APEH_MOUSE
ID APEH_MOUSE Reviewed; 732 AA.
AC Q8R146; G3X9I2; Q8K029; Q8R0M9;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 142.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, Kidney, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R146-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R146-2; Sequence=VSP_008866;
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 EMBL; AC137678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466560; EDL21266.1; -; Genomic_DNA.
DR EMBL; BC025494; AAH25494.1; -; mRNA.
DR EMBL; BC026594; AAH26594.1; -; mRNA.
DR EMBL; BC034199; AAH34199.1; -; mRNA.
DR CCDS; CCDS52923.1; -. [Q8R146-1]
DR RefSeq; NP_666338.2; NM_146226.2. [Q8R146-1]
DR AlphaFoldDB; Q8R146; -.
DR SMR; Q8R146; -.
DR BioGRID; 231690; 16.
DR STRING; 10090.ENSMUSP00000080058; -.
DR ChEMBL; CHEMBL2189142; -.
DR ESTHER; mouse-apeh; ACPH_Peptidase_S9.
DR MEROPS; S09.004; -.
DR iPTMnet; Q8R146; -.
DR PhosphoSitePlus; Q8R146; -.
DR EPD; Q8R146; -.
DR jPOST; Q8R146; -.
DR MaxQB; Q8R146; -.
DR PaxDb; Q8R146; -.
DR PeptideAtlas; Q8R146; -.
DR PRIDE; Q8R146; -.
DR ProteomicsDB; 296059; -. [Q8R146-1]
DR ProteomicsDB; 296060; -. [Q8R146-2]
DR Antibodypedia; 30567; 248 antibodies from 29 providers.
DR DNASU; 235606; -.
DR Ensembl; ENSMUST00000193254; ENSMUSP00000141856; ENSMUSG00000032590. [Q8R146-1]
DR GeneID; 235606; -.
DR KEGG; mmu:235606; -.
DR UCSC; uc009ros.2; mouse. [Q8R146-2]
DR UCSC; uc009rot.2; mouse. [Q8R146-1]
DR CTD; 327; -.
DR MGI; MGI:88041; Apeh.
DR VEuPathDB; HostDB:ENSMUSG00000032590; -.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00390000013172; -.
DR HOGENOM; CLU_014230_1_1_1; -.
DR InParanoid; Q8R146; -.
DR OMA; FVVDTQM; -.
DR OrthoDB; 265965at2759; -.
DR PhylomeDB; Q8R146; -.
DR TreeFam; TF312937; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-72764; Eukaryotic Translation Termination.
DR BioGRID-ORCS; 235606; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Apeh; mouse.
DR PRO; PR:Q8R146; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R146; protein.
DR Bgee; ENSMUSG00000032590; Expressed in fetal liver hematopoietic progenitor cell and 245 other tissues.
DR ExpressionAtlas; Q8R146; baseline and differential.
DR Genevisible; Q8R146; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008242; F:omega peptidase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0050435; P:amyloid-beta metabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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; Alternative splicing; Cytoplasm; Hydrolase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..732
FT /note="Acylamino-acid-releasing enzyme"
FT /id="PRO_0000122431"
FT ACT_SITE 587
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
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:0000250|UniProtKB:P13798"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13798"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 508..522
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008866"
FT CONFLICT 89
FT /note="R -> P (in Ref. 3; AAH25494)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 81581 MW; 899321A91EF39AD3 CRC64;
MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW TQRDLDRMEN
IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GAVSGEEKQF
LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK
ALDVSASDEE MARPKKPDQA IKGDQFVFYE DWGETMVSKS IPVLCVLDIE SGNISVLEGV
PENVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDESL
AVCSPRLSPD QCRVVYLQYP SLAPHHQCSQ LFLYDWYTKV TSLVVDIVPR QLGESFSGIY
CSLLPLGCWS ADSQRVVFDS VQRSRQDLFA VDTQTGSVTS LTAGGSAGSW KLLTIDRDLM
VAQFSTPNLP PSLKVGFLPP AGKEQSVSWV SLEEAEPIPD IHWGIRVLHP PPDQENVQYA
DLDFEAILLQ PSNSPDKSQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS
TGFGQDSILS LPGNVGHQDV KDVQFAVQQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY
PETYSACIAR NPVINIVSMM GTTDIPDWCM VETGFPYSND YLPDLNVLEE MLDKSPIKYI
PQVKTPVLLM LGQEDRRVPF KQGLEYYHAL KARNVPVRLL LYPKSTHALS EVEVESDSFM
NTVLWLHTHL GS
