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Q6PTT0 (ACY1B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. 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-1B

Short name=ACY-1B
EC=3.5.1.14
Alternative name(s):
ACY IB
N-acyl-L-amino-acid amidohydrolase
Gene names
Name:Acy1b
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). Ref.1

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.

Sequence similarities

Belongs to the peptidase M20A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Aminoacylase-1B
PRO_0000274010

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

Sequences

Sequence LengthMass (Da)Tools
Q6PTT0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F335317AF2574927

FASTA40845,823
        10         20         30         40         50         60 
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV 

        70         80         90        100        110        120 
TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYTRG AQDMKCVSIQ 

       130        140        150        160        170        180 
YLEAVKRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RHEFHALRAG FALDEGLANP 

       190        200        210        220        230        240 
TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN 

       250        260        270        280        290        300 
PHLKEGSVTS VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEEQL QSWCQEAGEG 

       310        320        330        340        350        360 
VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMTLTLEP EIFPAATDSR YIRAVGIPAL 

       370        380        390        400 
GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS VPALPGES 

« Hide

References

[1]"The rat kidney acylase I, characterization and molecular cloning. Differences with other acylases I."
Giardina T., Perrier J., Puigserver A.
Eur. J. Biochem. 267:6249-6255(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 161-178, FUNCTION.
Strain: Wistar.
Tissue: Kidney.
[2]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY580165 mRNA. Translation: AAS90691.1.
UniGeneRn.3679.

3D structure databases

ProteinModelPortalQ6PTT0.
SMRQ6PTT0. Positions 7-198, 321-408.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ6PTT0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2030. rat.

Organism-specific databases

RGD2030. Acy1.

Phylogenomic databases

HOVERGENHBG000982.
InParanoidQ6PTT0.
PhylomeDBQ6PTT0.

Gene expression databases

GenevestigatorQ6PTT0.

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

PROQ6PTT0.

Entry information

Entry nameACY1B_RAT
AccessionPrimary (citable) accession number: Q6PTT0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 62 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