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Protein

Aspartyl aminopeptidase 4

Gene

APE4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Miscellaneous

Present with 172 molecules/cell in log phase SD medium.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)DescriptionActionsGraphical viewLength
    Metal bindingi97Zinc 1By similarity1
    Binding sitei173SubstrateBy similarity1
    Metal bindingi273Zinc 1By similarity1
    Metal bindingi273Zinc 2By similarity1
    Binding sitei308SubstrateBy similarity1
    Metal bindingi309Zinc 2By similarity1
    Metal bindingi362Zinc 1By similarity1
    Binding sitei362SubstrateBy similarity1
    Binding sitei365SubstrateBy similarity1
    Binding sitei390SubstrateBy similarity1
    Binding sitei397SubstrateBy similarity1
    Metal bindingi456Zinc 2By similarity1

    GO - Molecular functioni

    • aminopeptidase activity Source: SGD
    • metalloaminopeptidase activity Source: GO_Central
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • peptide metabolic process Source: GO_Central
    • proteolysis Source: SGD

    Keywordsi

    Molecular functionAminopeptidase, Hydrolase, Metalloprotease, Protease
    LigandMetal-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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001734551 – 490Aspartyl aminopeptidase 4Add BLAST490

    Proteomic databases

    MaxQBiP38821
    PaxDbiP38821
    PRIDEiP38821
    TopDownProteomicsiP38821

    Interactioni

    Subunit structurei

    Tetrahedron-shaped homododecamer built from six homodimers.1 Publication

    Protein-protein interaction databases

    BioGridi36546, 62 interactors
    DIPiDIP-2097N
    IntActiP38821, 20 interactors
    STRINGi4932.YHR113W

    Structurei

    3D structure databases

    ProteinModelPortaliP38821
    SMRiP38821
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M18 family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00390000003164
    HOGENOMiHOG000253244
    InParanoidiP38821
    KOiK01267
    OMAiCFDHEEI
    OrthoDBiEOG092C3JCE

    Family and domain databases

    Gene3Di2.30.250.10, 1 hit
    InterProiView protein in InterPro
    IPR001948 Peptidase_M18
    IPR023358 Peptidase_M18_dom2
    PANTHERiPTHR28570 PTHR28570, 1 hit
    PfamiView protein in Pfam
    PF02127 Peptidase_M18, 1 hit
    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

    Similar proteinsi

    Entry informationi

    Entry nameiDNPEP_YEAST
    AccessioniPrimary (citable) accession number: P38821
    Secondary accession number(s): D3DL63
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: May 23, 2018
    This is version 137 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health