TGQPYVIHTN
VFTGGKGNRE MQFYLWFDPT ADFHTYTVLW NPLNIIFLVD GIPIRVFKNN EANGVAYPKS
QPMKIYSSLW EADDWATQGG KVKTDWTNAP FSASYRSFND VDCCSRTSIW NWVTCNANSN
SWMWTTLNSN QLGQLKWVQK DYMIYNYCTD FKRFPQGLPT ECNLN
