Reviewed,
UniProtKB/Swiss-Prot Q68FS4 (AMPL_RAT)
Last modified
January 19, 2010.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Cytosol aminopeptidase EC=3.4.11.1 Alternative name(s): Leucine aminopeptidase Leucyl aminopeptidase Leucine aminopeptidase 3 Short name=LAP Proline aminopeptidase EC=3.4.11.5 Prolyl aminopeptidase | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 519 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
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. One zinc ion is tightly bound and essential for enzyme activity, while the second metal coordination site can be occupied by zinc, magnesium or manganese to give enzymes of different activities By similarity. |
| Subunit structure | Homohexamer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase M17 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Alternative initiation |
| Ligand | Magnesium Manganese Metal-binding Zinc |
| Molecular function | Aminopeptidase Hydrolase Protease |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activityInferred from electronic annotation. Source: InterPro zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q68FS4-1) 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. | ||||||
| Isoform 2 (identifier: Q68FS4-2) The sequence of this isoform differs from the canonical sequence as follows: 1-31: Missing. | ||||||
| Note: The initiator methionine is removed. No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 519 | 519 | Cytosol aminopeptidase | PRO_0000274146 | |||||
Sites | |||||||||
| Active site | 294 | 1 | By similarity | ||||||
| Active site | 368 | 1 | By similarity | ||||||
| Metal binding | 282 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 287 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 287 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 305 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 364 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 366 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 366 | 1 | Zinc 2 By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 33 | 1 | N-acetylthreonine By similarity | ||||||
| Modified residue | 221 | 1 | N6-acetyllysine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 31 | 31 | Missing in isoform 2. | VSP_022633 | |||||
Sequences
| ||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
| [2] | Lubec G., Afjehi-Sadat L., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 69-79; 85-103; 189-200; 283-294; 322-342; 369-384; 441-455; 458-469; 477-496 AND 506-513, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC079381 mRNA. Translation: AAH79381.1. |
| IPI | IPI00471530. IPI00829505. |
| RefSeq | NP_001011910.1. |
| UniGene | Rn.99790 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LAP based on UniProtKB P00727. |
| SMR | Q68FS4. Positions 33-518. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q68FS4. |
Protein family/group databases | |
| MEROPS | M17.001. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000004770; ENSRNOP00000004770; ENSRNOG00000003289; Rattus norvegicus. [Genome view] |
| GeneID | 289668. |
| KEGG | rno:289668. |
| UCSC | NM_001011910. rat. |
Organism-specific databases | |
| CTD | 289668. |
| RGD | 1307985. Lap3. |
Phylogenomic databases | |
| eggNOG | maNOG07537. |
| HOVERGEN | Q68FS4. |
| InParanoid | Q68FS4. |
| OMA | GIYSKDK. |
| OrthoDB | EOG9WQ3NS. |
| PhylomeDB | Q68FS4. |
Enzyme and pathway databases | |
| BRENDA | 3.4.11.1. 248. 3.4.11.5. 248. |
Gene expression databases | |
| ArrayExpress | Q68FS4. |
| Genevestigator | Q68FS4. |
Family and domain databases | |
| InterPro | IPR011356. Peptidase_M17. IPR000819. Peptidase_M17_C. IPR008283. Peptidase_M17_N. [Graphical view] |
| PANTHER | PTHR11963:SF3. Peptidase_M17. 1 hit. |
| Pfam | PF00883. Peptidase_M17. 1 hit. PF02789. Peptidase_M17_N. 1 hit. [Graphical view] |
| PRINTS | PR00481. LAMNOPPTDASE. |
| PROSITE | PS00631. CYTOSOL_AP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 630137. |
Entry information
| Entry name | AMPL_RAT | ||||||||
| Accession | Primary (citable) accession number: Q68FS4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


