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Entry version 66 (26 Feb 2020)
Sequence version 1 (01 Oct 2002)
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Protein

Physarolisin

Gene
N/A
Organism
Physarum polycephalum (Slime mold)
Status
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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9 in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)(2).1 Publication EC:3.4.21.103

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 diisopropylfluorophosphate (DFP) and diazoacetyl-D,L-norleucine methyl ester (DAN).2 Publications

<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=48.3 µM for Lys-Pro-Ile-Glu-Phe+Phe(NO2)-Arg-Leu1 Publication

    pH dependencei

    Optimum pH is 1.7 with hemoglogin as substrate.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei248Charge relay systemBy similarity1
    Active sitei252Charge relay systemBy similarity1
    Active sitei484Charge relay systemBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi529CalciumBy similarity1
    <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>Sitei529DNA binding1
    Metal bindingi530Calcium; via carbonyl oxygenBy similarity1
    Metal bindingi552Calcium; via carbonyl oxygenBy similarity1
    Metal bindingi554CalciumBy similarity1

    <p>The <a href="http://www.geneontology.org/">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

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">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
    LigandCalcium, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.4.21.103, 4800

    Protein family/group databases

    MEROPS protease database

    More...
    MEROPSi
    S53.006

    <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="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:
    Physarolisin (EC:3.4.21.103)
    Alternative name(s):
    Physaropepsin
    Cleaved into the following 2 chains:
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiPhysarum polycephalum (Slime mold)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri5791 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaAmoebozoaEvoseaEumycetozoaMyxogastriaMyxogastromycetidaePhysariidaPhysaraceaePhysarum

    <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 – 18Sequence analysisAdd BLAST18
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_000029894619 – 173Removed in mature form1 PublicationAdd BLAST155
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000298947174 – 575PhysarolisinAdd BLAST402
    ChainiPRO_0000298948174 – 389Physarolisin heavy chainAdd BLAST216
    ChainiPRO_0000298949390 – 575Physarolisin light chainAdd BLAST186

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi200N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi262N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi307N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi380N-linked (GlcNAc...) asparagineSequence analysis1
    Glycosylationi453N-linked (GlcNAc...) asparagineSequence analysis1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Autocatalytically processed.
    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein, Zymogen

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q8MZS4

    <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="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini179 – 574Peptidase S53Add BLAST396

    Keywords - Domaini

    Signal

    Phylogenomic databases

    KEGG Orthology (KO)

    More...
    KOi
    K20756

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd04056, Peptidases_S53, 1 hit
    cd11377, Pro-peptidase_S53, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.200, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000209, Peptidase_S8/S53_dom
    IPR036852, Peptidase_S8/S53_dom_sf
    IPR023828, Peptidase_S8_Ser-AS
    IPR015366, S53_propep
    IPR030400, Sedolisin_dom

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00082, Peptidase_S8, 1 hit
    PF09286, Pro-kuma_activ, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00944, Pro-kuma_activ, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52743, SSF52743, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51695, SEDOLISIN, 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="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">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="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    Q8MZS4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRLLSLLFLL GLATLSFAVR SQWAQQGRAT HEALITIRFA LTQQNLDVLE
    60 70 80 90 100
    RTLLDISDTT SKNYGKWKTA EEVTELVAPA REISERVASF LERQGATKVE
    110 120 130 140 150
    NFRDMVKVTA PVSWIEETLH TNLFFFQHKT RTSKVIIRAD GGYKIPAEIA
    160 170 180 190 200
    EHVDFVAGLF EFPSIKNART QVGAGVDGYI VPYVIFDLYG IPTTFPVHPN
    210 220 230 240 250
    SSICLVEFQD DQSYNKDDLK KFAKENEITE TVVSHTVGPY SGSSADTEST
    260 270 280 290 300
    LDVQYGGAIA LNTTVWFWTV EDWMYDFATD FLNTKNPPLV VSMSWGWPEP
    310 320 330 340 350
    EQCQVGNCTG DETSLEYVVR TNVEFQKIGA IGTTLLAASG DQGAPGDSDP
    360 370 380 390 400
    ECNSKKKPLS SIFPGASPWV LSVGATMLSN MTTEDADPSA EPPICKSWTC
    410 420 430 440 450
    STSTTELVCT IPQALITTGG GFSDYSLQPS YQNAAVAAYF KSGVPLPPQT
    460 470 480 490 500
    DFNASNRGFP DVSALGHNYL IALSGDFEQV DGTSASTPVF AAIIAHLNSY
    510 520 530 540 550
    RLNNGKPPLA FAVPLIYQAF ASDPTIFNDI TTGDNKCTED CCSKFGYEAT
    560 570
    KGWDPVTGVG TPVFSKLLAF VQTLP
    Length:575
    Mass (Da):62,709
    Last modified:October 1, 2002 - 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="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA538BDA91E473BC5
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AF502290 mRNA Translation: AAM27198.1

    Genome annotation databases

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ag:AAM27198

    <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="http://www.uniprot.org/help/uniref">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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF502290 mRNA Translation: AAM27198.1

    3D structure databases

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    Protein family/group databases

    MEROPSiS53.006

    Proteomic databases

    PRIDEiQ8MZS4

    Genome annotation databases

    KEGGiag:AAM27198

    Phylogenomic databases

    KOiK20756

    Enzyme and pathway databases

    BRENDAi3.4.21.103, 4800

    Family and domain databases

    CDDicd04056, Peptidases_S53, 1 hit
    cd11377, Pro-peptidase_S53, 1 hit
    Gene3Di3.40.50.200, 1 hit
    InterProiView protein in InterPro
    IPR000209, Peptidase_S8/S53_dom
    IPR036852, Peptidase_S8/S53_dom_sf
    IPR023828, Peptidase_S8_Ser-AS
    IPR015366, S53_propep
    IPR030400, Sedolisin_dom
    PfamiView protein in Pfam
    PF00082, Peptidase_S8, 1 hit
    PF09286, Pro-kuma_activ, 1 hit
    SMARTiView protein in SMART
    SM00944, Pro-kuma_activ, 1 hit
    SUPFAMiSSF52743, SSF52743, 1 hit
    PROSITEiView protein in PROSITE
    PS51695, SEDOLISIN, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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 nameiPHYSA_PHYPO
    <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: Q8MZS4
    <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="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: October 1, 2002
    Last modified: February 26, 2020
    This is version 66 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)

    <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
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