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Protein

Penicillopepsin-2

Gene

pepA

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

Functioni

Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions, but can also activate trypsinogen and hydrolyze the B chain of insulin between positions 'Gly-20' and 'Glu-21'.1 Publication

Catalytic activityi

Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and activates trypsinogen.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)DescriptionActionsGraphical viewLength
    Active sitei103PROSITE-ProRule annotation1
    Active sitei283PROSITE-ProRule annotation1

    GO - Molecular functioni

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

    Keywordsi

    Molecular functionAspartyl protease, Hydrolase, Protease

    Enzyme and pathway databases

    BRENDAi3.4.23.20. 4621.

    Protein family/group databases

    MEROPSiA01.026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Penicillopepsin-2Curated (EC:3.4.23.201 Publication)
    Alternative name(s):
    Aspartic protease pepA
    Penicillopepsin-JT21 Publication
    Gene namesi
    Name:pepA1 Publication
    OrganismiPenicillium janthinellum (Penicillium vitale)
    Taxonomic identifieri5079 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    Subcellular locationi

    • Secreted By similarity

    GO - Cellular componenti

    • extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 20Sequence analysisAdd BLAST20
    PropeptideiPRO_000040705521 – 71Activation peptide1 PublicationAdd BLAST51
    ChainiPRO_500014520072 – 394Penicillopepsin-2Add BLAST323

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi132N-linked (GlcNAc...)PROSITE-ProRule annotation1
    Disulfide bondi319 ↔ 354PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP78735.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini87 – 391Peptidase A1PROSITE-ProRule annotationAdd BLAST305

    Sequence similaritiesi

    Belongs to the peptidase A1 family.PROSITE-ProRule annotation
    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.
    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...

    Entry informationi

    Entry nameiPEPA2_PENJA
    AccessioniPrimary (citable) accession number: P78735
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: May 1, 1997
    Last modified: January 18, 2017
    This is version 72 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    PubMed:10850809 has identified a second propeptide cleavage site after Lys-68 and both possible mature proteins were found in equal quantities in a heterologous expression system in Aspergillus awamori.Curated

    Keywords - Technical termi

    Direct protein sequencing

    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.