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Q6PTT0

- ACY1B_RAT

UniProt

Q6PTT0 - ACY1B_RAT

Protein

Aminoacylase-1B

Gene

Acy1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).1 Publication

    Catalytic activityi

    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.

    Cofactori

    Binds 2 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi80 – 801Zinc 1By similarity
    Active sitei82 – 821By similarity
    Metal bindingi113 – 1131Zinc 1By similarity
    Metal bindingi113 – 1131Zinc 2By similarity
    Active sitei147 – 1471Proton acceptorBy similarity
    Metal bindingi148 – 1481Zinc 2By similarity
    Metal bindingi175 – 1751Zinc 1By similarity
    Metal bindingi373 – 3731Zinc 2By similarity

    GO - Molecular functioni

    1. aminoacylase activity Source: RGD
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: InterPro

    GO - Biological processi

    1. cellular amino acid metabolic process Source: InterPro
    2. protein catabolic process Source: RGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aminoacylase-1B (EC:3.5.1.14)
    Short name:
    ACY-1B
    Alternative name(s):
    ACY IB
    N-acyl-L-amino-acid amidohydrolase
    Gene namesi
    Name:Acy1b
    Synonyms:Acy1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2030. Acy1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 408408Aminoacylase-1BPRO_0000274010Add
    BLAST

    Proteomic databases

    PRIDEiQ6PTT0.

    Expressioni

    Gene expression databases

    GenevestigatoriQ6PTT0.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PTT0.
    SMRiQ6PTT0. Positions 7-198, 321-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M20A family.Curated

    Phylogenomic databases

    HOVERGENiHBG000982.
    InParanoidiQ6PTT0.
    PhylomeDBiQ6PTT0.

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR001261. ArgE/DapE_CS.
    IPR010159. N-acyl_aa_amidohydrolase.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036696. ACY-1. 1 hit.
    SUPFAMiSSF55031. SSF55031. 1 hit.
    TIGRFAMsiTIGR01880. Ac-peptdase-euk. 1 hit.
    PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
    PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6PTT0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ    50
    KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK 100
    DSEGYIYTRG AQDMKCVSIQ YLEAVKRLKV EGHRFPRTIH MTFVPDEEVG 150
    GHQGMELFVQ RHEFHALRAG FALDEGLANP TDAFTVFYSE RSPWWVRVTS 200
    TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS 250
    VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEEQL QSWCQEAGEG 300
    VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMTLTLEP EIFPAATDSR 350
    YIRAVGIPAL GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS 400
    VPALPGES 408
    Length:408
    Mass (Da):45,823
    Last modified:July 5, 2004 - v1
    Checksum:iF335317AF2574927
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY580165 mRNA. Translation: AAS90691.1.
    UniGeneiRn.3679.

    Genome annotation databases

    UCSCiRGD:2030. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY580165 mRNA. Translation: AAS90691.1 .
    UniGenei Rn.3679.

    3D structure databases

    ProteinModelPortali Q6PTT0.
    SMRi Q6PTT0. Positions 7-198, 321-408.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q6PTT0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:2030. rat.

    Organism-specific databases

    RGDi 2030. Acy1.

    Phylogenomic databases

    HOVERGENi HBG000982.
    InParanoidi Q6PTT0.
    PhylomeDBi Q6PTT0.

    Miscellaneous databases

    PROi Q6PTT0.

    Gene expression databases

    Genevestigatori Q6PTT0.

    Family and domain databases

    Gene3Di 3.30.70.360. 1 hit.
    InterProi IPR001261. ArgE/DapE_CS.
    IPR010159. N-acyl_aa_amidohydrolase.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view ]
    Pfami PF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036696. ACY-1. 1 hit.
    SUPFAMi SSF55031. SSF55031. 1 hit.
    TIGRFAMsi TIGR01880. Ac-peptdase-euk. 1 hit.
    PROSITEi PS00758. ARGE_DAPE_CPG2_1. 1 hit.
    PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiACY1B_RAT
    AccessioniPrimary (citable) accession number: Q6PTT0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3