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Q9SMP1 (XTH11_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 103. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable xyloglucan endotransglucosylase/hydrolase protein 11

Short name=At-XTH11
Short name=XTH-11
EC=2.4.1.207
Gene names
Name:XTH11
Ordered Locus Names:At3g48580
ORF Names:T8P19.90
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May catalyze 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

Secretedcell wall Probable. Secretedextracellular spaceapoplast 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 1 subfamily.

Caution

In contrast to other xyloglucan endotransglucosylase proteins, the catalytic motif is atypical and lacks the proton donor site. It therefore may not be functional in vivo.

Sequence caution

The sequence AAM66971.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAB62347.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentApoplast
Cell wall
Secreted
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular glucan metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds

Inferred from electronic annotation. Source: InterPro

xyloglucan:xyloglucosyl transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9SMP1-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 277253Probable xyloglucan endotransglucosylase/hydrolase protein 11
PRO_0000011811

Sites

Active site1071Nucleophile By similarity

Amino acid modifications

Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: 0ED0BC4CD7AD0F2D

FASTA27731,939
        10         20         30         40         50         60 
MRGSDQKILL MVMVVVAVVA AAQGQEETTG FVTWGNNYYQ TWGHQALVIN KTSELQLTLD 

        70         80         90        100        110        120 
KNSGSGFESQ LIYGSGYFNV RIKAPQTTST GVITSFYLIS RSSRHDELCF QILGKNGPPY 

       130        140        150        160        170        180 
LLNTNMYLYG EGGKDQRFRL WFDPTKDYHS YSFLWNPNQL VFYVDDTPIR VYSKNPDVYY 

       190        200        210        220        230        240 
PSVQTMFLMG SVQNGSIIDP KQMPYIAKFQ ASKIEGCKTE FMGIDKCTDP KFWWNRKQLS 

       250        260        270 
SKEKTLYLNA RKTYLDYDYC SDRQRYPKVP QECGSYT 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [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]"Arabidopsis ORF Clones."
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
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]"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
AL133315 Genomic DNA. Translation: CAB62347.1. Different initiation.
CP002686 Genomic DNA. Translation: AEE78432.1.
BT025721 mRNA. Translation: ABF82624.1.
AY088649 mRNA. Translation: AAM66971.1. Different initiation.
PIRT46202.
RefSeqNP_566910.1. NM_114717.2. [Q9SMP1-1]
UniGeneAt.35708.

3D structure databases

ProteinModelPortalQ9SMP1.
SMRQ9SMP1. Positions 32-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT3G48580.1-P.

Protein family/group databases

CAZyGH16. Glycoside Hydrolase Family 16.

Proteomic databases

PaxDbQ9SMP1.
PRIDEQ9SMP1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G48580.1; AT3G48580.1; AT3G48580. [Q9SMP1-1]
GeneID824018.
KEGGath:AT3G48580.

Organism-specific databases

TAIRAT3G48580.

Phylogenomic databases

eggNOGNOG242693.
HOGENOMHOG000236368.
InParanoidQ9SMP1.
KOK08235.
OMAFEMERIR.

Enzyme and pathway databases

BioCycARA:AT3G48580-MONOMER.
ARA:GQT-2167-MONOMER.

Gene expression databases

GenevestigatorQ9SMP1.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008264. Beta_glucanase.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000757. Glyco_hydro_16.
IPR016455. XET.
IPR010713. XET_C.
[Graphical view]
PfamPF00722. Glyco_hydro_16. 1 hit.
PF06955. XET_C. 1 hit.
[Graphical view]
PIRSFPIRSF005604. XET. 1 hit.
PRINTSPR00737. GLHYDRLASE16.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameXTH11_ARATH
AccessionPrimary (citable) accession number: Q9SMP1
Secondary accession number(s): Q1ECL3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2003
Last sequence update: May 31, 2011
Last modified: May 14, 2014
This is version 103 of the entry and version 2 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