Reviewed,
UniProtKB/Swiss-Prot Q9ZU91 (E133_ARATH)
Last modified
June 16, 2009.
Version 64.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Arabidopsis thaliana (Mouse-ear cress) [Complete proteome] | ||||
| Taxonomic identifier | 3702 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis |
Protein attributes
| Sequence length | 501 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. |
| Subcellular location | |
| Sequence similarities | Belongs to the glycosyl hydrolase 17 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Plant defense |
| Cellular component | Cell membrane Membrane |
| Coding sequence diversity | Alternative splicing |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | GPI-anchor Glycoprotein Lipoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense responseInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | anchored to plasma membrane Ref.3 Inferred from direct assay. Source: TAIR |
| Molecular function | cation binding Inferred from electronic annotation. Source: InterPro glucan endo-1,3-beta-D-glucosidase activityInferred 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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||
| Chain | 19 – 483 | 465 | Putative glucan endo-1,3-beta-glucosidase 3 | PRO_0000011886 | |||||
| Propeptide | 484 – 501 | 18 | Removed in mature form Potential | PRO_0000011887 | |||||
Sites | |||||||||
| Active site | 263 | 1 | Nucleophile By similarity | ||||||
| Active site | 326 | 1 | Proton donor By similarity | ||||||
Amino acid modifications | |||||||||
| Lipidation | 483 | 1 | GPI-anchor amidated serine Potential | ||||||
| Glycosylation | 88 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 107 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 171 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 253 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 295 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 353 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 357 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 451 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 456 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 457 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 466 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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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. 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. |
Cross-references
Sequence databases | |
|---|---|
| AC006069 Genomic DNA. Translation: AAD12708.2. AY085500 mRNA. Translation: AAM62724.1. | |
| IPI | IPI00518068. |
| PIR | B84427. |
| RefSeq | NP_565269.1. |
| UniGene | At.27628 At.72695 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GHS based on UniProtKB P15737. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM43. Carbohydrate-Binding Module Family 43. GH17. Glycoside Hydrolase Family 17. |
Proteomic databases | |
| PRIDE | Q9ZU91. |
Genome annotation databases | |
| GeneID | 814692. |
| GenomeReviews | Gene locus AT2G01630 in contig CT485783_GR. |
| NMPDR | fig|3702.1.peg.7766. |
Organism-specific databases | |
| TAIR | At2g01630. |
Phylogenomic databases | |
| OMA | Q9ZU91. LPPNKEA. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.39. 302. |
Gene expression databases | |
| ArrayExpress | Q9ZU91. |
| GermOnline | AT2G01630. Arabidopsis thaliana. |
Family and domain databases | |
| InterPro | IPR000490. Glyco_hydro_17. IPR013781. Glyco_hydro_sg_catalytic. IPR012946. X8. [Graphical view] |
| Gene3D | G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. |
| Pfam | PF00332. Glyco_hydro_17. 1 hit. PF07983. X8. 1 hit. [Graphical view] |
| SMART | SM00768. X8. 1 hit. [Graphical view] |
| PROSITE | PS00587. GLYCOSYL_HYDROL_F17. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | E133_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9ZU91 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
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 |

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