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Q6AYS7 (ACY1A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminoacylase-1A

Short name=ACY-1A
EC=3.5.1.14
Alternative name(s):
ACY IA
N-acyl-L-amino-acid amidohydrolase
Gene names
Name:Acy1a
Synonyms:Acy1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence 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-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate.

An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Aminoacylase-1A
PRO_0000274009

Sites

Active site821 By similarity
Active site1471Proton acceptor By similarity
Metal binding801Zinc 1 By similarity
Metal binding1131Zinc 1 By similarity
Metal binding1131Zinc 2 By similarity
Metal binding1481Zinc 2 By similarity
Metal binding1751Zinc 1 By similarity
Metal binding3731Zinc 2 By similarity

Experimental info

Sequence conflict3 – 86TKGPES → SKVPEE in AAS90690. Ref.1
Sequence conflict1321G → S in AAS90690. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6AYS7 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: CC9B4505927D432A

FASTA40845,804
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY580164 mRNA. Translation: AAS90690.1.
BC078930 mRNA. Translation: AAH78930.1.
RefSeqNP_001005383.1. NM_001005383.1.
XP_006243777.1. XM_006243715.1.
XP_006243778.1. XM_006243716.1.
UniGeneRn.3679.

3D structure databases

ProteinModelPortalQ6AYS7.
SMRQ6AYS7. Positions 7-198, 321-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000015852.

Proteomic databases

PaxDbQ6AYS7.
PRIDEQ6AYS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015851; ENSRNOP00000015852; ENSRNOG00000011189.
GeneID300981.
KEGGrno:300981.

Organism-specific databases

CTD95.
RGD2030. Acy1.

Phylogenomic databases

eggNOGCOG0624.
GeneTreeENSGT00730000111049.
HOGENOMHOG000021196.
HOVERGENHBG000982.
InParanoidQ6AYS7.
KOK14677.
OMAKGMELFV.
OrthoDBEOG7N8ZVZ.
TreeFamTF313693.

Enzyme and pathway databases

BRENDA3.5.1.14. 5301.

Gene expression databases

GenevestigatorQ6AYS7.

Family and domain databases

Gene3D3.30.70.360. 1 hit.
InterProIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF036696. ACY-1. 1 hit.
SUPFAMSSF55031. SSF55031. 1 hit.
TIGRFAMsTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio647830.

Entry information

Entry nameACY1A_RAT
AccessionPrimary (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: May 14, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries