P13676 (ACPH_RAT) Reviewed, UniProtKB/Swiss-Prot

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
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. Ref.3
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	Phosphoprotein
Technical term	Complete proteome Reference proteome
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_0000122434
Sites
	Active site	587	1	Charge relay system By similarity
	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	Blocked amino end (Met) Ref.1
	Modified residue	185	1	Phosphoserine By similarity
	Modified residue	187	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	625 – 628	4	IPDW → M in CAA33040. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P13676 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 43F234879E10235B	FASTA	732	81,384
	10 20 30 40 50 60 MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW TQRDLERMEN 70 80 90 100 110 120 IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG TMKAVLRKAG GTVSGEEKQF 130 140 150 160 170 180 LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK 190 200 210 220 230 240 ALDISASDDE MARPKKPDQA IKGDQFVFYE DWGETMVSKS IPVLCVLDID SGNISVLEGV 250 260 270 280 290 300 PENVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDGSL 310 320 330 340 350 360 AICSPRLSPD QCRIVYLQYP CLAPHHQCSQ LCLYDWYTKV TSVVVDIVPR QLGESFSGIY 370 380 390 400 410 420 CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQTGSITS LTAAGSAGSW KLLTIDKDLM 430 440 450 460 470 480 VAQFSTPSLP PSLKVGFLPP PGKEQSVSWV SLEEAEPIPG IHWGVRVLHP PPDQENVQYA 490 500 510 520 530 540 DLDFEAILLQ PSNPPDKTQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS 550 560 570 580 590 600 TGFGQDSILS LPGNVGHQDV KDVQFAVEQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY 610 620 630 640 650 660 PETYSACIAR NPVINIASMM GSTDIPDWCM VETGFPYSNS CLPDLNVWEE MLDKSPIKYI 670 680 690 700 710 720 PQVKTPVLLM LGQEDRRVPF KQGMEYYRAL KARNVPVRLL LYPKSNHALS EVEAESDSFM 730 NAVLWLHTHL GS

References

[1]	"Cloning and sequence analysis of a rat liver cDNA encoding acyl-peptide hydrolase." Kobayashi K., Lin L.-W., Yeadon J.E., Klickstein L.B., Smith J.A. J. Biol. Chem. 264:8892-8899(1989) [PubMed: 2722805] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Structural organization of the rat acyl-peptide hydrolase gene." Lin L.-W., Lee F.J.S., Smith J.A. Nucleic Acids Res. 17:4397-4400(1989) [PubMed: 2578023] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley.
[3]	"Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction." Kobayashi K., Smith J.A. J. Biol. Chem. 262:11435-11445(1987) [PubMed: 3305492] [Abstract] Cited for: BLOCKAGE OF N-TERMINUS, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04733 mRNA. Translation: AAA88506.1. X14915 Genomic DNA. Translation: CAA33040.1. Sequence problems.
IPI	IPI00203532.
PIR	S07624. A33706.
RefSeq	NP_036632.1. NM_012500.1.
UniGene	Rn.11057.
3D structure databases
ProteinModelPortal	P13676.
ModBase	Search...
Protein-protein interaction databases
STRING	P13676.
Protein family/group databases
MEROPS	S09.004.
Proteomic databases
PRIDE	P13676.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	24206.
KEGG	rno:24206.
UCSC	NM_012500. rat.
Organism-specific databases
CTD	327.
RGD	2125. Apeh.
Phylogenomic databases
eggNOG	roNOG04047.
GeneTree	ENSGT00390000013172.
HOVERGEN	HBG000869.
InParanoid	P13676.
OrthoDB	EOG495ZR6.
Gene expression databases
ArrayExpress	P13676.
Genevestigator	P13676.
GermOnline	ENSRNOG00000029572. Rattus norvegicus.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR002471. Pept_S9_AS. IPR001375. Peptidase_S9. IPR004106. Peptidase_S9A_B_C_N. [Graphical view]
Gene3D	G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 2 hits.
KO	K01303.
Pfam	PF00326. Peptidase_S9. 1 hit. [Graphical view]
SUPFAM	SSF50993. Peptidase_S9A_N. 1 hit.
PROSITE	PS00708. PRO_ENDOPEP_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	602597.

Entry information

Entry name

ACPH_RAT

Accession

Primary (citable) accession number: P13676
Secondary accession number(s): P14320, P70479

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	November 16, 2011
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program