ID A0AAA9T614_BOVIN Unreviewed; 733 AA. AC A0AAA9T614; DT 29-MAY-2024, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 1. DT 27-NOV-2024, entry version 4. 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|VGNC:VGNC:26010}; 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 {ECO:0000313|Ensembl:ENSBTAP00000092000.1, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000092000.1, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000092000.1, RC ECO:0000313|Proteomes:UP000009136}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000092000.1} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000092000.1}; RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. 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. Also, involved in the CC degradation of oxidized and glycated proteins. CC {ECO:0000256|ARBA:ARBA00045885}. 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}. CC -!- SIMILARITY: Belongs to the peptidase S9C family. CC {ECO:0000256|ARBA:ARBA00010040}. 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 Ensembl; ENSBTAT00000117024.1; ENSBTAP00000092000.1; ENSBTAG00000011583.7. DR VGNC; VGNC:26010; APEH. DR GeneTree; ENSGT00390000013172; -. DR Proteomes; UP000009136; Chromosome 22. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR FunFam; 2.120.10.30:FF:000047; Acylamino-acid-releasing enzyme; 1. DR FunFam; 3.40.50.1820:FF:000043; acylamino-acid-releasing enzyme; 1. 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_fold. DR InterPro; IPR002471; Pept_S9_AS. DR InterPro; IPR001375; Peptidase_S9_cat. 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 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}. FT DOMAIN 44..284 FT /note="Acylamino-acid-releasing enzyme N-terminal" FT /evidence="ECO:0000259|Pfam:PF19283" FT DOMAIN 520..699 FT /note="Peptidase S9 prolyl oligopeptidase catalytic" FT /evidence="ECO:0000259|Pfam:PF00326" SQ SEQUENCE 733 AA; 81031 MW; CB7E1D1E8FC0CF44 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 RNVPVRAAVQ FPRAMVAVCS GRTRETVSRF SPQPSGSVPP APA //