ID   ACPH_RABIT              Reviewed;           6 AA.
AC   P25154;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-DEC-2020, entry version 64.
DE   RecName: Full=Acylamino-acid-releasing enzyme;
DE            Short=AARE;
DE            EC=3.4.19.1;
DE   AltName: Full=Acyl-peptide hydrolase;
DE            Short=APH;
DE   AltName: Full=Acylaminoacyl-peptidase;
DE   Flags: Fragment;
GN   Name=APEH;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC   TISSUE=Muscle;
RX   PubMed=1807161; DOI=10.1016/0003-2697(91)90267-w;
RA   Krishna R.G., Chin C.C.Q., Wold F.;
RT   "N-terminal sequence analysis of N alpha-acetylated proteins after
RT   unblocking with N-acylaminoacyl-peptide hydrolase.";
RL   Anal. Biochem. 199:45-50(1991).
CC   -!- FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal
CC       peptide bond of an N-acetylated peptide to generate an N-acetylated
CC       amino acid and a peptide with a free N-terminus. It preferentially
CC       cleaves off Ac-Ala, Ac-Met and Ac-Ser.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N-
CC         terminus of a polypeptide.; EC=3.4.19.1;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A49792; A49792.
DR   iPTMnet; P25154; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..>6
FT                   /note="Acylamino-acid-releasing enzyme"
FT                   /id="PRO_0000122433"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:1807161"
FT   NON_TER         6
SQ   SEQUENCE   6 AA;  775 MW;  6732D6C40B16F000 CRC64;
     MERQVL