P19205 · ACPH_PIG
- ProteinAcylamino-acid-releasing enzyme
- GeneAPEH
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids732 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
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 (By similarity).
It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity).
Also, involved in the degradation of oxidized and glycated proteins (By similarity).
It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By similarity).
Also, involved in the degradation of oxidized and glycated proteins (By similarity).
Catalytic activity
Activity regulation
Homotetramerization is required for activity (Probable). Tetramerization results in the formation of a gated channel which is involved in substrate selection and substrate access to the catalytic sites (Probable).
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 587 | Charge relay system | ||||
Sequence: S | ||||||
Active site | 675 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 707 | Charge relay system | ||||
Sequence: H |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | omega peptidase activity | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAcylamino-acid-releasing enzyme
- EC number
- Short namesAARE
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionP19205
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000122432 | 1-732 | Acylamino-acid-releasing enzyme | |||
Sequence: MERQVLLSEPEEAAALYRGLSRQPALSAACLGPEVTTQYGGRYRTVHTEWTQRDLERMENIRFCRQYLVFHDGDSVVFAGPAGNSVETRGELLSRESPSGTMKAVLRKAGGTGTAEEKQFLEVWEKNRKLKSFNLSALEKHGPVYEDDCFGCLSWSHSETHLLYVADKKRPKAESFFQTKALDVTGSDDEMARTKKPDQAIKGDQFLFYEDWGENMVSKSTPVLCVLDIESGNISVLEGVPESVSPGQAFWAPGDTGVVFVGWWHEPFRLGIRFCTNRRSALYYVDLTGGKCELLSDESVAVTSPRLSPDQCRIVYLRFPSLVPHQQCGQLCLYDWYTRVTSVVVDIVPRQLGEDFSGIYCSLLPLGCWSADSQRVVFDSPQRSRQDLFAVDTQMGSVTSLTAGGSGGSWKLLTIDRDLMVVQFSTPSVPPSLKVGFLPPAGKEQAVSWVSLEEAEPFPDISWSIRVLQPPPQQEHVQYAGLDFEAILLQPSNSPEKTQVPMVVMPHGGPHSSFVTAWMLFPAMLCKMGFAVLLVNYRGSTGFGQDSILSLPGNVGHQDVKDVQFAVEQVLQEEHFDAGRVALMGGSHGGFLSCHLIGQYPETYSACVVRNPVINIASMMGSTDIPDWCMVEAGFSYSSDCLPDLSVWAAMLDKSPIKYAPQVKTPLLLMLGQEDRRVPFKQGMEYYRVLKARNVPVRLLLYPKSTHALSEVEVESDSFMNAVLWLCTHLGS | ||||||
Modified residue | 187 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the liver (at protein level).
Structure
Sequence
- Sequence statusComplete
- Length732
- Mass (Da)81,244
- Last updated1996-02-01 v2
- Checksum017BD40E049A604C
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 167 | in Ref. 2; AA sequence | ||||
Sequence: D → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D00524 EMBL· GenBank· DDBJ | BAA00411.1 EMBL· GenBank· DDBJ | mRNA |