Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9ZU91 (E133_ARATH)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Putative glucan endo-1,3-beta-glucosidase 3
    EC=3.2.1.39
Alternative name(s):
    (1->3)-beta-glucan endohydrolase 3
      Short name=(1->3)-beta-glucanase 3
    Beta-1,3-endoglucanase 3
      Short name=Beta-1,3-glucanase 3
Gene names
Ordered Locus Names: At2g01630
ORF Names: T8O11.20
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Hide | Top

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity

Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor. Ref.3 Ref.4 Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Hide | Top

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentanchored to plasma membrane Ref.3

Inferred from direct assay. Source: TAIR

   Molecular functioncation binding

Inferred from electronic annotation. Source: InterPro

glucan endo-1,3-beta-D-glucosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

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: Q9ZU91-1)

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.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 483465Putative glucan endo-1,3-beta-glucosidase 3
PRO_0000011886
Propeptide484 – 50118Removed in mature form Potential
PRO_0000011887

Sites

Active site2631Nucleophile By similarity
Active site3261Proton donor By similarity

Amino acid modifications

Lipidation4831GPI-anchor amidated serine Potential
Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1711N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation4511N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential

Hide | Top

Sequences

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

Last modified June 1, 2002. Version 2.
Checksum: 3858B1C25FD37920

FASTA50153,992
        10         20         30         40         50         60 
MAALLLLFLF LFASSALSQD SLIGVNIGTE VTNMPSPTQV VALLKSQNIN RVRLYDADRS 

        70         80         90        100        110        120 
MLLAFAHTGV QVIISVPNDQ LLGISQSNAT AANWVTRNVA AYYPATNITT IAVGSEVLTS 

       130        140        150        160        170        180 
LTNAASVLVS ALKYIQAALV TANLDRQIKV STPHSSTIIL DSFPPSQAFF NKTWDPVIVP 

       190        200        210        220        230        240 
LLKFLQSTGS PLLLNVYPYF DYVQSNGVIP LDYALFQPLQ ANKEAVDANT LLHYTNVFDA 

       250        260        270        280        290        300 
IVDAAYFAMS YLNFTNIPIV VTESGWPSKG GPSEHDATVE NANTYNSNLI QHVINKTGTP 

       310        320        330        340        350        360 
KHPGTAVTTY IYELYNEDTR PGPVSEKNWG LFYTNGTPVY TLRLAGAGAI LANDTTNQTF 

       370        380        390        400        410        420 
CIAKEKVDRK MLQAALDWAC GPGKVDCSAL MQGESCYEPD DVVAHSTYAF NAYYQKMGKA 

       430        440        450        460        470        480 
SGSCDFKGVA TVTTTDPSRG TCVFPGSAKS NQTLGNNTSA LAPSANSTTS GCIPKYYHHP 

       490        500 
HASFGDLTLL SLLLIIALVF L

« Hide

Hide | Top

References

[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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].
[3]"Identification of glycosylphosphatidylinositol-anchored proteins in Arabidopsis. A proteomic and genomic analysis."
Borner G.H.H., Lilley K.S., Stevens T.J., Dupree P.
Plant Physiol. 132:568-577(2003) [PubMed: 12805588] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
Tissue: Callus.
[4]"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins."
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C., Jensen O.N.
Mol. Cell. Proteomics 2:1261-1270(2003) [PubMed: 14517339] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]"Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
J. Proteome Res. 5:935-943(2006) [PubMed: 16602701] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Hide | Top

Cross-references

Sequence databases

AC006069 Genomic DNA. Translation: AAD12708.2.
AY085500 mRNA. Translation: AAM62724.1.
IPIIPI00518068.
PIRB84427.
RefSeqNP_565269.1.
UniGeneAt.27628
At.72695

3D structure databases

HSSPHSSP built from PDB template 1GHS based on UniProtKB P15737.
ModBaseSearch...

Protein family/group databases

CAZyCBM43. Carbohydrate-Binding Module Family 43.
GH17. Glycoside Hydrolase Family 17.

Proteomic databases

PRIDEQ9ZU91.

Genome annotation databases

GeneID814692.
GenomeReviewsGene locus AT2G01630 in contig CT485783_GR.
NMPDRfig|3702.1.peg.7766.

Organism-specific databases

TAIRAt2g01630.

Phylogenomic databases

OMAQ9ZU91. LPPNKEA.

Enzyme and pathway databases

BRENDA3.2.1.39. 302.

Gene expression databases

ArrayExpressQ9ZU91.
GermOnlineAT2G01630. Arabidopsis thaliana.

Family and domain databases

InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_sg_catalytic.
IPR012946. X8.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTSM00768. X8. 1 hit.
[Graphical view]
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameE133_ARATH
AccessionPrimary (citable) accession number: Q9ZU91
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents