Reviewed,
UniProtKB/Swiss-Prot P25154 (ACPH_RABIT)
Last modified
June 16, 2009.
Version 46.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Acylamino-acid-releasing enzyme Short name=AARE EC=3.4.19.1 Alternative name(s): Acyl-peptide hydrolase Short name=APH Acylaminoacyl-peptidase | ||
| Gene names |
| ||
| Organism | Oryctolagus cuniculus (Rabbit) | ||
| Taxonomic identifier | 9986 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 6 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser. |
| Catalytic activity | Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S9C family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| PTM | Acetylation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | hydrolase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "N-terminal sequence analysis of N alpha-acetylated proteins after unblocking with N-acylaminoacyl-peptide hydrolase." Krishna R.G., Chin C.C.Q., Wold F. Anal. Biochem. 199:45-50(1991) [PubMed: 1807161] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Muscle. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A49792. |
3D structure databases | |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P25154. |
Enzyme and pathway databases | |
| BRENDA | 3.4.19.1. 255. |
Family and domain databases | |
| InterPro | IPR002471. Pept_S9_AS. [Graphical view] |
| PROSITE | PS00708. PRO_ENDOPEP_SER. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACPH_RABIT | ||||||||
| Accession | Primary (citable) accession number: P25154 | ||||||||
| Entry history |
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| 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


