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Protein

Aspartyl aminopeptidase 4

Gene

APE4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Aspartyl aminopeptidase that contributes to peptide degradation both in the cytosol and the vacuole. Cells may respond to environmental conditions by changing the distributions of the cytosolic enzyme to the vacuole when cells need more active vacuolar degradation.1 Publication

Catalytic activityi

Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Enzyme regulationi

The metalloproteases inhibitors EDTA and 1.10-phenanthroline both inhibit the activity, whereas bestatin, an inhibitor of most aminopeptidases, does not affect enzyme activity.1 Publication

Kineticsi

  1. KM=64 µM for angiotensin I1 Publication

    pH dependencei

    Optimum pH is 7.5-7.9.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi97 – 971Zinc 1By similarity
    Binding sitei173 – 1731SubstrateBy similarity
    Metal bindingi273 – 2731Zinc 1By similarity
    Metal bindingi273 – 2731Zinc 2By similarity
    Binding sitei308 – 3081SubstrateBy similarity
    Metal bindingi309 – 3091Zinc 2By similarity
    Metal bindingi362 – 3621Zinc 1By similarity
    Binding sitei362 – 3621SubstrateBy similarity
    Binding sitei365 – 3651SubstrateBy similarity
    Binding sitei390 – 3901SubstrateBy similarity
    Binding sitei397 – 3971SubstrateBy similarity
    Metal bindingi456 – 4561Zinc 2By similarity

    GO - Molecular functioni

    • aminopeptidase activity Source: SGD
    • metallopeptidase activity Source: UniProtKB-KW
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • proteolysis Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31155-MONOMER.
    BRENDAi3.4.11.21. 984.

    Protein family/group databases

    MEROPSiM18.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartyl aminopeptidase 4 (EC:3.4.11.21)
    Gene namesi
    Name:APE4
    Ordered Locus Names:YHR113W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome VIII

    Organism-specific databases

    EuPathDBiFungiDB:YHR113W.
    SGDiS000001155. APE4.

    Subcellular locationi

    GO - Cellular componenti

    • fungal-type vacuole lumen Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Aspartyl aminopeptidase 4PRO_0000173455Add
    BLAST

    Proteomic databases

    MaxQBiP38821.
    PeptideAtlasiP38821.
    TopDownProteomicsiP38821.

    Interactioni

    Subunit structurei

    Tetrahedron-shaped homododecamer built from six homodimers.1 Publication

    Protein-protein interaction databases

    BioGridi36546. 23 interactions.
    DIPiDIP-2097N.
    IntActiP38821. 20 interactions.
    MINTiMINT-484319.

    Structurei

    3D structure databases

    ProteinModelPortaliP38821.
    SMRiP38821. Positions 20-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M18 family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000003164.
    HOGENOMiHOG000253244.
    InParanoidiP38821.
    KOiK01267.
    OMAiVANDSPC.
    OrthoDBiEOG75TMP1.

    Family and domain databases

    Gene3Di2.30.250.10. 1 hit.
    InterProiIPR001948. Peptidase_M18.
    IPR023358. Peptidase_M18_dom2.
    [Graphical view]
    PfamiPF02127. Peptidase_M18. 1 hit.
    [Graphical view]
    PRINTSiPR00932. AMINO1PTASE.

    Sequencei

    Sequence statusi: Complete.

    P38821-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFRIQLRTMS SKTCKSDYPK EFVSFLNSSH SPYHTVHNIK KHLVSNGFKE
    60 70 80 90 100
    LSERDSWAGH VAQKGKYFVT RNGSSIIAFA VGGKWEPGNP IAITGAHTDS
    110 120 130 140 150
    PALRIKPISK RVSEKYLQVG VETYGGAIWH SWFDKDLGVA GRVFVKDAKT
    160 170 180 190 200
    GKSIARLVDL NRPLLKIPTL AIHLDRDVNQ KFEFNRETQL LPIGGLQEDK
    210 220 230 240 250
    TEAKTEKEIN NGEFTSIKTI VQRHHAELLG LIAKELAIDT IEDIEDFELI
    260 270 280 290 300
    LYDHNASTLG GFNDEFVFSG RLDNLTSCFT SMHGLTLAAD TEIDRESGIR
    310 320 330 340 350
    LMACFDHEEI GSSSAQGADS NFLPNILERL SILKGDGSDQ TKPLFHSAIL
    360 370 380 390 400
    ETSAKSFFLS SDVAHAVHPN YANKYESQHK PLLGGGPVIK INANQRYMTN
    410 420 430 440 450
    SPGLVLVKRL AEAAKVPLQL FVVANDSPCG STIGPILASK TGIRTLDLGN
    460 470 480 490
    PVLSMHSIRE TGGSADLEFQ IKLFKEFFER YTSIESEIVV
    Length:490
    Mass (Da):54,174
    Last modified:February 1, 1995 - v1
    Checksum:i511CD6EB85C4EA53
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00059 Genomic DNA. Translation: AAB68851.1.
    BK006934 Genomic DNA. Translation: DAA06807.1.
    PIRiS48955.
    RefSeqiNP_011981.1. NM_001179243.1.

    Genome annotation databases

    EnsemblFungiiYHR113W; YHR113W; YHR113W.
    GeneIDi856513.
    KEGGisce:YHR113W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00059 Genomic DNA. Translation: AAB68851.1.
    BK006934 Genomic DNA. Translation: DAA06807.1.
    PIRiS48955.
    RefSeqiNP_011981.1. NM_001179243.1.

    3D structure databases

    ProteinModelPortaliP38821.
    SMRiP38821. Positions 20-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36546. 23 interactions.
    DIPiDIP-2097N.
    IntActiP38821. 20 interactions.
    MINTiMINT-484319.

    Protein family/group databases

    MEROPSiM18.002.

    Proteomic databases

    MaxQBiP38821.
    PeptideAtlasiP38821.
    TopDownProteomicsiP38821.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYHR113W; YHR113W; YHR113W.
    GeneIDi856513.
    KEGGisce:YHR113W.

    Organism-specific databases

    EuPathDBiFungiDB:YHR113W.
    SGDiS000001155. APE4.

    Phylogenomic databases

    GeneTreeiENSGT00390000003164.
    HOGENOMiHOG000253244.
    InParanoidiP38821.
    KOiK01267.
    OMAiVANDSPC.
    OrthoDBiEOG75TMP1.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31155-MONOMER.
    BRENDAi3.4.11.21. 984.

    Miscellaneous databases

    PROiP38821.

    Family and domain databases

    Gene3Di2.30.250.10. 1 hit.
    InterProiIPR001948. Peptidase_M18.
    IPR023358. Peptidase_M18_dom2.
    [Graphical view]
    PfamiPF02127. Peptidase_M18. 1 hit.
    [Graphical view]
    PRINTSiPR00932. AMINO1PTASE.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Identification of yeast aspartyl aminopeptidase gene by purifying and characterizing its product from yeast cells."
      Yokoyama R., Kawasaki H., Hirano H.
      FEBS J. 273:192-198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ENZYME REGULATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    8. "Aspartyl aminopeptidase is imported from the cytoplasm to the vacuole by selective autophagy in Saccharomyces cerevisiae."
      Yuga M., Gomi K., Klionsky D.J., Shintani T.
      J. Biol. Chem. 286:13704-13713(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ATG19.

    Entry informationi

    Entry nameiDNPEP_YEAST
    AccessioniPrimary (citable) accession number: P38821
    Secondary accession number(s): D3DL63
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: June 8, 2016
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 172 molecules/cell in log phase SD medium.1 Publication

    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
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.