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P25154

- ACPH_RABIT

UniProt

P25154 - ACPH_RABIT

Protein

Acylamino-acid-releasing enzyme

Gene

APEH

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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 activityi

    Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acylamino-acid-releasing enzyme (EC:3.4.19.1)
    Short name:
    AARE
    Alternative name(s):
    Acyl-peptide hydrolase
    Short name:
    APH
    Acylaminoacyl-peptidase
    Gene namesi
    Name:APEH
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›6›6Acylamino-acid-releasing enzymePRO_0000122433

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Homotetramer.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9C family.Curated

    Sequencei

    Sequence statusi: Fragment.

    Length:6
    Mass (Da):775
    Last modified:May 1, 1992 - v1
    Checksum:i6732D6C40B16F000
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei6 – 61

    Sequence databases

    PIRiA49792.

    Cross-referencesi

    Sequence databases

    PIRi A49792.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
      Tissue: Muscle.

    Entry informationi

    Entry nameiACPH_RABIT
    AccessioniPrimary (citable) accession number: P25154
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3