Reviewed, UniProtKB/Swiss-Prot P19205 (ACPH_PIG)

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

Gene names

Name:

APEH

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 732	732	Acylamino-acid-releasing enzyme		PRO_0000122432
Sites
	Active site	587	1	Charge relay system Ref.2
	Active site	675	1	Charge relay system By similarity
	Active site	707	1	Charge relay system By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.2 Ref.1
	Modified residue	187	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	167	1	D → E AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P19205-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 017BD40E049A604C	FASTA	732	81,244
	10 20 30 40 50 60 MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GRYRTVHTEW TQRDLERMEN 70 80 90 100 110 120 IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTGTAEEKQF 130 140 150 160 170 180 LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVADKKR PKAESFFQTK 190 200 210 220 230 240 ALDVTGSDDE MARTKKPDQA IKGDQFLFYE DWGENMVSKS TPVLCVLDIE SGNISVLEGV 250 260 270 280 290 300 PESVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLTGG KCELLSDESV 310 320 330 340 350 360 AVTSPRLSPD QCRIVYLRFP SLVPHQQCGQ LCLYDWYTRV TSVVVDIVPR QLGEDFSGIY 370 380 390 400 410 420 CSLLPLGCWS ADSQRVVFDS PQRSRQDLFA VDTQMGSVTS LTAGGSGGSW KLLTIDRDLM 430 440 450 460 470 480 VVQFSTPSVP PSLKVGFLPP AGKEQAVSWV SLEEAEPFPD ISWSIRVLQP PPQQEHVQYA 490 500 510 520 530 540 GLDFEAILLQ PSNSPEKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS 550 560 570 580 590 600 TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDAGR VALMGGSHGG FLSCHLIGQY 610 620 630 640 650 660 PETYSACVVR NPVINIASMM GSTDIPDWCM VEAGFSYSSD CLPDLSVWAA MLDKSPIKYA 670 680 690 700 710 720 PQVKTPLLLM LGQEDRRVPF KQGMEYYRVL KARNVPVRLL LYPKSTHALS EVEVESDSFM 730 NAVLWLCTHL GS

References

[1]	"The primary structure of porcine liver acylamino acid-releasing enzyme deduced from cDNA sequences." Mitta M., Asada K., Uchimura Y., Kimizuka F., Kato I., Sakiyama F., Tsunasawa S. J. Biochem. 106:548-551(1989) [PubMed: 2691504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1. Tissue: Liver.
[2]	"Complete covalent structure of porcine liver acylamino acid-releasing enzyme and identification of its active site serine residue." Miyagi M., Sakiyama F., Kato I., Tsunasawa S. J. Biochem. 118:771-779(1995) [PubMed: 8576092] [Abstract] Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1, MASS SPECTROMETRY, ACTIVE SITE SER-587. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D00524 mRNA. Translation: BAA00411.1.
PIR	JU0132.
RefSeq	NP_999088.1.
UniGene	Ssc.3208
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	S09.004.
Genome annotation databases
GeneID	396961.
KEGG	ssc:396961.
Organism-specific databases
CTD	396961.
Phylogenomic databases
HOVERGEN	P19205.
Enzyme and pathway databases
BRENDA	3.4.19.1. 249.
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]
ProtoNet	Search...

Entry information

Entry name

ACPH_PIG

Accession

Primary (citable) accession number: P19205
Secondary accession number(s): Q9TS46

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	February 1, 1996
Last modified:	September 1, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)