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Q9ZU91 (E133_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 93. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

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.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Ontologies

Keywords
   Biological processPlant defense
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGPI-anchor
Glycoprotein
Lipoprotein
   Technical termComplete proteome
Reference 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

Inferred from direct assay Ref.4. Source: TAIR

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

Inferred from electronic annotation. Source: 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: 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 483465Glucan 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

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

References

« Hide 'large scale' 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] [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]"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].
[4]"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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Callus.
[5]"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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"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] [Europe PMC] [Abstract]
Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC006069 Genomic DNA. Translation: AAD12708.2.
CP002685 Genomic DNA. Translation: AEC05475.1.
AY085500 mRNA. Translation: AAM62724.1.
IPIIPI00518068.
PIRB84427.
RefSeqNP_565269.1. NM_126224.2.
UniGeneAt.27628.
At.42475.
At.75580.

3D structure databases

ProteinModelPortalQ9ZU91.
SMRQ9ZU91. Positions 23-342, 359-448.
ModBaseSearch...

Protein family/group databases

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

Proteomic databases

PaxDbQ9ZU91.
PRIDEQ9ZU91.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G01630.1; AT2G01630.1; AT2G01630.
GeneID814692.
KEGGath:AT2G01630.

Organism-specific databases

TAIRAt2g01630.

Phylogenomic databases

eggNOGNOG290245.
HOGENOMHOG000238220.
InParanoidQ9ZU91.
OMAYDADRAM.
PhylomeDBQ9ZU91.
ProtClustDBCLSN2916960.

Gene expression databases

ArrayExpressQ9ZU91.
GenevestigatorQ9ZU91.
GermOnlineAT2G01630. Arabidopsis thaliana.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR012946. X8.
[Graphical view]
PfamPF00332. Glyco_hydro_17. 1 hit.
PF07983. X8. 1 hit.
[Graphical view]
SMARTSM00768. X8. 1 hit.
[Graphical view]
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetSearch...

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: May 1, 2013
This is version 93 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents