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Protein

Aspartic protease pepA

Gene

pepA

Organism
Penicillium janthinellum (Penicillium vitale)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin.1 Publication

Catalytic activityi

Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.1 Publication

Kineticsi

  1. KM=0.4 mM for Ac-Lys-p-nitrophenylalanyl-amide1 Publication
  2. KM=0.4 mM for Ac-Ala-Lys-p-nitrophenylalanyl-amide1 Publication
  3. KM=0.5 mM for Ac-Ala-Ala-Lys-p-nitrophenylalanyl-amide1 Publication
  4. KM=0.59 mM for Ac-Lys-p-nitrophenylalanyl-Ala-amide1 Publication
  5. KM=0.5 mM for Ac-Ala-Lys-p-nitrophenylalanyl-Ala-amide1 Publication
  6. KM=0.35 mM for Ac-Ala-Ala-Lys-p-nitrophenylalanyl-Ala-amide1 Publication
  7. KM=0.21 mM for Ac-Lys-p-nitrophenylalanyl-Ala-Ala-amide1 Publication
  8. KM=0.41 mM for Ac-Ala-Lys-p-nitrophenylalanyl-Ala-Ala-amide1 Publication
  9. KM=0.32 mM for Ac-Ala-Ala-Lys-p-nitrophenylalanyl-Ala-Ala-amide1 Publication
  10. KM=0.46 mM for Ac-Ala-Ala-Ala-Lys-p-nitrophenylalanyl-Ala-Ala-amide1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei103 – 1031PROSITE-ProRule annotation
    Active sitei284 – 2841PROSITE-ProRule annotation

    GO - Molecular functioni

    • aspartic-type endopeptidase activity Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BRENDAi3.4.23.20. 4621.

    Protein family/group databases

    MEROPSiA01.026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aspartic protease pepA (EC:3.4.23.18)
    Alternative name(s):
    Penicillopepsin-JT2
    Gene namesi
    Name:pepA
    OrganismiPenicillium janthinellum (Penicillium vitale)
    Taxonomic identifieri5079 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    Subcellular locationi

    GO - Cellular componenti

    • extracellular region Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence analysisAdd
    BLAST
    Propeptidei27 – 7145Activation peptideBy similarityPRO_0000407055Add
    BLAST
    Chaini72 – 394323Aspartic protease pepAPRO_5000145200Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence analysis
    Disulfide bondi319 ↔ 354By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Structurei

    3D structure databases

    ProteinModelPortaliP78735.
    SMRiP78735. Positions 74-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini87 – 391305Peptidase A1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated
    Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase_A1.
    IPR001969. Aspartic_peptidase_AS.
    IPR033121. PEPTIDASE_A1.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 2 hits.
    PfamiPF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    PS51767. PEPTIDASE_A1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P78735-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVVFSKITVV LAGLATVASA VPTGTSRKST FTVNQKARPV AQAKAINLPG
    60 70 80 90 100
    MYASALSKYG AAVPASVKAA AESGTAVTTP EANDVEYLTP VNVGGTTLNL
    110 120 130 140 150
    DFDTGSADLW VFSSELSSSE STGHSLYKPS SNATKLAGYS WSITYGDQSS
    160 170 180 190 200
    ASGDVYKDFV VVGGVKASPQ AVEAASQISQ QFVNDKNNDG LLGLAFSSIN
    210 220 230 240 250
    TVKPKSQTTF FDTVKGQLDS PLFAVTLKHN APGTYDFGFV DKNKYTGSLT
    260 270 280 290 300
    YAQVDSSQGF WSFTADGYKI GSKSGGSIQG IADTGTTLLL LPDNVVSDYY
    310 320 330 340 350
    GQVSGAQQDS SAGGYTVPCS AQLPDFTVTI GSYNAVVPGS LINYAPLQSG
    360 370 380 390
    SSTCFGGIQS NSGLGFSIFG DIFLKSQYVV FDANGPRLGF APQA
    Length:394
    Mass (Da):40,840
    Last modified:May 1, 1997 - v1
    Checksum:iFCFE8246FFAD31F4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U81483 Genomic DNA. Translation: AAB63942.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U81483 Genomic DNA. Translation: AAB63942.1.

    3D structure databases

    ProteinModelPortaliP78735.
    SMRiP78735. Positions 74-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    MEROPSiA01.026.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.4.23.20. 4621.

    Family and domain databases

    Gene3Di2.40.70.10. 2 hits.
    InterProiIPR001461. Aspartic_peptidase_A1.
    IPR001969. Aspartic_peptidase_AS.
    IPR033121. PEPTIDASE_A1.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view]
    PANTHERiPTHR13683. PTHR13683. 2 hits.
    PfamiPF00026. Asp. 1 hit.
    [Graphical view]
    PRINTSiPR00792. PEPSIN.
    SUPFAMiSSF50630. SSF50630. 1 hit.
    PROSITEiPS00141. ASP_PROTEASE. 2 hits.
    PS51767. PEPTIDASE_A1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat)."
      Cao Q.N., Stubbs M., Ngo K.Q., Ward M., Cunningham A., Pai E.F., Tu G.C., Hofmann T.
      Protein Sci. 9:991-1001(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: NRRL905.

    Entry informationi

    Entry nameiPEPA_PENJA
    AccessioniPrimary (citable) accession number: P78735
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: May 1, 1997
    Last modified: April 13, 2016
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. 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.