Q9SG80 (ASD1_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 72.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Alpha-L-arabinofuranosidase 1 Short name=AtASD1 EC=3.2.1.55 | ||||||||
| Gene names |
| ||||||||
| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 678 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)
| Function | May be involved in the coordinated dissolution of the cell wall matrix during abscission and in the secondary cell wall formation in xylem vessels. Prefers arabinoxylan, but may also use pectic arabinans as substrates. Ref.6 Ref.7 Ref.8 |
| Catalytic activity | Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.6 Ref.7 |
| Subcellular location | Secreted › extracellular space › extracellular matrix Potential. |
| Tissue specificity | Expressed in roots, leaves, flowers, stems, siliques and seedlings. Observed in zones of cell proliferation, the vascular system and floral abscission zones. Expressed in the guard cells in stems, in xylem vessels and parenchyma cells surrounding the vessels, in the cambium and in the phloem, but not in the secondary xylem. Ref.1 Ref.6 Ref.8 |
| Induction | Not induced by hormones or during leaf senescence. Ref.1 |
| Disruption phenotype | No developmental phenotype, even in a asd1/asd2 double mutant. Ref.8 |
| Sequence similarities | Belongs to the glycosyl hydrolase 51 family. Contains 1 CBM-cenC (cenC-type cellulose-binding) domain. |
| Biophysicochemical properties | Kinetic parameters: KM=0.48 mM for p-nitrophenyl-beta-D-xylopyranoside Ref.6 Ref.7 KM=5.2 mM for (1,5)-alpha-L-arabinobiose (at 37 degrees Celsius) pH dependence: Optimum pH is 4.3. Temperature dependence: Optimum temperature is 67 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro xylan catabolic processInferred from direct assay Ref.6. Source: TAIR |
| Cellular_component | apoplast Inferred from direct assay PubMed 18538804. Source: TAIR plant-type cell wallInferred from direct assay PubMed 17526915. Source: TAIR proteinaceous extracellular matrixInferred from electronic annotation. Source: UniProtKB-SubCell vacuoleInferred from direct assay PubMed 15539469. Source: TAIR |
| Molecular_function | alpha-N-arabinofuranosidase activity Inferred from direct assay Ref.6. Source: TAIR xylan 1,4-beta-xylosidase activityInferred from direct assay Ref.6. Source: TAIR |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 33 | 33 | Potential | ||||||
| Chain | 34 – 678 | 645 | Alpha-L-arabinofuranosidase 1 | PRO_0000384371 | |||||
Regions | |||||||||
| Domain | 152 – 239 | 88 | CBM-cenC | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 181 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 362 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 523 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 555 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 251 | 1 | L → P in AAN28883. Ref.4 | ||||||
| Sequence conflict | 251 | 1 | L → P in AAK50089. Ref.4 | ||||||
| Sequence conflict | 253 – 254 | 2 | QM → HL in AAO92261. Ref.1 | ||||||
| Sequence conflict | 453 | 1 | R → G in AAO92261. Ref.1 | ||||||
| Sequence conflict | 499 | 1 | E → D in AAO92261. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Two alpha-L-arabinofuranosidase genes in Arabidopsis thaliana are differentially expressed during vegetative growth and flower development." Fulton L.M., Cobbett C.S. J. Exp. Bot. 54:2467-2477(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION BY HORMONES. Strain: cv. Columbia. |
| [2] | "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. Tabata S.Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [4] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [5] | "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. Shinozaki K.Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-678. Strain: cv. Columbia. |
| [6] | "Purification and characterization of enzymes exhibiting beta-D-xylosidase activities in stem tissues of Arabidopsis." Minic Z., Rihouey C., Do C.T., Lerouge P., Jouanin L. Plant Physiol. 135:867-878(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY. |
| [7] | "Purification, functional characterization, cloning, and identification of mutants of a seed-specific arabinan hydrolase in Arabidopsis." Minic Z., Do C.-T., Rihouey C., Morin H., Lerouge P., Jouanin L. J. Exp. Bot. 57:2339-2351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES. |
| [8] | "Cell wall modifications in Arabidopsis plants with altered alpha-L-arabinofuranosidase activity." Chavez Montes R.A., Ranocha P., Martinez Y., Minic Z., Jouanin L., Marquis M., Saulnier L., Fulton L.M., Cobbett C.S., Bitton F., Renou J.-P., Jauneau A., Goffner D. Plant Physiol. 147:63-77(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY243509 mRNA. Translation: AAO92261.1. AC011708 Genomic DNA. Translation: AAF19575.1. CP002686 Genomic DNA. Translation: AEE74949.1. AF372949 mRNA. Translation: AAK50089.1. AY143944 mRNA. Translation: AAN28883.1. AK222175 mRNA. Translation: BAD95302.1. AK220766 mRNA. Translation: BAD93969.1. |
| IPI | IPI00526411. |
| RefSeq | NP_187685.1. NM_111911.4. |
| UniGene | At.20271. |
3D structure databases | |
| ProteinModelPortal | Q9SG80. |
| SMR | Q9SG80. Positions 229-559. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 3702.AT3G10740.1-P. |
Protein family/group databases | |
| CAZy | GH51. Glycoside Hydrolase Family 51. |
Proteomic databases | |
| PaxDb | Q9SG80. |
| PRIDE | Q9SG80. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT3G10740.1; AT3G10740.1; AT3G10740. |
| GeneID | 820243. |
| KEGG | ath:AT3G10740. |
Organism-specific databases | |
| TAIR | At3g10740. |
Phylogenomic databases | |
| eggNOG | COG3534. |
| HOGENOM | HOG000115340. |
| InParanoid | Q9SG80. |
| KO | K01209. |
| OMA | LEYLGIG. |
| PhylomeDB | Q9SG80. |
| ProtClustDB | CLSN2684036. |
Gene expression databases | |
| Genevestigator | Q9SG80. |
Family and domain databases | |
| InterPro | IPR010720. Alpha-L-AF_C. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Pfam | PF06964. Alpha-L-AF_C. 1 hit. [Graphical view] |
| SMART | SM00813. Alpha-L-AF_C. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ASD1_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9SG80 Secondary accession number(s): Q56W72 Q94JT7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant 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 |

Clusters with
