Reviewed, UniProtKB/Swiss-Prot Q6AYS7 (ACY1A_RAT)

Names and origin

Protein names

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

Gene names

Name:	Acy1a
Synonyms:	Acy1

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	408 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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) By similarity.
Catalytic activity	An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the peptidase M20A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
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 soluble fraction Inferred from direct assay. Source: RGD
Molecular function	aminoacylase activity Inferred from direct assay. Source: RGD 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
	Chain	1 – 408	408	Aminoacylase-1A		PRO_0000274009
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	373	1	Zinc 2 By similarity
Experimental info
	Sequence conflict	3 – 8	6	TKGPES → SKVPEE in AAS90690. Ref.1
	Sequence conflict	132	1	G → S in AAS90690. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6AYS7-1 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: CC9B4505927D432A	FASTA	408	45,804
	10 20 30 40 50 60 MTTKGPESEH PSVTLFRQYL RICTVQPNPD YGSAVTFLEE RARQLGLSCQ KIEVAPGYVI 70 80 90 100 110 120 TVLTWPGTNP LLHSILLNSH TDVVPVFKEH WHHDPFEAFK DSEGYIYARG AQDMKSVSIQ 130 140 150 160 170 180 YLEAVRRLKS EGHRFPRTIH MTFVPDEEVG GHKGMELFVK RPEFQALRAG FALDEGLANP 190 200 210 220 230 240 TDAFTVFYSE RSPWWIRVTS TGKPGHASRF IEDTAAEKLH KVVNSILAFR EKERQRLQAN 250 260 270 280 290 300 PHLKEGAVTS VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEKQL QSWCQEAGEG 310 320 330 340 350 360 VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMNLTLEP EIFPAATDSR YIRAVGIPAL 370 380 390 400 GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS VPALPGES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The rat kidney acylase 1. Evidence for a new cDNA form and comparisons with the porcine intestinal enzyme." Perrier J., Durand A., Giardina T., Puigserver A. Comp. Biochem. Physiol. 138B:277-283(2004) [PubMed: 15253876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar.
[2]	"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: Kidney.
[3]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 89-100; 116-126; 169-190 AND 368-378, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY580164 mRNA. Translation: AAS90690.1. BC078930 mRNA. Translation: AAH78930.1.
IPI	IPI00464791.
RefSeq	NP_001005383.1.
UniGene	Rn.3679
3D structure databases
SMR	Q6AYS7. Positions 7-198, 321-408.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6AYS7.
Genome annotation databases
Ensembl	ENSRNOT00000015851; ENSRNOP00000015852; ENSRNOG00000011189; Rattus norvegicus. [Genome view]
GeneID	300981.
KEGG	rno:300981.
UCSC	NM_001005383. rat.
Organism-specific databases
CTD	300981.
RGD	2030. Acy1.
Phylogenomic databases
HOVERGEN	Q6AYS7.
OMA	KSVSIQY.
Enzyme and pathway databases
BRENDA	3.5.1.14. 248.
Gene expression databases
ArrayExpress	Q6AYS7.
Genevestigator	Q6AYS7.
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...
Other Resources
NextBio	647830.

Entry information

Entry name

ACY1A_RAT

Accession

Primary (citable) accession number: Q6AYS7
Secondary accession number(s): Q6PTT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	September 13, 2004
Last modified:	November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)