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P19205

- ACPH_PIG

UniProt

P19205 - ACPH_PIG

Protein

Acylamino-acid-releasing enzyme

Gene

APEH

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    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.

    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 system1 PublicationPROSITE-ProRule annotation
    Active sitei675 – 6751Charge relay systemPROSITE-ProRule annotation
    Active sitei707 – 7071Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 732732Acylamino-acid-releasing enzymePRO_0000122432Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei187 – 1871PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP19205.
    PRIDEiP19205.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000012138.

    Structurei

    3D structure databases

    ProteinModelPortaliP19205.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9C family.Curated

    Phylogenomic databases

    eggNOGiCOG1506.
    HOGENOMiHOG000007443.
    HOVERGENiHBG000869.
    KOiK01303.

    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.

    P19205-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GRYRTVHTEW    50
    TQRDLERMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG 100
    TMKAVLRKAG GTGTAEEKQF LEVWEKNRKL KSFNLSALEK HGPVYEDDCF 150
    GCLSWSHSET HLLYVADKKR PKAESFFQTK ALDVTGSDDE MARTKKPDQA 200
    IKGDQFLFYE DWGENMVSKS TPVLCVLDIE SGNISVLEGV PESVSPGQAF 250
    WAPGDTGVVF VGWWHEPFRL GIRFCTNRRS ALYYVDLTGG KCELLSDESV 300
    AVTSPRLSPD QCRIVYLRFP SLVPHQQCGQ LCLYDWYTRV TSVVVDIVPR 350
    QLGEDFSGIY CSLLPLGCWS ADSQRVVFDS PQRSRQDLFA VDTQMGSVTS 400
    LTAGGSGGSW KLLTIDRDLM VVQFSTPSVP PSLKVGFLPP AGKEQAVSWV 450
    SLEEAEPFPD ISWSIRVLQP PPQQEHVQYA GLDFEAILLQ PSNSPEKTQV 500
    PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS TGFGQDSILS 550
    LPGNVGHQDV KDVQFAVEQV LQEEHFDAGR VALMGGSHGG FLSCHLIGQY 600
    PETYSACVVR NPVINIASMM GSTDIPDWCM VEAGFSYSSD CLPDLSVWAA 650
    MLDKSPIKYA PQVKTPLLLM LGQEDRRVPF KQGMEYYRVL KARNVPVRLL 700
    LYPKSTHALS EVEVESDSFM NAVLWLCTHL GS 732
    Length:732
    Mass (Da):81,244
    Last modified:February 1, 1996 - v2
    Checksum:i017BD40E049A604C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671D → E AA sequence (PubMed:8576092)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00524 mRNA. Translation: BAA00411.1.
    PIRiJU0132.
    RefSeqiNP_999088.1. NM_213923.1.
    UniGeneiSsc.3208.

    Genome annotation databases

    GeneIDi396961.
    KEGGissc:396961.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00524 mRNA. Translation: BAA00411.1 .
    PIRi JU0132.
    RefSeqi NP_999088.1. NM_213923.1.
    UniGenei Ssc.3208.

    3D structure databases

    ProteinModelPortali P19205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000012138.

    Chemistry

    ChEMBLi CHEMBL2021757.

    Protein family/group databases

    MEROPSi S09.004.

    Proteomic databases

    PaxDbi P19205.
    PRIDEi P19205.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396961.
    KEGGi ssc:396961.

    Organism-specific databases

    CTDi 327.

    Phylogenomic databases

    eggNOGi COG1506.
    HOGENOMi HOG000007443.
    HOVERGENi HBG000869.
    KOi K01303.

    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. "The primary structure of porcine liver acylamino acid-releasing enzyme deduced from cDNA sequences."
      Mitta M., Asada K., Uchimura Y., Kimizuka F., Kato I., Sakiyama F., Tsunasawa S.
      J. Biochem. 106:548-551(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1.
      Tissue: Liver.
    2. "Complete covalent structure of porcine liver acylamino acid-releasing enzyme and identification of its active site serine residue."
      Miyagi M., Sakiyama F., Kato I., Tsunasawa S.
      J. Biochem. 118:771-779(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE SER-587.
      Tissue: Liver.

    Entry informationi

    Entry nameiACPH_PIG
    AccessioniPrimary (citable) accession number: P19205
    Secondary accession number(s): Q9TS46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 97 of the entry and version 2 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