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Q9ZSU4 (XTH14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xyloglucan endotransglucosylase/hydrolase protein 14

Short name=At-XTH14
Short name=XTH-14
EC=2.4.1.207
Gene names
Name:XTH14
Synonyms:XTR9
Ordered Locus Names:At4g25820
ORF Names:F14M19.100
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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. Ref.1

Subcellular location

Secretedcell wall Probable. Secretedextracellular spaceapoplast Probable.

Tissue specificity

Root specific. Ref.5

Post-translational modification

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

N-glycosylated; not essential for its enzymatic activity. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 16 family. XTH group 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 287260Xyloglucan endotransglucosylase/hydrolase protein 14
PRO_0000011814

Sites

Active site1041Nucleophile By similarity
Active site1081Proton donor By similarity

Amino acid modifications

Glycosylation1121N-linked (GlcNAc...) Probable

Sequences

Sequence LengthMass (Da)Tools
Q9ZSU4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 42D596152C85848D

FASTA28732,740
        10         20         30         40         50         60 
MACFATKQPL LLSLLLAIGF FVVAASAGNF YESFDITWGN GRANIFENGQ LLTCTLDKVS 

        70         80         90        100        110        120 
GSGFQSKKEY LFGKIDMKLK LVAGNSAGTV TAYYLSSKGT AWDEIDFEFL GNRTGHPYTI 

       130        140        150        160        170        180 
HTNVFTGGKG DREMQFRLWF DPTADFHTYT VHWNPVNIIF LVDGIPIRVF KNNEKNGVAY 

       190        200        210        220        230        240 
PKNQPMRIYS SLWEADDWAT EGGRVKIDWS NAPFKASYRN FNDQSSCSRT SSSKWVTCEP 

       250        260        270        280 
NSNSWMWTTL NPAQYGKMMW VQRDFMIYNY CTDFKRFPQG LPKECKL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT04236.
RefSeqNP_194312.1. NM_118714.3.
UniGeneAt.2902.

3D structure databases

ProteinModelPortalQ9ZSU4.
SMRQ9ZSU4. Positions 30-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G25820.1-P.

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PaxDbQ9ZSU4.
PRIDEQ9ZSU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G25820.1; AT4G25820.1; AT4G25820.
GeneID828687.
KEGGath:AT4G25820.

Organism-specific databases

GeneFarm2637. 265.
TAIRAT4G25820.

Phylogenomic databases

eggNOGCOG2273.
HOGENOMHOG000236368.
InParanoidQ9ZSU4.
KOK08235.
OMAANIFENG.
PhylomeDBQ9ZSU4.
ProtClustDBCLSN2685868.

Enzyme and pathway databases

BioCycARA:AT4G25820-MONOMER.
BRENDA2.4.1.207. 399.

Gene expression databases

GenevestigatorQ9ZSU4.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFPIRSF005604. XET. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXTH14_ARATH
AccessionPrimary (citable) accession number: Q9ZSU4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names