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P80227

- ACPH_BOVIN

UniProt

P80227 - ACPH_BOVIN

Protein

Acylamino-acid-releasing enzyme

Gene

APEH

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      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 sitei585 – 5851Charge relay systemPROSITE-ProRule annotation
    Active sitei673 – 6731Charge relay systemPROSITE-ProRule annotation
    Active sitei705 – 7051Charge 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
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 22

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nuclear membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 730730Acylamino-acid-releasing enzymePRO_0000122429Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei183 – 1831PhosphoserineBy similarity
    Modified residuei185 – 1851PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiP80227.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP80227.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9C family.Curated

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00390000013172.
    HOGENOMiHOG000007443.
    HOVERGENiHBG000869.
    InParanoidiP80227.
    KOiK01303.
    OMAiPEQENVQ.
    OrthoDBiEOG776SPB.
    TreeFamiTF312937.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [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.

    P80227-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERQVLLSEP EEAAALYRGL SRQPALSAAC LGPEVTTQYG GRYRTVHTEW    50
    TQRDLERMEN IRFCRQYLVF HDGDSVVFAG PAGNSVETRG ELLSRESPSG 100
    TMKAVLRKAG STGEEKQFLE VWEKNRKLKS FNLSALEKHG PVYEDDCFGC 150
    LSWSHSETHL LYVAEKKRPK AESFFQTKAL DISGSDDEMA RPKKPDQAIK 200
    GDQFLFYEDW GENMVSKGSP VLCVLDIESG NISVLEGVPE SVSPGQAFWA 250
    PGDTGVVFAG WWHEPFRLGI RFCTNRRSAL YYVDLTGGNC ELLSDDSLAV 300
    TSPRLSPDQC RIVYLQFPSL VPHQQCGQLC LYDWYTRVTV VVVDVVPRQL 350
    GENFSGIYCS LLPLGCWSAD SQRVVFDTAQ RSRQDLFAVD TQMGTVTPLT 400
    AGGSGGSWKL LTIDRDLMVA QFSTPNLPPC LKVGFLPPAG MEQEVVWVSL 450
    EEAEPIPDIS WSIRVLQPPP EQEHAQYVGL DFEAILIQPS NPPDKTQVPM 500
    VVMPHGGPHS SFVTSWMLLP AMLCKMGFAA LLVNYRGSTG FGQDSILSLP 550
    GNVGSQDVKD VQFAVEQVLQ EEHFDAGRVA LLGGSHGGFL SCHLIGQYPE 600
    TYGACVVRNP VINIASMMGS TDIPDWCVVE AGYLYSSDCL PDPNVWSEML 650
    NKSPIKYTPQ VKTPVLLMLG QEDRRVPFKQ GMEYYRALKA RNVPVRLLLY 700
    PKSTHSLSEV EVESDSFMNA VIWMCTHLGH 730
    Length:730
    Mass (Da):81,093
    Last modified:February 10, 2009 - v2
    Checksum:i838882B5B703DF15
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC123400 mRNA. Translation: AAI23401.1.
    PIRiS36842.
    RefSeqiNP_001076900.1. NM_001083431.1.
    UniGeneiBt.2056.

    Genome annotation databases

    EnsembliENSBTAT00000015388; ENSBTAP00000015388; ENSBTAG00000011583.
    GeneIDi514666.
    KEGGibta:514666.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC123400 mRNA. Translation: AAI23401.1 .
    PIRi S36842.
    RefSeqi NP_001076900.1. NM_001083431.1.
    UniGenei Bt.2056.

    3D structure databases

    ProteinModelPortali P80227.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S09.004.

    Proteomic databases

    PRIDEi P80227.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000015388 ; ENSBTAP00000015388 ; ENSBTAG00000011583 .
    GeneIDi 514666.
    KEGGi bta:514666.

    Organism-specific databases

    CTDi 327.

    Phylogenomic databases

    eggNOGi COG1506.
    GeneTreei ENSGT00390000013172.
    HOGENOMi HOG000007443.
    HOVERGENi HBG000869.
    InParanoidi P80227.
    KOi K01303.
    OMAi PEQENVQ.
    OrthoDBi EOG776SPB.
    TreeFami TF312937.

    Miscellaneous databases

    NextBioi 20871454.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR015943. WD40/YVTN_repeat-like_dom.
    [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. NIH - Mammalian Gene Collection (MGC) project
      Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Thalamus.
    2. "Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation."
      Sharma K.K., Ortwerth B.J.
      Eur. J. Biochem. 216:631-637(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 194-213.
      Tissue: Lens.

    Entry informationi

    Entry nameiACPH_BOVIN
    AccessioniPrimary (citable) accession number: P80227
    Secondary accession number(s): A4FUX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 87 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