XTH9_ARATH
ID XTH9_ARATH Reviewed; 290 AA.
AC Q8LDW9; Q9ZR10;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 9;
DE Short=At-XTH9;
DE Short=XTH-9;
DE EC=2.4.1.207;
DE Flags: Precursor;
GN Name=XTH9; Synonyms=EXGT-A6, XTR16; OrderedLocusNames=At4g03210;
GN ORFNames=F4C21.14;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Flower;
RX PubMed=10945279; DOI=10.1271/bbb.64.1538;
RA Hyodo H., Takemura M., Yokota A., Ohyama K., Kohchi T.;
RT "Systematic isolation of highly transcribed genes in inflorescence apices
RT in Arabidopsis thaliana from an equalized cDNA library.";
RL Biosci. Biotechnol. Biochem. 64:1538-1541(2000).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
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 [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12856951; DOI=10.1023/a:1023904217641;
RA Hyodo H., Yamakawa S., Takeda Y., Tsuduki M., Yokota A., Nishitani K.,
RA Kohchi T.;
RT "Active gene expression of a xyloglucan endotransglucosylase/hydrolase
RT gene, XTH9, in inflorescence apices is related to cell elongation in
RT Arabidopsis thaliana.";
RL Plant Mol. Biol. 52:473-482(2003).
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 Involved in internodal cell elongation. {ECO:0000269|PubMed:12856951}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8LDW9-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in shoot apices. In the vegetative
CC and reproductive phases, it accumulates in the shoot apex region, where
CC cell division is most active. In the reproductive phase, it is also
CC expressed in flower buds, flower stalks and internodes bearing flowers.
CC {ECO:0000269|PubMed:11673616, ECO:0000269|PubMed:12856951}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAM62971.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC005275; AAD14449.1; -; Genomic_DNA.
DR EMBL; AL161496; CAB77806.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82292.1; -; Genomic_DNA.
DR EMBL; AY044333; AAK73274.1; -; mRNA.
DR EMBL; AY072353; AAL62345.1; -; mRNA.
DR EMBL; BT002199; AAN72210.1; -; mRNA.
DR EMBL; AY085753; AAM62971.1; ALT_INIT; mRNA.
DR PIR; G85040; G85040.
DR RefSeq; NP_192230.1; NM_116559.3. [Q8LDW9-1]
DR AlphaFoldDB; Q8LDW9; -.
DR SMR; Q8LDW9; -.
DR STRING; 3702.AT4G03210.1; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR iPTMnet; Q8LDW9; -.
DR PaxDb; Q8LDW9; -.
DR PRIDE; Q8LDW9; -.
DR ProteomicsDB; 242514; -. [Q8LDW9-1]
DR EnsemblPlants; AT4G03210.1; AT4G03210.1; AT4G03210. [Q8LDW9-1]
DR GeneID; 828024; -.
DR Gramene; AT4G03210.1; AT4G03210.1; AT4G03210. [Q8LDW9-1]
DR KEGG; ath:AT4G03210; -.
DR Araport; AT4G03210; -.
DR TAIR; locus:2125437; AT4G03210.
DR eggNOG; ENOG502QS4T; Eukaryota.
DR InParanoid; Q8LDW9; -.
DR OMA; WDEPVMS; -.
DR PhylomeDB; Q8LDW9; -.
DR BioCyc; ARA:AT4G03210-MON; -.
DR PRO; PR:Q8LDW9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LDW9; baseline and differential.
DR Genevisible; Q8LDW9; 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; ISS: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: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; 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; PS51762; GH16_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoplast; Cell wall;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..290
FT /note="Xyloglucan endotransglucosylase/hydrolase protein 9"
FT /id="PRO_0000011809"
FT DOMAIN 27..215
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT ACT_SITE 105
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
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 276
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 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 223..234
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
FT DISULFID 271..284
FT /evidence="ECO:0000250|UniProtKB:Q8GZD5"
SQ SEQUENCE 290 AA; 33141 MW; D5A3DA08A97C0E69 CRC64;
MVGMDLFKCV MMIMVLVVSC GEAVSGAKFD ELYRSSWAMD HCVNEGEVTK LKLDNYSGAG
FESRSKYLFG KVSIQIKLVE GDSAGTVTAF YMSSDGPNHN EFDFEFLGNT TGEPYIVQTN
IYVNGVGNRE QRLNLWFDPT TEFHTYSILW SKRSVVFMVD ETPIRVQKNL EEKGIPFAKD
QAMGVYSSIW NADDWATQGG LVKTDWSHAP FVASYKEFQI DACEIPTTTD LSKCNGDQKF
WWDEPTVSEL SLHQNHQLIW VRANHMIYDY CFDATRFPVT PLECQHHRHL
