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Protein

Aspartyl aminopeptidase

Gene

dnpp-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Plays a role in membrane trafficking and is specifically involved in the recycling and degradation of endocytic cargo.1 Publication

Catalytic activityi

Release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate.1 Publication

Cofactori

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

Kineticsi

  1. KM=13.58 mM for H-Asp-NHMec (at pH 7.5).
  2. KM=8.854 mM for H-Glu-NHMec (at pH 7.5).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi92 – 921Zinc 1By similarity
    Binding sitei166 – 1661SubstrateBy similarity
    Metal bindingi263 – 2631Zinc 1By similarity
    Metal bindingi263 – 2631Zinc 2By similarity
    Binding sitei299 – 2991SubstrateBy similarity
    Metal bindingi300 – 3001Zinc 2By similarity
    Metal bindingi343 – 3431Zinc 1By similarity
    Binding sitei343 – 3431SubstrateBy similarity
    Binding sitei346 – 3461SubstrateBy similarity
    Binding sitei371 – 3711SubstrateBy similarity
    Binding sitei378 – 3781SubstrateBy similarity
    Metal bindingi437 – 4371Zinc 2By similarity

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • metalloaminopeptidase activity Source: GO_Central
    • zinc ion binding Source: InterPro

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM18.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartyl aminopeptidaseImported (EC:3.4.11.211 Publication)
    Gene namesi
    Name:dnpp-1Imported
    ORF Names:F01F1.9Imported
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    Proteomesi
    • UP000001940 Componenti: Chromosome III

    Organism-specific databases

    WormBaseiF01F1.9; CE01235; WBGene00017163; dnpp-1.

    Subcellular locationi

    • Cytoplasmcytosol 1 Publication

    • Note: Diffuse expression in the cytosol.1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Animals are viable. Suppresses the abnormal formation of intestinal vacuoles phenotype in mutants lacking the phospholipid-transporting ATPase tat-1 or its chaperone chat-1.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi92 – 921H → F in M3; results in loss of enzymatic activity; when associated with F-166 and F-437. 1 Publication
    Mutagenesisi166 – 1661H → F in M3; results in loss of enzymatic activity; when associated with F-92 and F-437. 1 Publication
    Mutagenesisi331 – 3311E → L in qx49; loss of enzymatic activity. 1 Publication
    Mutagenesisi437 – 4371H → F in M3; results in loss of enzymatic activity; when associated with F-92 and F-166. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Aspartyl aminopeptidaseCuratedPRO_0000173453Add
    BLAST

    Proteomic databases

    EPDiQ19087.
    PaxDbiQ19087.
    PRIDEiQ19087.

    Expressioni

    Tissue specificityi

    Expressed in various cell types and tissues including the pharynx, neurons, body wall muscle, intestine and vulva.1 Publication

    Developmental stagei

    Expressed from the embryonic stage to adulthood.1 Publication

    Interactioni

    Subunit structurei

    Tetrahedron-shaped homododecamer built from six homodimers.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-367822,EBI-367822

    GO - Molecular functioni

    • identical protein binding Source: IntAct

    Protein-protein interaction databases

    IntActiQ19087. 2 interactions.
    STRINGi6239.F01F1.9.

    Structurei

    3D structure databases

    ProteinModelPortaliQ19087.
    SMRiQ19087. Positions 12-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M18 family.Curated

    Phylogenomic databases

    eggNOGiKOG2596. Eukaryota.
    COG1362. LUCA.
    GeneTreeiENSGT00390000003164.
    HOGENOMiHOG000253244.
    InParanoidiQ19087.
    KOiK01267.
    OMAiYFFTRNY.
    OrthoDBiEOG789CB1.
    PhylomeDBiQ19087.

    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.

    Q19087-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAAALKPSAP EIRKAAQEFI NYLNKAVTPF HATQEVKDRL LQAGFTELPE
    60 70 80 90 100
    SGHWDIQPTS KYFVTKNRSA ILAFAVGGSY KPGSGFSIVV GHTDSPCLRV
    110 120 130 140 150
    KPISHQKSDK FLQVGVSTYG GGIWRTWFDR DLSVAGLVIV KNGEKLQHKL
    160 170 180 190 200
    IDVKKPVLFI PNLAIHLETD RTTFKPNTET ELRPILETFA AAGINAPQKP
    210 220 230 240 250
    ESTGFADPRN ITNNHHPQFL GLIAKEAGCQ PEDIVDLDLY LYDTNKAAIV
    260 270 280 290 300
    GMEDEFISGA RLDNQVGTYT AISGLLESLT GESFKNDPQI RIAACFDNEE
    310 320 330 340 350
    VGSDSAMGAS SSFTEFVLRR LSAGGSTTAF EEAIGKSMLI SADQAHATHP
    360 370 380 390 400
    NYSAKHEENH RPAFHGGVVV KVNVNQRYAT TSTTHAALKQ VAFEAQVPLQ
    410 420 430 440 450
    VVVVRNDSPC GSTVGPILAT KLGLQTVDVG CPQLAMHSIR EFADTSSIYQ
    460 470
    ATTLYSTFYE RLSTVLSNMQ
    Length:470
    Mass (Da):51,157
    Last modified:November 1, 1996 - v1
    Checksum:i839830EE2F60F13F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FO080705 Genomic DNA. Translation: CCD65992.1.
    PIRiT15946.
    RefSeqiNP_498265.1. NM_065864.5.
    UniGeneiCel.10640.

    Genome annotation databases

    EnsemblMetazoaiF01F1.9; F01F1.9; WBGene00017163.
    GeneIDi175822.
    KEGGicel:CELE_F01F1.9.
    UCSCiF01F1.9. c. elegans.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    FO080705 Genomic DNA. Translation: CCD65992.1.
    PIRiT15946.
    RefSeqiNP_498265.1. NM_065864.5.
    UniGeneiCel.10640.

    3D structure databases

    ProteinModelPortaliQ19087.
    SMRiQ19087. Positions 12-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ19087. 2 interactions.
    STRINGi6239.F01F1.9.

    Protein family/group databases

    MEROPSiM18.002.

    Proteomic databases

    EPDiQ19087.
    PaxDbiQ19087.
    PRIDEiQ19087.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblMetazoaiF01F1.9; F01F1.9; WBGene00017163.
    GeneIDi175822.
    KEGGicel:CELE_F01F1.9.
    UCSCiF01F1.9. c. elegans.

    Organism-specific databases

    CTDi175822.
    WormBaseiF01F1.9; CE01235; WBGene00017163; dnpp-1.

    Phylogenomic databases

    eggNOGiKOG2596. Eukaryota.
    COG1362. LUCA.
    GeneTreeiENSGT00390000003164.
    HOGENOMiHOG000253244.
    InParanoidiQ19087.
    KOiK01267.
    OMAiYFFTRNY.
    OrthoDBiEOG789CB1.
    PhylomeDBiQ19087.

    Miscellaneous databases

    PROiQ19087.

    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. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    2. "Inactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores endocytic sorting and recycling in tat-1 mutants."
      Li X., Chen B., Yoshina S., Cai T., Yang F., Mitani S., Wang X.
      Mol. Biol. Cell 24:1163-1175(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-92; HIS-166; GLU-331 AND HIS-437.

    Entry informationi

    Entry nameiDNPEP_CAEEL
    AccessioniPrimary (citable) accession number: Q19087
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 24, 2001
    Last sequence update: November 1, 1996
    Last modified: July 6, 2016
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    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.