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   27-MAR-2024, entry version 153.
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.Q8LDW9; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   GlyCosmos; Q8LDW9; 2 sites, No reported glycans.
DR   iPTMnet; Q8LDW9; -.
DR   PaxDb; 3702-AT4G03210-1; -.
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; AT4G03210; XTH9.
DR   eggNOG; ENOG502QS4T; Eukaryota.
DR   InParanoid; Q8LDW9; -.
DR   OMA; FQPSWAL; -.
DR   OrthoDB; 337487at2759; -.
DR   PhylomeDB; Q8LDW9; -.
DR   BioCyc; ARA:AT4G03210-MONOMER; -.
DR   PRO; PR:Q8LDW9; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8LDW9; 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; 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   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:SF108; XYLOGLUCAN ENDOTRANSGLUCOSYLASE_HYDROLASE PROTEIN 9; 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; Q8LDW9; AT.
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
//