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Protein

Xyloglucan endotransglucosylase/hydrolase protein 9

Gene

XTH9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. Involved in internodal cell elongation.1 Publication

Catalytic activityi

Breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose residue of an acceptor, which can be a xyloglucan or an oligosaccharide of xyloglucan.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei101 – 1011NucleophileBy similarity
Active sitei105 – 1051Proton donorBy similarity

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  2. xyloglucan:xyloglucosyl transferase activity Source: TAIR

GO - Biological processi

  1. cellular glucan metabolic process Source: InterPro
  2. cell wall organization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciARA:AT4G03210-MONOMER.
ARA:GQT-624-MONOMER.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Xyloglucan endotransglucosylase/hydrolase protein 9 (EC:2.4.1.207)
Short name:
At-XTH9
Short name:
XTH-9
Gene namesi
Name:XTH9
Synonyms:EXGT-A6, XTR16
Ordered Locus Names:At4g03210
ORF Names:F4C21.14
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G03210.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: UniProtKB-SubCell
  2. cell wall Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Apoplast, Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 290264Xyloglucan endotransglucosylase/hydrolase protein 9PRO_0000011809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Contains at least one intrachain disulfide bond essential for its enzymatic activity.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8LDW9.
PRIDEiQ8LDW9.

Expressioni

Tissue specificityi

Highly expressed in shoot apices. In the vegetative and reproductive phases, it accumulates in the shoot apex region, where cell division is most active. In the reproductive phase, it is also expressed in flower buds, flower stalks and internodes bearing flowers.2 Publications

Gene expression databases

ExpressionAtlasiQ8LDW9. baseline and differential.
GenevestigatoriQ8LDW9.

Structurei

3D structure databases

ProteinModelPortaliQ8LDW9.
SMRiQ8LDW9. Positions 29-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2273.
HOGENOMiHOG000236368.
InParanoidiQ8LDW9.
KOiK08235.
OMAiFQIDACE.
PhylomeDBiQ8LDW9.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR013320. ConA-like_dom.
IPR000757. Glyco_hydro_16.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamiPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005604. XET. 1 hit.
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8LDW9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVGMDLFKCV MMIMVLVVSC GEAVSGAKFD ELYRSSWAMD HCVNEGEVTK
60 70 80 90 100
LKLDNYSGAG FESRSKYLFG KVSIQIKLVE GDSAGTVTAF YMSSDGPNHN
110 120 130 140 150
EFDFEFLGNT TGEPYIVQTN IYVNGVGNRE QRLNLWFDPT TEFHTYSILW
160 170 180 190 200
SKRSVVFMVD ETPIRVQKNL EEKGIPFAKD QAMGVYSSIW NADDWATQGG
210 220 230 240 250
LVKTDWSHAP FVASYKEFQI DACEIPTTTD LSKCNGDQKF WWDEPTVSEL
260 270 280 290
SLHQNHQLIW VRANHMIYDY CFDATRFPVT PLECQHHRHL
Length:290
Mass (Da):33,141
Last modified:November 28, 2003 - v2
Checksum:iD5A3DA08A97C0E69
GO

Sequence cautioni

The sequence AAM62971.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005275 Genomic DNA. Translation: AAD14449.1.
AL161496 Genomic DNA. Translation: CAB77806.1.
CP002687 Genomic DNA. Translation: AEE82292.1.
AY044333 mRNA. Translation: AAK73274.1.
AY072353 mRNA. Translation: AAL62345.1.
BT002199 mRNA. Translation: AAN72210.1.
AY085753 mRNA. Translation: AAM62971.1. Different initiation.
PIRiG85040.
RefSeqiNP_192230.1. NM_116559.2. [Q8LDW9-1]
UniGeneiAt.3932.
At.5453.

Genome annotation databases

EnsemblPlantsiAT4G03210.1; AT4G03210.1; AT4G03210. [Q8LDW9-1]
GeneIDi828024.
KEGGiath:AT4G03210.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005275 Genomic DNA. Translation: AAD14449.1.
AL161496 Genomic DNA. Translation: CAB77806.1.
CP002687 Genomic DNA. Translation: AEE82292.1.
AY044333 mRNA. Translation: AAK73274.1.
AY072353 mRNA. Translation: AAL62345.1.
BT002199 mRNA. Translation: AAN72210.1.
AY085753 mRNA. Translation: AAM62971.1. Different initiation.
PIRiG85040.
RefSeqiNP_192230.1. NM_116559.2. [Q8LDW9-1]
UniGeneiAt.3932.
At.5453.

3D structure databases

ProteinModelPortaliQ8LDW9.
SMRiQ8LDW9. Positions 29-290.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PaxDbiQ8LDW9.
PRIDEiQ8LDW9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G03210.1; AT4G03210.1; AT4G03210. [Q8LDW9-1]
GeneIDi828024.
KEGGiath:AT4G03210.

Organism-specific databases

TAIRiAT4G03210.

Phylogenomic databases

eggNOGiCOG2273.
HOGENOMiHOG000236368.
InParanoidiQ8LDW9.
KOiK08235.
OMAiFQIDACE.
PhylomeDBiQ8LDW9.

Enzyme and pathway databases

BioCyciARA:AT4G03210-MONOMER.
ARA:GQT-624-MONOMER.

Gene expression databases

ExpressionAtlasiQ8LDW9. baseline and differential.
GenevestigatoriQ8LDW9.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR013320. ConA-like_dom.
IPR000757. Glyco_hydro_16.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamiPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005604. XET. 1 hit.
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49899. SSF49899. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Systematic isolation of highly transcribed genes in inflorescence apices in Arabidopsis thaliana from an equalized cDNA library."
    Hyodo H., Takemura M., Yokota A., Ohyama K., Kohchi T.
    Biosci. Biotechnol. Biochem. 64:1538-1541(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Flower.
  6. "A comprehensive expression analysis of all members of a gene family encoding cell-wall enzymes allowed us to predict cis-regulatory regions involved in cell-wall construction in specific organs of Arabidopsis."
    Yokoyama R., Nishitani K.
    Plant Cell Physiol. 42:1025-1033(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: current perspectives and a new unifying nomenclature."
    Rose J.K.C., Braam J., Fry S.C., Nishitani K.
    Plant Cell Physiol. 43:1421-1435(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE.
  8. "Active gene expression of a xyloglucan endotransglucosylase/hydrolase gene, XTH9, in inflorescence apices is related to cell elongation in Arabidopsis thaliana."
    Hyodo H., Yamakawa S., Takeda Y., Tsuduki M., Yokota A., Nishitani K., Kohchi T.
    Plant Mol. Biol. 52:473-482(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiXTH9_ARATH
AccessioniPrimary (citable) accession number: Q8LDW9
Secondary accession number(s): Q9ZR10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: November 28, 2003
Last modified: January 7, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.