Reviewed,
UniProtKB/Swiss-Prot Q6AYS7 (ACY1A_RAT)
Last modified
November 3, 2009.
Version 43.
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: Aminoacylase-1A EC=3.5.1.14 Alternative name(s): N-acyl-L-amino-acid amidohydrolase ACY-1A ACY IA | ||||
| 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 | 408 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) By similarity. |
| Catalytic activity | An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid. |
| Cofactor | Binds 2 zinc ions per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the peptidase M20A family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fractionInferred from direct assay. Source: RGD |
| Molecular function | aminoacylase activity Inferred from direct assay. Source: RGD metallopeptidase activityInferred from electronic annotation. Source: InterPro protein dimerization activityInferred from electronic annotation. Source: InterPro zinc 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 – 408 | 408 | Aminoacylase-1A | PRO_0000274009 | |||||
Sites | |||||||||
| Active site | 82 | 1 | By similarity | ||||||
| Active site | 147 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 80 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 113 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 113 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 148 | 1 | Zinc 2 By similarity | ||||||
| Metal binding | 175 | 1 | Zinc 1 By similarity | ||||||
| Metal binding | 373 | 1 | Zinc 2 By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 3 – 8 | 6 | TKGPES → SKVPEE in AAS90690. Ref.1 | ||||||
| Sequence conflict | 132 | 1 | G → S in AAS90690. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The rat kidney acylase 1. Evidence for a new cDNA form and comparisons with the porcine intestinal enzyme." Perrier J., Durand A., Giardina T., Puigserver A. Comp. Biochem. Physiol. 138B:277-283(2004) [PubMed: 15253876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar. |
| [2] | "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: Kidney. |
| [3] | Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 89-100; 116-126; 169-190 AND 368-378, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AY580164 mRNA. Translation: AAS90690.1. BC078930 mRNA. Translation: AAH78930.1. | |
| IPI | IPI00464791. |
| RefSeq | NP_001005383.1. |
| UniGene | Rn.3679 |
3D structure databases | |
| SMR | Q6AYS7. Positions 7-198, 321-408. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6AYS7. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000015851; ENSRNOP00000015852; ENSRNOG00000011189; Rattus norvegicus. [Genome view] |
| GeneID | 300981. |
| KEGG | rno:300981. |
| UCSC | NM_001005383. rat. |
Organism-specific databases | |
| CTD | 300981. |
| RGD | 2030. Acy1. |
Phylogenomic databases | |
| HOVERGEN | Q6AYS7. |
| OMA | KSVSIQY. |
Enzyme and pathway databases | |
| BRENDA | 3.5.1.14. 248. |
Gene expression databases | |
| ArrayExpress | Q6AYS7. |
| Genevestigator | Q6AYS7. |
Family and domain databases | |
| InterPro | IPR001261. ArgE/DapE_CS. IPR010159. N-acyl_aa_amidohydrolase. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view] |
| Pfam | PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view] |
| PIRSF | PIRSF036696. ACY-1. 1 hit. |
| TIGRFAMs | TIGR01880. Ac-peptdase-euk. 1 hit. |
| PROSITE | PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 647830. |
Entry information
| Entry name | ACY1A_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6AYS7 Secondary accession number(s): Q6PTT1 | ||||||||
| 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


