Reviewed,
UniProtKB/Swiss-Prot Q9FJD5 (LAC17_ARATH)
Last modified
November 3, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Laccase-17 EC=1.10.3.2 Alternative name(s): Benzenediol:oxygen oxidoreductase 17 Urishiol oxidase 17 Diphenol oxidase 17 | ||||||
| Gene names |
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| 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 | 577 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Lignin degradation and detoxification of lignin-derived products By similarity. |
| Catalytic activity | 4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O. |
| Cofactor | Binds 4 copper ions per monomer By similarity. |
| Subcellular location | Secreted › extracellular space › apoplast Potential. |
| Tissue specificity | Ubiquitous with higher levels in the inflorescence stem. Ref.3 Ref.4 |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lignin degradation |
| Cellular component | Apoplast Secreted |
| Domain | Repeat Signal |
| Ligand | Copper Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Glycoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW laccase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||
| Chain | 23 – 577 | 555 | Laccase-17 | PRO_0000283645 | |||||
Regions | |||||||||
| Domain | 30 – 146 | 117 | Plastocyanin-like 1 | ||||||
| Domain | 156 – 309 | 154 | Plastocyanin-like 2 | ||||||
| Domain | 427 – 561 | 135 | Plastocyanin-like 3 | ||||||
Sites | |||||||||
| Metal binding | 80 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 82 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 125 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 127 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 478 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 481 | 1 | Copper 1; type 2 By similarity | ||||||
| Metal binding | 483 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 540 | 1 | Copper 3; type 3 By similarity | ||||||
| Metal binding | 541 | 1 | Copper 4; type 1 By similarity | ||||||
| Metal binding | 542 | 1 | Copper 2; type 3 By similarity | ||||||
| Metal binding | 546 | 1 | Copper 4; type 1 By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 35 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 76 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 112 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 185 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 201 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 237 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 297 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 335 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 383 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 391 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 401 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 437 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 444 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 450 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 460 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence features of the regions of 1,013,767 bp covered by sixteen physically assigned P1 and TAC clones." Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N., Tabata S. DNA Res. 5:297-308(1998) [PubMed: 9872454] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [2] | "Arabidopsis ORF clones." Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [3] | "Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana." McCaig B.C., Meagher R.B., Dean J.F.D. Planta 221:619-636(2005) [PubMed: 15940465] [Abstract] Cited for: TISSUE SPECIFICITY. |
| [4] | "Mutant identification and characterization of the laccase gene family in Arabidopsis." Cai X., Davis E.J., Ballif J., Liang M., Bushman E., Haroldsen V., Torabinejad J., Wu Y. J. Exp. Bot. 57:2563-2569(2006) [PubMed: 16804053] [Abstract] Cited for: TISSUE SPECIFICITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AB015475 Genomic DNA. Translation: BAB08370.1. BT015359 mRNA. Translation: AAU05482.1. BT015890 mRNA. Translation: AAU95426.1. | |
| IPI | IPI00539440. |
| RefSeq | NP_200810.1. |
| UniGene | At.7684 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AOZ based on UniProtKB P37064. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9FJD5. |
Genome annotation databases | |
| GeneID | 836124. |
| GenomeReviews | Gene locus AT5G60020 in contig BA000015_GR. |
| KEGG | ath:AT5G60020. |
| NMPDR | fig|3702.1.peg.28007. |
Organism-specific databases | |
| TAIR | At5g60020. |
Phylogenomic databases | |
| OMA | TETILIA. |
Enzyme and pathway databases | |
| BRENDA | 1.10.3.2. 302. |
Gene expression databases | |
| Genevestigator | Q9FJD5. |
Family and domain databases | |
| InterPro | IPR001117. Cu-oxidase. IPR011706. Cu-oxidase_2. IPR011707. Cu-oxidase_3. IPR002355. Cu_oxidase_Cu_BS. IPR008972. Cupredoxin. IPR017761. Laccase. [Graphical view] |
| Gene3D | G3DSA:2.60.40.420. Cupredoxin. 3 hits. |
| Pfam | PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03389. laccase. 1 hit. |
| PROSITE | PS00079. MULTICOPPER_OXIDASE1. 1 hit. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LAC17_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q9FJD5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


