ID   ACPH_BOVIN              Reviewed;         730 AA.
AC   P80227; A4FUX4;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 126.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 194-213.
RC   TISSUE=Lens;
RX   PubMed=8375399; DOI=10.1111/j.1432-1033.1993.tb18183.x;
RA   Sharma K.K., Ortwerth B.J.;
RT   "Bovine lens acylpeptide hydrolase. Purification and characterization of a
RT   tetrameric enzyme resistant to urea denaturation and proteolytic
RT   inactivation.";
RL   Eur. J. Biochem. 216:631-637(1993).
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; BC123400; AAI23401.1; -; mRNA.
DR   PIR; S36842; S36842.
DR   RefSeq; NP_001076900.1; NM_001083431.1.
DR   AlphaFoldDB; P80227; -.
DR   STRING; 9913.ENSBTAP00000015388; -.
DR   ESTHER; bovin-acph; ACPH_Peptidase_S9.
DR   MEROPS; S09.004; -.
DR   PaxDb; P80227; -.
DR   PRIDE; P80227; -.
DR   Ensembl; ENSBTAT00000015388; ENSBTAP00000015388; ENSBTAG00000011583.
DR   GeneID; 514666; -.
DR   KEGG; bta:514666; -.
DR   CTD; 327; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011583; -.
DR   VGNC; VGNC:26010; APEH.
DR   eggNOG; KOG2100; Eukaryota.
DR   GeneTree; ENSGT00390000013172; -.
DR   HOGENOM; CLU_014230_1_1_1; -.
DR   InParanoid; P80227; -.
DR   OMA; FVVDTQM; -.
DR   OrthoDB; 265965at2759; -.
DR   TreeFam; TF312937; -.
DR   Proteomes; UP000009136; Chromosome 22.
DR   Bgee; ENSBTAG00000011583; Expressed in digestive system secreted substance and 107 other tissues.
DR   ExpressionAtlas; P80227; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:Ensembl.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:Ensembl.
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..730
FT                   /note="Acylamino-acid-releasing enzyme"
FT                   /id="PRO_0000122429"
FT   ACT_SITE        585
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        673
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        705
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P13798"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13798"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P13798"
SQ   SEQUENCE   730 AA;  81093 MW;  838882B5B703DF15 CRC64;
     MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GRYRTVHTEW TQRDLERMEN
     IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG STGEEKQFLE
     VWEKNRKLKS FNLSALEKHG PVYEDDCFGC LSWSHSETHL LYVAEKKRPK AESFFQTKAL
     DISGSDDEMA RPKKPDQAIK GDQFLFYEDW GENMVSKGSP VLCVLDIESG NISVLEGVPE
     SVSPGQAFWA PGDTGVVFAG WWHEPFRLGI RFCTNRRSAL YYVDLTGGNC ELLSDDSLAV
     TSPRLSPDQC RIVYLQFPSL VPHQQCGQLC LYDWYTRVTV VVVDVVPRQL GENFSGIYCS
     LLPLGCWSAD SQRVVFDTAQ RSRQDLFAVD TQMGTVTPLT AGGSGGSWKL LTIDRDLMVA
     QFSTPNLPPC LKVGFLPPAG MEQEVVWVSL EEAEPIPDIS WSIRVLQPPP EQEHAQYVGL
     DFEAILIQPS NPPDKTQVPM VVMPHGGPHS SFVTSWMLLP AMLCKMGFAA LLVNYRGSTG
     FGQDSILSLP GNVGSQDVKD VQFAVEQVLQ EEHFDAGRVA LLGGSHGGFL SCHLIGQYPE
     TYGACVVRNP VINIASMMGS TDIPDWCVVE AGYLYSSDCL PDPNVWSEML NKSPIKYTPQ
     VKTPVLLMLG QEDRRVPFKQ GMEYYRALKA RNVPVRLLLY PKSTHSLSEV EVESDSFMNA
     VIWMCTHLGH