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Reviewed, UniProtKB/Swiss-Prot P25154 (ACPH_RABIT)

Last modified June 16, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Name: APEH
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length6 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Cytoplasm.

Sequence similarities

Belongs to the peptidase S9C family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›6›6Acylamino-acid-releasing enzyme
PRO_0000122433

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1

Experimental info

Non-terminal residue61

Sequences

Sequence LengthMass (Da)Tools
P25154-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 6732D6C40B16F000

FASTA6775
MERQVL 

« Hide

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

PIRA49792.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP25154.

Enzyme and pathway databases

BRENDA3.4.19.1. 255.

Family and domain databases

InterProIPR002471. Pept_S9_AS.
[Graphical view]
PROSITEPS00708. PRO_ENDOPEP_SER. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACPH_RABIT
AccessionPrimary (citable) accession number: P25154
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents