XTH4_ARATH
ID XTH4_ARATH Reviewed; 296 AA.
AC Q39099; Q94F33;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 4;
DE Short=At-XTH4;
DE Short=XTH-4;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH4; Synonyms=EXGT-A1, EXT; OrderedLocusNames=At2g06850;
GN ORFNames=T9F8.4;
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 [MRNA].
RX PubMed=8244968; DOI=10.1016/s0021-9258(19)74400-7;
RA Okazawa K., Sato Y., Nakagawa T., Asada K., Kato I., Tomita E.,
RA Nishitani K.;
RT "Molecular cloning and cDNA sequencing of endoxyloglucan transferase, a
RT novel class of glycosyltransferase that mediates molecular grafting between
RT matrix polysaccharides in plant cell walls.";
RL J. Biol. Chem. 268:25364-25368(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10557219; DOI=10.1104/pp.121.3.715;
RA Akamatsu T., Hanzawa Y., Ohtake Y., Takahashi T., Nishitani K., Komeda Y.;
RT "Expression of endoxyloglucan transferase genes in acaulis mutants of
RT Arabidopsis.";
RL Plant Physiol. 121:715-721(1999).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION.
RX PubMed=8696366; DOI=10.1046/j.1365-313x.1996.9060879.x;
RA Xu W., Campbell P., Vargheese A.K., Braam J.;
RT "The Arabidopsis XET-related gene family: environmental and hormonal
RT regulation of expression.";
RL Plant J. 9:879-889(1996).
RN [8]
RP ENZYME ACTIVITY, AND GLYCOSYLATION.
RX PubMed=10406121; DOI=10.1046/j.1365-313x.1999.00459.x;
RA Campbell P., Braam J.;
RT "In vitro activities of four xyloglucan endotransglycosylases from
RT Arabidopsis.";
RL Plant J. 18:371-382(1999).
RN [9]
RP 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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=15593128; DOI=10.1002/pmic.200400882;
RA Boudart G., Jamet E., Rossignol M., Lafitte C., Borderies G., Jauneau A.,
RA Esquerre-Tugaye M.-T., Pont-Lezica R.;
RT "Cell wall proteins in apoplastic fluids of Arabidopsis thaliana rosettes:
RT identification by mass spectrometry and bioinformatics.";
RL Proteomics 5:212-221(2005).
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 -!- 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:0000269|PubMed:10406121};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
CC extracellular space, apoplast {ECO:0000269|PubMed:15593128}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in young developing
CC tissues. Expressed in 7 day old seedlings, roots, nodes bearing
CC flowers, flower buds and siliques. {ECO:0000269|PubMed:10557219}.
CC -!- INDUCTION: By auxin and brassinolide. {ECO:0000269|PubMed:11673616,
CC ECO:0000269|PubMed:8696366}.
CC -!- PTM: Contains at least one intrachain disulfide bond essential for its
CC enzymatic activity. {ECO:0000250}.
CC -!- PTM: N-glycosylated; not essential for its enzymatic activity.
CC {ECO:0000269|PubMed:10406121}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK62373.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D16454; BAA03921.1; -; mRNA.
DR EMBL; AF163819; AAD45123.1; -; Genomic_DNA.
DR EMBL; AC005561; AAC98464.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06021.1; -; Genomic_DNA.
DR EMBL; AF386928; AAK62373.1; ALT_FRAME; mRNA.
DR EMBL; AY054547; AAK96738.1; -; mRNA.
DR EMBL; AY056201; AAL07050.1; -; mRNA.
DR EMBL; AY059873; AAL24355.1; -; mRNA.
DR EMBL; AY064672; AAL47378.1; -; mRNA.
DR EMBL; AY114644; AAM47963.1; -; mRNA.
DR EMBL; AY085465; AAM62691.1; -; mRNA.
DR PIR; C49539; C49539.
DR RefSeq; NP_178708.1; NM_126666.4.
DR AlphaFoldDB; Q39099; -.
DR SMR; Q39099; -.
DR BioGRID; 640; 5.
DR STRING; 3702.AT2G06850.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR iPTMnet; Q39099; -.
DR PaxDb; Q39099; -.
DR PRIDE; Q39099; -.
DR ProteomicsDB; 242471; -.
DR EnsemblPlants; AT2G06850.1; AT2G06850.1; AT2G06850.
DR GeneID; 815247; -.
DR Gramene; AT2G06850.1; AT2G06850.1; AT2G06850.
DR KEGG; ath:AT2G06850; -.
DR Araport; AT2G06850; -.
DR TAIR; locus:2065821; AT2G06850.
DR eggNOG; ENOG502QQUC; Eukaryota.
DR HOGENOM; CLU_048041_0_0_1; -.
DR InParanoid; Q39099; -.
DR OrthoDB; 1209387at2759; -.
DR PhylomeDB; Q39099; -.
DR BioCyc; ARA:AT2G06850-MON; -.
DR PRO; PR:Q39099; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q39099; baseline and differential.
DR Genevisible; Q39099; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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; IMP:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IGI:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009645; P:response to low light intensity stimulus; IEP:TAIR.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; 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; 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; PTHR31062; 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; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal;
KW Transferase.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..296
FT /note="Xyloglucan endotransglucosylase/hydrolase protein 4"
FT /id="PRO_0000011804"
FT DOMAIN 26..223
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
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 202..203
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 207
FT /ligand="xyloglucan"
FT /ligand_id="ChEBI:CHEBI:18233"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT BINDING 282
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 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:10406121"
FT DISULFID 231..240
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 277..290
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT CONFLICT 205..206
FT /note="TR -> PK (in Ref. 5; AAK62373)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 34291 MW; 455F3574BE7751CC CRC64;
MTVSSSPWAL MALFLMVSST MVMAIPPRKA IDVPFGRNYV PTWAFDHQKQ FNGGSELQLI
LDKYTGTGFQ SKGSYLFGHF SMHIKLPAGD TAGVVTAFYL SSTNNEHDEI DFEFLGNRTG
QPAILQTNVF TGGKGNREQR IYLWFDPSKA YHTYSILWNM YQIVFFVDNI PIRTFKNAKD
LGVRFPFNQP MKLYSSLWNA DDWATRGGLE KTNWANAPFV ASYKGFHIDG CQASVEAKYC
ATQGRMWWDQ KEFRDLDAEQ WRRLKWVRMK WTIYNYCTDR TRFPVMPAEC KRDRDA
