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Q9SVV2 (XTH26_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

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

Names and origin

Protein namesRecommended name:
Probable xyloglucan endotransglucosylase/hydrolase protein 26
Short name=At-XTH26
Short name=XTH-26
EC=2.4.1.207
Gene names
Name:XTH26
Synonyms:XTR18
Ordered Locus Names:At4g28850
ORF Names:F16A16.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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.

Subcellular location

Secreted › cell wall Probable. Secreted › extracellular space › apoplast Probable.

Post-translational modification

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

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 – 292265Probable xyloglucan endotransglucosylase/hydrolase protein 26
PRO_0000011826

Sites

Active site1011Nucleophile By similarity
Active site1051Proton donor By similarity

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SVV2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 32CD5FFE6707FA28

FASTA29232,924
        10         20         30         40         50         60 
MAGLQAKTLM FVLAAALATL GRTFVEADFS KNFIVTWGKD HMFMNGTNLR LVLDKSAGSA 

        70         80         90        100        110        120 
IKSKVAHLFG SVEMLIKLVP GNSAGTVAAY YLSSTGSTHD EIDFEFLGNA TGQPYTIHTN 

       130        140        150        160        170        180 
LYAQGKGNRE QQFRPWFNPT NGFHNYTIHW NPSEVVWFVD GTPIRVFRNY ESEGIAYPNK 

       190        200        210        220        230        240 
QGMKVFASLW NAEDWATQGG RVKTNWTLAP FVAEGRRYKA RACLWKGSVS IKQCVDPTIR 

       250        260        270        280        290 
SNWWTSPSFS QLTASQLTKM QKIRDGFMIY DYCKDTNRFK GVMPPECSKK QF

« Hide

References

« Hide 'large scale' references
[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. 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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"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.

Web resources

XTH-World

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL035353 Genomic DNA. Translation: CAA22967.1.
AL161573 Genomic DNA. Translation: CAB81473.1.
CP002687 Genomic DNA. Translation: AEE85554.1.
AK230242 mRNA. Translation: BAF02046.1.
IPIIPI00541410.
PIRT04514.
RefSeqNP_194614.1. NM_119029.2.
UniGeneAt.50378.

3D structure databases

ProteinModelPortalQ9SVV2.
SMRQ9SVV2. Positions 29-291.
ModBaseSearch...

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PaxDbQ9SVV2.
PRIDEQ9SVV2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G28850.1; AT4G28850.1; AT4G28850.
GeneID829006.
KEGGath:AT4G28850.

Organism-specific databases

TAIRAt4g28850.

Phylogenomic databases

eggNOGCOG2273.
HOGENOMHOG000236368.
InParanoidQ9SVV2.
KOK08235.
OMAASSSNWY.
PhylomeDBQ9SVV2.
ProtClustDBPLN03161.

Gene expression databases

GenevestigatorQ9SVV2.
GermOnlineAT4G28850. Arabidopsis thaliana.

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. ConA_like_lec_gl. 1 hit.
PROSITEPS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXTH26_ARATH
AccessionPrimary (citable) accession number: Q9SVV2
Secondary accession number(s): Q0WLG1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

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