ID   ACPH_PIG                Reviewed;         732 AA.
AC   P19205; Q9TS46;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 124.
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;
GN   Name=APEH;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT
RP   MET-1.
RC   TISSUE=Liver;
RX   PubMed=2691504; DOI=10.1093/oxfordjournals.jbchem.a122891;
RA   Mitta M., Asada K., Uchimura Y., Kimizuka F., Kato I., Sakiyama F.,
RA   Tsunasawa S.;
RT   "The primary structure of porcine liver acylamino acid-releasing enzyme
RT   deduced from cDNA sequences.";
RL   J. Biochem. 106:548-551(1989).
RN   [2]
RP   PROTEIN SEQUENCE, ACETYLATION AT MET-1, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND ACTIVE SITE SER-587.
RC   TISSUE=Liver;
RX   PubMed=8576092; DOI=10.1093/oxfordjournals.jbchem.a124979;
RA   Miyagi M., Sakiyama F., Kato I., Tsunasawa S.;
RT   "Complete covalent structure of porcine liver acylamino acid-releasing
RT   enzyme and identification of its active site serine residue.";
RL   J. Biochem. 118:771-779(1995).
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}.
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DR   EMBL; D00524; BAA00411.1; -; mRNA.
DR   PIR; JU0132; JU0132.
DR   RefSeq; NP_999088.1; NM_213923.1.
DR   AlphaFoldDB; P19205; -.
DR   STRING; 9823.ENSSSCP00000012138; -.
DR   BindingDB; P19205; -.
DR   ChEMBL; CHEMBL2021757; -.
DR   ESTHER; pig-acph; ACPH_Peptidase_S9.
DR   MEROPS; S09.004; -.
DR   iPTMnet; P19205; -.
DR   PaxDb; P19205; -.
DR   PeptideAtlas; P19205; -.
DR   PRIDE; P19205; -.
DR   GeneID; 396961; -.
DR   KEGG; ssc:396961; -.
DR   CTD; 327; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   InParanoid; P19205; -.
DR   OrthoDB; 265965at2759; -.
DR   PRO; PR:P19205; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.120.10.30; -; 1.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR045550; AARE_N.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF19283; APEH_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..732
FT                   /note="Acylamino-acid-releasing enzyme"
FT                   /id="PRO_0000122432"
FT   ACT_SITE        587
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084,
FT                   ECO:0000269|PubMed:8576092"
FT   ACT_SITE        675
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        707
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:2691504,
FT                   ECO:0000269|PubMed:8576092"
FT   MOD_RES         187
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13798"
FT   CONFLICT        167
FT                   /note="D -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   732 AA;  81244 MW;  017BD40E049A604C CRC64;
     MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GRYRTVHTEW TQRDLERMEN
     IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTGTAEEKQF
     LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVADKKR PKAESFFQTK
     ALDVTGSDDE MARTKKPDQA IKGDQFLFYE DWGENMVSKS TPVLCVLDIE SGNISVLEGV
     PESVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLTGG KCELLSDESV
     AVTSPRLSPD QCRIVYLRFP SLVPHQQCGQ LCLYDWYTRV TSVVVDIVPR QLGEDFSGIY
     CSLLPLGCWS ADSQRVVFDS PQRSRQDLFA VDTQMGSVTS LTAGGSGGSW KLLTIDRDLM
     VVQFSTPSVP PSLKVGFLPP AGKEQAVSWV SLEEAEPFPD ISWSIRVLQP PPQQEHVQYA
     GLDFEAILLQ PSNSPEKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS
     TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDAGR VALMGGSHGG FLSCHLIGQY
     PETYSACVVR NPVINIASMM GSTDIPDWCM VEAGFSYSSD CLPDLSVWAA MLDKSPIKYA
     PQVKTPLLLM LGQEDRRVPF KQGMEYYRVL KARNVPVRLL LYPKSTHALS EVEVESDSFM
     NAVLWLCTHL GS