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Acylamino-acid-releasing enzyme (AARE) (EC 3.4.19.1) (Acyl-peptide hydrolase) (APH) (Acylaminoacyl-peptidase) (Oxidized protein hydrolase) (OPH)

 ACPH_HUMAN              Reviewed;         732 AA.
P13798; Q9BQ33; Q9P0Y2;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 4.
05-DEC-2018, entry version 182.
RecName: Full=Acylamino-acid-releasing enzyme;
Short=AARE;
EC=3.4.19.1;
AltName: Full=Acyl-peptide hydrolase;
Short=APH;
AltName: Full=Acylaminoacyl-peptidase;
AltName: Full=Oxidized protein hydrolase;
Short=OPH;
Name=APEH; Synonyms=D3F15S2, D3S48E, DNF15S2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8724851; DOI=10.1093/dnares/3.1.31;
Mitta M., Ohnogi H., Mizutani S., Sakiyama F., Kato I., Tsunasawa S.;
"The nucleotide sequence of human acylamino acid-releasing enzyme.";
DNA Res. 3:31-35(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=10719179; DOI=10.1016/S0167-4838(00)00004-2;
Fujino T., Watanabe K., Beppu M., Kikugawa K., Yasuda H.;
"Identification of oxidized protein hydrolase of human erythrocytes as
acylpeptide hydrolase.";
Biochim. Biophys. Acta 1478:102-112(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PRELIMINARY NUCLEOTIDE SEQUENCE OF 102-732.
PubMed=2565880; DOI=10.1016/0888-7543(89)90342-X;
Naylor S.L., Marshall A., Hensel C., Martinez P.F., Holley B.,
Sakaguchi A.Y.;
"The DNF15S2 locus at 3p21 is transcribed in normal lung and small
cell lung cancer.";
Genomics 4:355-361(1989).
[5]
PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, AND ACETYLATION AT MET-1.
PubMed=10395453; DOI=10.1023/A:1021047730831;
Scaloni A., Ingallinella P., Andolfo A., Jones W., Marino G.,
Manning J.M.;
"Structural investigations on human erythrocyte acylpeptide hydrolase
by mass spectrometric procedures.";
J. Protein Chem. 18:349-360(1999).
[6]
FUNCTION.
PubMed=1861871;
Erlandsson R., Boldog F., Persson B., Zabarovsky E.R., Allikmets R.L.,
Sumegi J., Klein G., Joernvall H.;
"The gene from the short arm of chromosome 3, at D3F15S2, frequently
deleted in renal cell carcinoma, encodes acylpeptide hydrolase.";
Oncogene 6:1293-1295(1991).
[7]
FUNCTION.
PubMed=2006156; DOI=10.1073/pnas.88.6.2194;
Jones W.M., Scaloni A., Bossa F., Popowicz A.M., Schneewind O.,
Manning J.M.;
"Genetic relationship between acylpeptide hydrolase and acylase, two
hydrolytic enzymes with similar binding but different catalytic
specificities.";
Proc. Natl. Acad. Sci. U.S.A. 88:2194-2198(1991).
[8]
ACTIVE SITES SER-587 AND HIS-707.
PubMed=1740429;
Scaloni A., Jones W.M., Barra D., Pospischil M., Sassa S.,
Popowicz A., Manning L.R., Schneewind O., Manning J.M.;
"Acylpeptide hydrolase: inhibitors and some active site residues of
the human enzyme.";
J. Biol. Chem. 267:3811-3818(1992).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=8411161; DOI=10.1006/jmbi.1993.1531;
Feese M., Scaloni A., Jones W.M., Mannig J.M., Remington S.J.;
"Crystallization and preliminary X-ray studies of human erythrocyte
acylpeptide hydrolase.";
J. Mol. Biol. 233:546-549(1993).
-!- FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal
peptide bond of an N-acetylated peptide to generate an N-
acetylated amino acid and a peptide with a free N-terminus. It
preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.
{ECO:0000269|PubMed:1861871, ECO:0000269|PubMed:2006156}.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the
N-terminus of a polypeptide.; EC=3.4.19.1;
-!- SUBUNIT: Homotetramer.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-723792, EBI-723792;
P53990:IST1; NbExp=4; IntAct=EBI-723792, EBI-945994;
O00214:LGALS8; NbExp=3; IntAct=EBI-723792, EBI-740058;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MASS SPECTROMETRY: Mass=81269.9; Mass_error=8.7;
Method=Electrospray; Range=1-732;
Evidence={ECO:0000269|PubMed:10395453};
-!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA35769.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D38441; BAA07476.1; -; mRNA.
EMBL; AF141383; AAF37321.1; -; mRNA.
EMBL; BC000362; AAH00362.1; -; mRNA.
EMBL; BC001499; AAH01499.1; -; mRNA.
EMBL; BC001826; AAH01826.1; -; mRNA.
EMBL; J03068; AAA35769.1; ALT_FRAME; mRNA.
CCDS; CCDS2801.1; -.
PIR; JC4655; JC4655.
RefSeq; NP_001631.3; NM_001640.3.
RefSeq; XP_011531962.1; XM_011533660.2.
UniGene; Hs.517969; -.
ProteinModelPortal; P13798; -.
BioGrid; 106824; 41.
IntAct; P13798; 5.
STRING; 9606.ENSP00000296456; -.
ChEMBL; CHEMBL1741174; -.
GuidetoPHARMACOLOGY; 2328; -.
ESTHER; human-APEH; ACPH_Peptidase_S9.
MEROPS; S09.004; -.
iPTMnet; P13798; -.
PhosphoSitePlus; P13798; -.
BioMuta; APEH; -.
DMDM; 38258902; -.
EPD; P13798; -.
MaxQB; P13798; -.
PaxDb; P13798; -.
PeptideAtlas; P13798; -.
PRIDE; P13798; -.
ProteomicsDB; 52988; -.
DNASU; 327; -.
Ensembl; ENST00000296456; ENSP00000296456; ENSG00000164062.
GeneID; 327; -.
KEGG; hsa:327; -.
UCSC; uc003cxf.4; human.
CTD; 327; -.
DisGeNET; 327; -.
EuPathDB; HostDB:ENSG00000164062.12; -.
GeneCards; APEH; -.
HGNC; HGNC:586; APEH.
HPA; HPA029700; -.
HPA; HPA029701; -.
HPA; HPA029702; -.
HPA; HPA029703; -.
MIM; 102645; gene.
neXtProt; NX_P13798; -.
OpenTargets; ENSG00000164062; -.
PharmGKB; PA24878; -.
eggNOG; KOG2100; Eukaryota.
eggNOG; COG1506; LUCA.
GeneTree; ENSGT00390000013172; -.
HOGENOM; HOG000007443; -.
HOVERGEN; HBG000869; -.
InParanoid; P13798; -.
KO; K01303; -.
PhylomeDB; P13798; -.
TreeFam; TF312937; -.
BioCyc; MetaCyc:HS08997-MONOMER; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
ChiTaRS; APEH; human.
GeneWiki; APEH_(gene); -.
GenomeRNAi; 327; -.
PRO; PR:P13798; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000164062; Expressed in 211 organ(s), highest expression level in mucosa of transverse colon.
CleanEx; HS_APEH; -.
ExpressionAtlas; P13798; baseline and differential.
Genevisible; P13798; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008242; F:omega peptidase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0050435; P:amyloid-beta metabolic process; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0006415; P:translational termination; TAS:Reactome.
Gene3D; 2.120.10.30; -; 1.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002471; Pept_S9_AS.
InterPro; IPR001375; Peptidase_S9.
Pfam; PF00326; Peptidase_S9; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 732 Acylamino-acid-releasing enzyme.
/FTId=PRO_0000122430.
ACT_SITE 587 587 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084,
ECO:0000269|PubMed:1740429}.
ACT_SITE 675 675 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084}.
ACT_SITE 707 707 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10084,
ECO:0000269|PubMed:1740429}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:10395453}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 187 187 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 541 541 T -> M (in dbSNP:rs3816877).
/FTId=VAR_051580.
CONFLICT 101 101 T -> S (in Ref. 1; BAA07476).
{ECO:0000305}.
CONFLICT 137 137 A -> V (in Ref. 1; BAA07476).
{ECO:0000305}.
CONFLICT 168 168 K -> R (in Ref. 1; BAA07476).
{ECO:0000305}.
CONFLICT 200 200 A -> P (in Ref. 1; BAA07476).
{ECO:0000305}.
CONFLICT 403 403 A -> V (in Ref. 2; AAF37321).
{ECO:0000305}.
SEQUENCE 732 AA; 81225 MW; A2C370516324D851 CRC64;
MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GQYRTVHTEW TQRDLERMEN
IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTGPGEEKQF
LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK
ALDVSASDDE IARLKKPDQA IKGDQFVFYE DWGENMVSKS IPVLCVLDVE SGNISVLEGV
PENVSPGQAF WAPGDAGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLIGG KCELLSDDSL
AVSSPRLSPD QCRIVYLQYP SLIPHHQCSQ LCLYDWYTKV TSVVVDVVPR QLGENFSGIY
CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQVGTVTS LTAGGSGGSW KLLTIDQDLM
VAQFSTPSLP PTLKVGFLPS AGKEQSVLWV SLEEAEPIPD IHWGIRVLQP PPEQENVQYA
GLDFEAILLQ PGSPPDKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS
TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDASH VALMGGSHGG FISCHLIGQY
PETYRACVAR NPVINIASML GSTDIPDWCV VEAGFPFSSD CLPDLSVWAE MLDKSPIRYI
PQVKTPLLLM LGQEDRRVPF KQGMEYYRAL KTRNVPVRLL LYPKSTHALS EVEVESDSFM
NAVLWLRTHL GS


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