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Database: UniProt
Entry: A0A2K5VH05_MACFA
LinkDB: A0A2K5VH05_MACFA
Original site: A0A2K5VH05_MACFA 
ID   A0A2K5VH05_MACFA        Unreviewed;       773 AA.
AC   A0A2K5VH05;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Acylamino-acid-releasing enzyme {ECO:0000256|ARBA:ARBA00018421};
DE            EC=3.4.19.1 {ECO:0000256|ARBA:ARBA00012917};
DE   AltName: Full=Acyl-peptide hydrolase {ECO:0000256|ARBA:ARBA00032596};
DE   AltName: Full=Acylaminoacyl-peptidase {ECO:0000256|ARBA:ARBA00032284};
GN   Name=APEH {ECO:0000313|Ensembl:ENSMFAP00000024050.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000024050.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000024050.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000024050.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00000721};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   AlphaFoldDB; A0A2K5VH05; -.
DR   Ensembl; ENSMFAT00000032188.2; ENSMFAP00000024050.2; ENSMFAG00000043600.2.
DR   VEuPathDB; HostDB:ENSMFAG00000043600; -.
DR   GeneTree; ENSGT00390000013172; -.
DR   Proteomes; UP000233100; Chromosome 2.
DR   Bgee; ENSMFAG00000043600; Expressed in adult mammalian kidney and 13 other cell types or tissues.
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:UniProtKB-EC.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0050435; P:amyloid-beta metabolic process; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IEA:Ensembl.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 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   PANTHER; PTHR42776:SF4; ACYLAMINO-ACID-RELEASING ENZYME; 1.
DR   PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR   Pfam; PF19283; APEH_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   4: Predicted;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT   DOMAIN          42..286
FT                   /note="Acylamino-acid-releasing enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19283"
FT   DOMAIN          523..698
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   773 AA;  85589 MW;  AD7684E8932BC9CD CRC64;
     MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GQYRTVHTEW TQRDLERMEN
     IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG SMKAVLRKAG GTGPGEEKQF
     LEVWEKNRKL KSFNLSVLEK HGPVYEDDCF GCLSWSHSET HLLYVAERKR PKAESFFQTK
     ALDVSASDDE IARLKKPDQP IKGDQFVFYE DWGENMVSKS IPVLCVLDVE SGNISVLEGV
     PENVSPGQAF WAPGDAGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLIGG KCELLSDDSL
     AVSSPRLSPD QCRIVYLQYP SLIPHHQCSQ LCLYDWYTKV TSVVVDIVPR QLGENFSGIY
     CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQVGTVTS LTAGGSGGSW KLLTIDRDLM
     VAQFSTPSLP PTLKVGFLPS AGKEQSVLWV SLEEAEPIPD IHWGIRVLQP PPEQENVQYA
     GLDFEAVLLQ PCNPPDKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS
     TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDASH VALMGGSHGG FISCHLIGQY
     PETYRACVAR NPVINIASML GSTDIPDWCV VEAGFPFSSD CLPDLSVWAE MLDKSPIKYI
     PQVKTPLLLM LGQEDRRVPF KQGMEYYRAL KTRNVPVRHM GSRLGLSQSH DLVNPVHKHR
     DTREDGWPAG PCAHSVGDYN SFQDPAVVGK AGKWAPVVTL ASRRTDEGPG PQQ
//
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