Reviewed, UniProtKB/Swiss-Prot P37111 (ACY1_PIG)

Names and origin

Protein names

Recommended name:
    Aminoacylase-1
    EC=3.5.1.14
Alternative name(s):
    N-acyl-L-amino-acid amidohydrolase
    ACY-1

Gene names

Name:

ACY1

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	407 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).
Catalytic activity	An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid.
Cofactor	Binds 2 zinc ions per subunit.
Subunit structure	Homodimer. Interacts with SPHK1 By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the peptidase M20A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aminoacylase activity Inferred from electronic annotation. Source: EC metallopeptidase activity Inferred from electronic annotation. Source: InterPro protein dimerization activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 407	406	Aminoacylase-1		PRO_0000185237
Sites
	Active site	82	1	By similarity
	Active site	147	1	Proton acceptor By similarity
	Metal binding	80	1	Zinc 1 By similarity
	Metal binding	113	1	Zinc 1 By similarity
	Metal binding	113	1	Zinc 2 By similarity
	Metal binding	148	1	Zinc 2 By similarity
	Metal binding	175	1	Zinc 1 By similarity
	Metal binding	372	1	Zinc 2 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
Experimental info
	Sequence conflict	395	1	Missing in CAA48565. Ref.2
	Sequence conflict	398	1	A → T in CAA48565. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P37111-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: FCB88982ADBFF3D4	FASTA	407	45,347
	10 20 30 40 50 60 MASKGREGEH PSVTLFRQYL RIRTVQPEPD YGAAVAFLEE RARQLGLGCQ KVEVVPGHVV 70 80 90 100 110 120 TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEGFK DADGYIYGRG AQDMKCVSIQ 130 140 150 160 170 180 YLEAVRRLKV EGHHFPRTIH MTFVPDEEVG GHQGMELFVK RPEFQALRAG FALDEGLASP 190 200 210 220 230 240 TDAFTVFYSE RSPWWLRVTS TGKPGHGSRF IEDTAAEKLH KVINSILAFR EKEKQRLQSN 250 260 270 280 290 300 QLKPGAVTSV NLTMLEGGVA YNVVPATMSA CFDFRVAPDV DLKAFEEQLQ SWCQAAGEGV 310 320 330 340 350 360 TFEFVQKWME TQVTSTDDSD PWWAAFSGVF KDMKLALELE ICPASTDARY IRAAGVPALG 370 380 390 400 FSPMNHTPVL LHDHDERLHE AVFLRGVDIY TQLLSALASV PALPSES

References

[1]	"The primary structure of porcine aminoacylase 1 deduced from cDNA sequence." Mitta M., Ohnogi H., Yamamoto A., Kato I., Sakiyama F., Tsunasawa S. J. Biochem. 112:737-742(1992) [PubMed: 1284246] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Kidney.
[2]	"Cloning and sequence analyses of cDNAs encoding aminoacylase I from porcine kidney." Jakob M., Miller Y.E., Roehm K.H. Biol. Chem. Hoppe-Seyler 373:1227-1231(1992) [PubMed: 1292507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"Porcine cosmid clone containing the ACY-1 and rpL29/HIP genes." Sawazaki T., Hamasima N. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	D13514 mRNA. Translation: BAA02731.1. X68564 mRNA. Translation: CAA48565.1. AB017196 Genomic DNA. Translation: BAA76403.1.
PIR	JN0584.
RefSeq	NP_999061.1.
UniGene	Ssc.14528
3D structure databases
SMR	P37111. Positions 7-198, 320-407.
ModBase	Search...
Protein family/group databases
MEROPS	M20.973.
Genome annotation databases
GeneID	396930.
KEGG	ssc:396930.
Organism-specific databases
CTD	396930.
Phylogenomic databases
HOVERGEN	P37111.
Enzyme and pathway databases
BRENDA	3.5.1.14. 249.
Family and domain databases
InterPro	IPR001261. ArgE/DapE_CS. IPR010159. N-acyl_aa_amidohydrolase. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF036696. ACY-1. 1 hit.
TIGRFAMs	TIGR01880. Ac-peptdase-euk. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACY1_PIG

Accession

Primary (citable) accession number: P37111

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)