Reviewed, UniProtKB/Swiss-Prot P13798 (ACPH_HUMAN)

Names and origin

Protein names

Recommended name:
    Acylamino-acid-releasing enzyme
      Short name=AARE
    EC=3.4.19.1
Alternative name(s):
    Acyl-peptide hydrolase
      Short name=APH
    Acylaminoacyl-peptidase
    Oxidized protein hydrolase
      Short name=OPH

Gene names

Name:	APEH
Synonyms:	D3F15S2, D3S48E, DNF15S2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Catalytic activity	Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the peptidase S9C family.
Mass spectrometry	Molecular weight is 81269.9±8.7 Da from positions 1 - 732. Determined by ESI. Ref.5
Sequence caution	The sequence AAA35769.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Uncategorized	acylaminoacyl-peptidase activity Ref.7 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 732	732	Acylamino-acid-releasing enzyme
Sites
	Active site	587	1	Charge relay system
	Active site	675	1	Charge relay system By similarity
	Active site	707	1	Charge relay system
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine
Experimental info
	Sequence conflict	101	1	T → S in BAA07476. Ref.1
	Sequence conflict	137	1	A → V in BAA07476. Ref.1
	Sequence conflict	168	1	K → R in BAA07476. Ref.1
	Sequence conflict	200	1	A → P in BAA07476. Ref.1
	Sequence conflict	403	1	A → V in AAF37321. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P13798-1 [UniParc]. Last modified November 7, 2003. Version 4. Checksum: A2C370516324D851	FASTA	732	81,225
	10 20 30 40 50 60 MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GQYRTVHTEW TQRDLERMEN 70 80 90 100 110 120 IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTGPGEEKQF 130 140 150 160 170 180 LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK 190 200 210 220 230 240 ALDVSASDDE IARLKKPDQA IKGDQFVFYE DWGENMVSKS IPVLCVLDVE SGNISVLEGV 250 260 270 280 290 300 PENVSPGQAF WAPGDAGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLIGG KCELLSDDSL 310 320 330 340 350 360 AVSSPRLSPD QCRIVYLQYP SLIPHHQCSQ LCLYDWYTKV TSVVVDVVPR QLGENFSGIY 370 380 390 400 410 420 CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQVGTVTS LTAGGSGGSW KLLTIDQDLM 430 440 450 460 470 480 VAQFSTPSLP PTLKVGFLPS AGKEQSVLWV SLEEAEPIPD IHWGIRVLQP PPEQENVQYA 490 500 510 520 530 540 GLDFEAILLQ PGSPPDKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS 550 560 570 580 590 600 TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDASH VALMGGSHGG FISCHLIGQY 610 620 630 640 650 660 PETYRACVAR NPVINIASML GSTDIPDWCV VEAGFPFSSD CLPDLSVWAE MLDKSPIRYI 670 680 690 700 710 720 PQVKTPLLLM LGQEDRRVPF KQGMEYYRAL KTRNVPVRLL LYPKSTHALS EVEVESDSFM 730 NAVLWLRTHL GS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of human acylamino acid-releasing enzyme." Mitta M., Ohnogi H., Mizutani S., Sakiyama F., Kato I., Tsunasawa S. DNA Res. 3:31-35(1996) [PubMed: 8724851] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase." Fujino T., Watanabe K., Beppu M., Kikugawa K., Yasuda H. Biochim. Biophys. Acta 1478:102-112(2000) [PubMed: 10719179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[4]	"The DNF15S2 locus at 3p21 is transcribed in normal lung and small cell lung cancer." Naylor S.L., Marshall A., Hensel C., Martinez P.F., Holley B., Sakaguchi A.Y. Genomics 4:355-361(1989) [PubMed: 2565880] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE OF 102-732.
[5]	"Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures." Scaloni A., Ingallinella P., Andolfo A., Jones W., Marino G., Manning J.M. J. Protein Chem. 18:349-360(1999) [PubMed: 10395453] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, ACETYLATION AT MET-1.
[6]	"The gene from the short arm of chromosome 3, at D3F15S2, frequently deleted in renal cell carcinoma, encodes acylpeptide hydrolase." Erlandsson R., Boldog F., Persson B., Zabarovsky E.R., Allikmets R.L., Sumegi J., Klein G., Joernvall H. Oncogene 6:1293-1295(1991) [PubMed: 1861871] [Abstract] Cited for: FUNCTION.
[7]	"Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities." Jones W.M., Scaloni A., Bossa F., Popowicz A.M., Schneewind O., Manning J.M. Proc. Natl. Acad. Sci. U.S.A. 88:2194-2198(1991) [PubMed: 2006156] [Abstract] Cited for: FUNCTION.
[8]	"Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme." Scaloni A., Jones W.M., Barra D., Pospischil M., Sassa S., Popowicz A., Manning L.R., Schneewind O., Manning J.M. J. Biol. Chem. 267:3811-3818(1992) [PubMed: 1740429] [Abstract] Cited for: ACTIVE SITES SER-587 AND HIS-707.
[9]	"Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase." Feese M., Scaloni A., Jones W.M., Mannig J.M., Remington S.J. J. Mol. Biol. 233:546-549(1993) [PubMed: 8411161] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Cross-references

Sequence databases
EMBLGenBankDDBJ	D38441 mRNA. Translation: BAA07476.1. AF141383 mRNA. Translation: AAF37321.1. BC000362 mRNA. Translation: AAH00362.1. BC001499 mRNA. Translation: AAH01499.1. BC001826 mRNA. Translation: AAH01826.1. J03068 mRNA. Translation: AAA35769.1. Frameshift.
PIR	JC4655.
RefSeq	NP_001631.3.
UniGene	Hs.517969
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P13798.
Protein family/group databases
MEROPS	S09.004.
PTM databases
PhosphoSite	P13798.
Proteomic databases
PeptideAtlas	P13798.
Genome annotation databases
Ensembl	ENSG00000164062. Homo sapiens. [Contig view]
GeneID	327.
KEGG	hsa:327.
Organism-specific databases
H-InvDB	HIX0003261.
HGNC	HGNC:586. APEH.
MIM	102645. gene.
PharmGKB	PA24878.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P13798.
HOVERGEN	P13798.
Gene expression databases
CleanEx	HS_APEH.
GermOnline	ENSG00000164062. Homo sapiens.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR002471. Pept_S9_AS. IPR001375. Peptidase_S9. [Graphical view]
Gene3D	G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
Pfam	PF00326. Peptidase_S9. 1 hit. [Graphical view]
PROSITE	PS00708. PRO_ENDOPEP_SER. 1 hit. [Graphical view]
ProDom	P13798. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

ACPH_HUMAN

Accession

Primary (citable) accession number: P13798
Secondary accession number(s): Q9BQ33, Q9P0Y2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 7, 2003
Last modified:	July 22, 2008
This is version 83 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)