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Protein

Xyloglucan endotransglucosylase/hydrolase protein 14

Gene

XTH14

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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. Has some preference for non-fucosylated xyloglucan polymer.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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei104 – 1041NucleophilePROSITE-ProRule annotation
Active sitei108 – 1081Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

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

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:AT4G25820-MONOMER.
BRENDAi2.4.1.207. 399.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Names & Taxonomyi

Protein namesi
Recommended name:
Xyloglucan endotransglucosylase/hydrolase protein 14 (EC:2.4.1.207)
Short name:
At-XTH14
Short name:
XTH-14
Gene namesi
Name:XTH14
Synonyms:XTR9
Ordered Locus Names:At4g25820
ORF Names:F14M19.100
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G25820.

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 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 287260Xyloglucan endotransglucosylase/hydrolase protein 14PRO_0000011814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Contains at least one intrachain disulfide bond essential for its enzymatic activity.By similarity
N-glycosylated; not essential for its enzymatic activity.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9ZSU4.
PRIDEiQ9ZSU4.

Expressioni

Tissue specificityi

Root specific.1 Publication

Gene expression databases

GenevestigatoriQ9ZSU4.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G25820.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9ZSU4.
SMRiQ9ZSU4. Positions 30-286.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2273.
HOGENOMiHOG000236368.
InParanoidiQ9ZSU4.
KOiK08235.
OMAiANIFENG.
PhylomeDBiQ9ZSU4.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamiPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005604. XET. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9ZSU4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MACFATKQPL LLSLLLAIGF FVVAASAGNF YESFDITWGN GRANIFENGQ
60 70 80 90 100
LLTCTLDKVS GSGFQSKKEY LFGKIDMKLK LVAGNSAGTV TAYYLSSKGT
110 120 130 140 150
AWDEIDFEFL GNRTGHPYTI HTNVFTGGKG DREMQFRLWF DPTADFHTYT
160 170 180 190 200
VHWNPVNIIF LVDGIPIRVF KNNEKNGVAY PKNQPMRIYS SLWEADDWAT
210 220 230 240 250
EGGRVKIDWS NAPFKASYRN FNDQSSCSRT SSSKWVTCEP NSNSWMWTTL
260 270 280
NPAQYGKMMW VQRDFMIYNY CTDFKRFPQG LPKECKL
Length:287
Mass (Da):32,740
Last modified:May 1, 1999 - v1
Checksum:i42D596152C85848D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093672 mRNA. Translation: AAD12249.1.
AL049480 Genomic DNA. Translation: CAB39603.1.
AL161564 Genomic DNA. Translation: CAB79437.1.
CP002687 Genomic DNA. Translation: AEE85118.1.
AY093183 mRNA. Translation: AAM13182.1.
BT003385 mRNA. Translation: AAO30048.1.
PIRiT04236.
RefSeqiNP_194312.1. NM_118714.3.
UniGeneiAt.2902.

Genome annotation databases

EnsemblPlantsiAT4G25820.1; AT4G25820.1; AT4G25820.
GeneIDi828687.
KEGGiath:AT4G25820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093672 mRNA. Translation: AAD12249.1.
AL049480 Genomic DNA. Translation: CAB39603.1.
AL161564 Genomic DNA. Translation: CAB79437.1.
CP002687 Genomic DNA. Translation: AEE85118.1.
AY093183 mRNA. Translation: AAM13182.1.
BT003385 mRNA. Translation: AAO30048.1.
PIRiT04236.
RefSeqiNP_194312.1. NM_118714.3.
UniGeneiAt.2902.

3D structure databases

ProteinModelPortaliQ9ZSU4.
SMRiQ9ZSU4. Positions 30-286.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G25820.1-P.

Protein family/group databases

CAZyiGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PaxDbiQ9ZSU4.
PRIDEiQ9ZSU4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G25820.1; AT4G25820.1; AT4G25820.
GeneIDi828687.
KEGGiath:AT4G25820.

Organism-specific databases

GeneFarmi2637. 265.
TAIRiAT4G25820.

Phylogenomic databases

eggNOGiCOG2273.
HOGENOMiHOG000236368.
InParanoidiQ9ZSU4.
KOiK08235.
OMAiANIFENG.
PhylomeDBiQ9ZSU4.

Enzyme and pathway databases

BioCyciARA:AT4G25820-MONOMER.
BRENDAi2.4.1.207. 399.

Gene expression databases

GenevestigatoriQ9ZSU4.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamiPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFiPIRSF005604. XET. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "In vitro activities of four xyloglucan endotransglycosylases from Arabidopsis."
    Campbell P., Braam J.
    Plant J. 18:371-382(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, GLYCOSYLATION.
  2. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
  5. "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.
  6. "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.

Entry informationi

Entry nameiXTH14_ARATH
AccessioniPrimary (citable) accession number: Q9ZSU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 111 of the entry and version 1 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.