Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 101 (18 Sep 2019)
Sequence version 1 (01 Nov 1999)
Previous versions | rss
Help videoAdd a publicationFeedback

Subtilisin-like serine protease Pen c 1

Penicillium citrinum
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Serine protease (PubMed:10103041, PubMed:7763554). Hydrolyzes azocasein (PubMed:10103041). Cleaves peptide bonds of the oxidized insulin B chain preferably at 15-Leu-|-Tyr-16, but also at 4-Gln-|-His-5 and 24-Phe-|-Phe-25, and to a lesser extent at 5-His-|-Leu-6 and 25-Phe-|-Tyr-26. Hydrolyzes amide bonds between amino acids and 7-amino-4-methylcoumarin (AMC) in vitro (PubMed:7763554).2 Publications

<p>This subsection of the <a href="">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by 0.1 mM diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), chymostatin and elastatinal. Not inhibited by N-alpha-p-tosyl-L-lysine chloromethylketone (TLCK), N-tosyl-L-phenylalanyl chloromethyl ketone (TPCK) or N-carbobenzoxy-L-phenylalanine chloromethylketone (ZPCK).1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.14 mM for t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-amide (Boc-VLK-MCA) (at pH 7.0)1 Publication
  2. KM=0.11 mM for t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-amide ((Boc-LSTR-MCA) (at pH 7.0)1 Publication
  3. KM=0.13 mM for succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide (Suc-LLVY-MCA) (at pH 7.0)1 Publication

    pH dependencei

    Active at pH 7 (up to 40 degrees Celsius for 30 min) and at pH 11 (up to 25 degrees Celsius).1 Publication

    Temperature dependencei

    Protease activity is retained up to 40 degrees Celsius for 30 min, but completely inactivated at 50 degrees Celsius (at pH 7). Activity is retained up to 25 degrees Celsius, and completely inactivated at 40 degrees Celsius (at pH 11).1 Publication


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei157Charge relay systemPROSITE-ProRule annotation1
    Active sitei188Charge relay systemPROSITE-ProRule annotation1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei280Important for catalytic activityBy similarity1
    Active sitei343Charge relay systemPROSITE-ProRule annotation1

    <p>The <a href="">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionHydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPS protease database


    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Subtilisin-like serine protease Pen c 1Curated (EC:3.4.21.-2 Publications)
    Alternative name(s):
    Alkaline serine protease1 Publication
    Allergen: Pen c 11 Publication
    <p>This subsection of the <a href="">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiPenicillium citrinumImported
    <p>This subsection of the <a href="">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5077 [NCBI]
    <p>This subsection of the <a href="">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti


    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the <a href="">'Pathology and Biotech'</a> section is used for proteins that cause an allergic reaction in mammals. We usually specify in which species the protein is allergenic.<p><a href='/help/allergenic_properties' target='_top'>More...</a></p>Allergenic propertiesi

    Causes an allergic reaction in human. Binds to IgE.2 Publications

    Keywords - Diseasei


    Protein family/group databases

    Allergome; a platform for allergen knowledge

    517 Pen c 1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 19Sequence analysisAdd BLAST19
    <p>This subsection of the <a href="">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000044663220 – 115Removed in mature formSequence analysis4 PublicationsAdd BLAST96
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_5004337123116 – 397Subtilisin-like serine protease Pen c 14 PublicationsAdd BLAST282


    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei113Not glycosylated1 Publication1
    Sitei249Not glycosylated1 Publication1
    Sitei284Not glycosylated1 Publication1

    Keywords - PTMi


    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

    Expression is induced in mycelia after 24 hours of growth. Maximal expression is reached at about 42 hours and expression is slightly decayed after 48 hours.1 Publication

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models


    Database of comparative protein structure models


    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini35 – 113Inhibitor I9Sequence analysisAdd BLAST79
    Domaini125 – 397Peptidase S8PROSITE-ProRule annotationAdd BLAST273

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the peptidase S8 family.SAAS annotationCurated

    Keywords - Domaini


    Family and domain databases

    Conserved Domains Database

    cd04077 Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    Gene3Di, 1 hit, 1 hit

    Integrated resource of protein families, domains and functional sites

    View protein in InterPro
    IPR034193 PCSK9_ProteinaseK-like
    IPR000209 Peptidase_S8/S53_dom
    IPR036852 Peptidase_S8/S53_dom_sf
    IPR023828 Peptidase_S8_Ser-AS
    IPR015500 Peptidase_S8_subtilisin-rel
    IPR010259 S8pro/Inhibitor_I9
    IPR037045 S8pro/Inhibitor_I9_sf

    Pfam protein domain database

    View protein in Pfam
    PF05922 Inhibitor_I9, 1 hit
    PF00082 Peptidase_S8, 1 hit

    Protein Motif fingerprint database; a protein domain database


    Superfamily database of structural and functional annotation

    SSF52743 SSF52743, 1 hit

    PROSITE; a protein domain and family database

    View protein in PROSITE
    PS51892 SUBTILASE, 1 hit
    PS00138 SUBTILASE_SER, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="">length</a> and <a href="">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <p>This subsection of the <a href="">Sequence</a> section indicates if the <a href="">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="">Sequence</a> section indicates if the <a href="">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y749-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    60 70 80 90 100
    110 120 130 140 150
    160 170 180 190 200
    210 220 230 240 250
    260 270 280 290 300
    310 320 330 340 350
    360 370 380 390
    Mass (Da):40,384
    Last modified:November 1, 1999 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2E4056A735C0EF24

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti136T → P AA sequence (PubMed:7763554).Curated1
    Sequence conflicti297C → S AA sequence (PubMed:7763554).Curated1
    Sequence conflicti305T → I AA sequence (PubMed:7763554).Curated1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database


    GenBank nucleotide sequence database


    DNA Data Bank of Japan; a nucleotide sequence database

    Links Updated
    AF084546 mRNA Translation: AAD25926.1

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    Links Updated
    AF084546 mRNA Translation: AAD25926.1

    3D structure databases


    Protein family/group databases

    Allergomei517 Pen c 1

    Family and domain databases

    CDDicd04077 Peptidases_S8_PCSK9_ProteinaseK_like, 1 hit
    Gene3Di3.30.70.80, 1 hit, 1 hit
    InterProiView protein in InterPro
    IPR034193 PCSK9_ProteinaseK-like
    IPR000209 Peptidase_S8/S53_dom
    IPR036852 Peptidase_S8/S53_dom_sf
    IPR023828 Peptidase_S8_Ser-AS
    IPR015500 Peptidase_S8_subtilisin-rel
    IPR010259 S8pro/Inhibitor_I9
    IPR037045 S8pro/Inhibitor_I9_sf
    PfamiView protein in Pfam
    PF05922 Inhibitor_I9, 1 hit
    PF00082 Peptidase_S8, 1 hit
    SUPFAMiSSF52743 SSF52743, 1 hit
    PROSITEiView protein in PROSITE
    PS51892 SUBTILASE, 1 hit
    PS00138 SUBTILASE_SER, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins


    MobiDB: a database of protein disorder and mobility annotations


    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPENC1_PENCI
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y749
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 10, 2019
    Last sequence update: November 1, 1999
    Last modified: September 18, 2019
    This is version 101 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing


    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again