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P13676

- ACPH_RAT

UniProt

P13676 - ACPH_RAT

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Protein
Acylamino-acid-releasing enzyme
Gene
Apeh
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus. It preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser.1 Publication

Catalytic activityi

Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei587 – 5871Charge relay system By similarity
Active sitei675 – 6751Charge relay system By similarity
Active sitei707 – 7071Charge relay system By similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Protein family/group databases

    MEROPSiS09.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acylamino-acid-releasing enzyme (EC:3.4.19.1)
    Short name:
    AARE
    Alternative name(s):
    Acyl-peptide hydrolase
    Short name:
    APH
    Acylaminoacyl-peptidase
    Gene namesi
    Name:Apeh
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2125. Apeh.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 732732Acylamino-acid-releasing enzyme
    PRO_0000122434Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11Blocked amino end (Met)1 Publication
    Modified residuei1 – 11N-acetylmethionine By similarity
    Modified residuei185 – 1851Phosphoserine By similarity
    Modified residuei187 – 1871Phosphoserine By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP13676.
    PRIDEiP13676.

    PTM databases

    PhosphoSiteiP13676.

    Expressioni

    Gene expression databases

    GenevestigatoriP13676.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP13676.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9C family.

    Phylogenomic databases

    eggNOGiCOG1506.
    HOGENOMiHOG000007443.
    HOVERGENiHBG000869.
    InParanoidiP13676.
    KOiK01303.
    PhylomeDBiP13676.

    Family and domain databases

    Gene3Di2.120.10.30. 2 hits.
    3.40.50.1820. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    [Graphical view]
    PfamiPF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13676-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW    50
    TQRDLERMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG 100
    TMKAVLRKAG GTVSGEEKQF LEVWEKNRKL KSFNLSALEK HGPVYEDDCF 150
    GCLSWSHSET HLLYVAEKKR PKAESFFQTK ALDISASDDE MARPKKPDQA 200
    IKGDQFVFYE DWGETMVSKS IPVLCVLDID SGNISVLEGV PENVSPGQAF 250
    WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDGSL 300
    AICSPRLSPD QCRIVYLQYP CLAPHHQCSQ LCLYDWYTKV TSVVVDIVPR 350
    QLGESFSGIY CSLLPLGCWS ADSQRVVFDS AQRSRQDLFA VDTQTGSITS 400
    LTAAGSAGSW KLLTIDKDLM VAQFSTPSLP PSLKVGFLPP PGKEQSVSWV 450
    SLEEAEPIPG IHWGVRVLHP PPDQENVQYA DLDFEAILLQ PSNPPDKTQV 500
    PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS TGFGQDSILS 550
    LPGNVGHQDV KDVQFAVEQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY 600
    PETYSACIAR NPVINIASMM GSTDIPDWCM VETGFPYSNS CLPDLNVWEE 650
    MLDKSPIKYI PQVKTPVLLM LGQEDRRVPF KQGMEYYRAL KARNVPVRLL 700
    LYPKSNHALS EVEAESDSFM NAVLWLHTHL GS 732
    Length:732
    Mass (Da):81,384
    Last modified:January 1, 1990 - v1
    Checksum:i43F234879E10235B
    GO

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti625 – 6284IPDW → M in CAA33040. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04733 mRNA. Translation: AAA88506.1.
    X14915 Genomic DNA. Translation: CAA33040.1. Sequence problems.
    PIRiA33706. S07624.
    RefSeqiNP_036632.1. NM_012500.1.
    UniGeneiRn.11057.

    Genome annotation databases

    GeneIDi24206.
    KEGGirno:24206.
    UCSCiRGD:2125. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04733 mRNA. Translation: AAA88506.1 .
    X14915 Genomic DNA. Translation: CAA33040.1 . Sequence problems.
    PIRi A33706. S07624.
    RefSeqi NP_036632.1. NM_012500.1.
    UniGenei Rn.11057.

    3D structure databases

    ProteinModelPortali P13676.
    ModBasei Search...

    Protein family/group databases

    MEROPSi S09.004.

    PTM databases

    PhosphoSitei P13676.

    Proteomic databases

    PaxDbi P13676.
    PRIDEi P13676.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24206.
    KEGGi rno:24206.
    UCSCi RGD:2125. rat.

    Organism-specific databases

    CTDi 327.
    RGDi 2125. Apeh.

    Phylogenomic databases

    eggNOGi COG1506.
    HOGENOMi HOG000007443.
    HOVERGENi HBG000869.
    InParanoidi P13676.
    KOi K01303.
    PhylomeDBi P13676.

    Miscellaneous databases

    NextBioi 602597.

    Gene expression databases

    Genevestigatori P13676.

    Family and domain databases

    Gene3Di 2.120.10.30. 2 hits.
    3.40.50.1820. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    [Graphical view ]
    Pfami PF00326. Peptidase_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of a rat liver cDNA encoding acyl-peptide hydrolase."
      Kobayashi K., Lin L.-W., Yeadon J.E., Klickstein L.B., Smith J.A.
      J. Biol. Chem. 264:8892-8899(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Structural organization of the rat acyl-peptide hydrolase gene."
      Lin L.-W., Lee F.J.S., Smith J.A.
      Nucleic Acids Res. 17:4397-4400(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Sprague-Dawley.
    3. "Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction."
      Kobayashi K., Smith J.A.
      J. Biol. Chem. 262:11435-11445(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: BLOCKAGE OF N-TERMINUS, FUNCTION.

    Entry informationi

    Entry nameiACPH_RAT
    AccessioniPrimary (citable) accession number: P13676
    Secondary accession number(s): P14320, P70479
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: June 11, 2014
    This is version 116 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, 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
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