Q2QSB9 (AMPL1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 40.
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: Putative leucine aminopeptidase 1 EC=3.4.11.1 Alternative name(s): Leucyl aminopeptidase 1 Short name=LAP 1 Proline aminopeptidase 1 EC=3.4.11.5 Prolyl aminopeptidase 1 | ||
| Gene names |
| ||
| Organism | Oryza sativa subsp. japonica (Rice) | ||
| Taxonomic identifier | 39947 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza |
Protein attributes
| Sequence length | 542 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity. |
| Catalytic activity | Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. Release of N-terminal proline from a peptide. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Subunit structure | Homohexamer Probable. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase M17 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Aminopeptidase Hydrolase Protease |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 542 | 542 | Putative leucine aminopeptidase 1 | PRO_0000247502 | |||||
Sites | |||||||||
| Active site | 323 | 1 | Potential | ||||||
| Active site | 400 | 1 | Potential | ||||||
| Metal binding | 294 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 299 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 299 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 336 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 396 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 398 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 398 | 1 | Zinc 2 By similarity | ||||||
Sequences
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References
| [1] | "The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications." The rice chromosomes 11 and 12 sequencing consortia BMC Biol. 3:20-20(2005) [PubMed: 16188032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DP000011 Genomic DNA. Translation: ABA97701.2. |
| RefSeq | NP_001066684.1. NM_001073216.1. |
| UniGene | Os.79677. |
3D structure databases | |
| ProteinModelPortal | Q2QSB9. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q2QSB9. |
Protein family/group databases | |
| MEROPS | M17.002. |
Proteomic databases | |
| PRIDE | Q2QSB9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | LOC_Os12g24650.1; LOC_Os12g24650.1; LOC_Os12g24650. |
| GeneID | 4352123. |
| KEGG | osa:4352123. |
Phylogenomic databases | |
| GeneTree | EPGT00070000029661. |
| OMA | FISAACE. |
| PhylomeDB | Q2QSB9. |
| ProtClustDB | CLSN2683023. |
Family and domain databases | |
| InterPro | IPR000819. Peptidase_M17_C. IPR023042. Peptidase_M17_cytosol_amino. IPR008283. Peptidase_M17_N. [Graphical view] |
| KO | K01255. |
| Pfam | PF00883. Peptidase_M17. 1 hit. PF02789. Peptidase_M17_N. 1 hit. [Graphical view] |
| PROSITE | PS00631. CYTOSOL_AP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPL1_ORYSJ | ||||||||
| Accession | Primary (citable) accession number: Q2QSB9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| Oryza sativa (rice) Index of Oryza sativa entries and their corresponding gene designations |
| SIMILARITY comments Index of protein domains and families |

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