Cationic trypsin

<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_section">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

• Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. EC:3.4.21.4

<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

Sites

<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

• endopeptidase activity Source: CAFA <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Chemical synthesis and kinetic study of the smallest naturally occurring trypsin inhibitor SFTI-1 isolated from sunflower seeds and its analogues."
    Zablotna E., Kazmierczak K., Jaskiewicz A., Stawikowski M., Kupryszewski G., Rolka K.
    Biochem. Biophys. Res. Commun. 292:855-859(2002) [PubMed] [Europe PMC] [Abstract]
  • "Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)."
    Vincent J.P., Lazdunski M.
    FEBS Lett. 63:240-244(1976) [PubMed] [Europe PMC] [Abstract]
• metal ion binding Source: UniProtKB-KW
• protein heterodimerization activity Source: CAFAInferred from direct assayⁱ
  • "X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex."
    Kawamura K., Yamada T., Kurihara K., Tamada T., Kuroki R., Tanaka I., Takahashi H., Niimura N.
    Acta Crystallogr. D Biol. Crystallogr. 67:140-148(2011) [PubMed] [Europe PMC] [Abstract]
• serine-type endopeptidase activity Source: CAFAInferred from direct assayⁱ
  • "Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor MCoTI-II."
    Avrutina O., Schmoldt H.U., Gabrijelcic-Geiger D., Le Nguyen D., Sommerhoff C.P., Diederichsen U., Kolmar H.
    Biol. Chem. 386:1301-1306(2005) [PubMed] [Europe PMC] [Abstract]
• serpin family protein binding Source: CAFAInferred from direct assayⁱ
  • "Chemical synthesis and kinetic study of the smallest naturally occurring trypsin inhibitor SFTI-1 isolated from sunflower seeds and its analogues."
    Zablotna E., Kazmierczak K., Jaskiewicz A., Stawikowski M., Kupryszewski G., Rolka K.
    Biochem. Biophys. Res. Commun. 292:855-859(2002) [PubMed] [Europe PMC] [Abstract]
  • "Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)."
    Vincent J.P., Lazdunski M.
    FEBS Lett. 63:240-244(1976) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• digestion Source: UniProtKB-KW
• proteolysis Source: CAFAInferred from direct assayⁱ
  • "Chemical synthesis and kinetic study of the smallest naturally occurring trypsin inhibitor SFTI-1 isolated from sunflower seeds and its analogues."
    Zablotna E., Kazmierczak K., Jaskiewicz A., Stawikowski M., Kupryszewski G., Rolka K.
    Biochem. Biophys. Res. Commun. 292:855-859(2002) [PubMed] [Europe PMC] [Abstract]
  • "Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)."
    Vincent J.P., Lazdunski M.
    FEBS Lett. 63:240-244(1976) [PubMed] [Europe PMC] [Abstract]

<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

Enzyme and pathway databases

Protein family/group databases

<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 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

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

Chemistry databases

<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

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Keywords - PTMⁱ

Proteomic databases

Miscellaneous databases

<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• protein heterodimerization activity Source: CAFAInferred from direct assayⁱ
  • "X-ray and neutron protein crystallographic analysis of the trypsin-BPTI complex."
    Kawamura K., Yamada T., Kurihara K., Tamada T., Kuroki R., Tanaka I., Takahashi H., Niimura N.
    Acta Crystallogr. D Biol. Crystallogr. 67:140-148(2011) [PubMed] [Europe PMC] [Abstract]
• serpin family protein binding Source: CAFAInferred from direct assayⁱ
  • "Chemical synthesis and kinetic study of the smallest naturally occurring trypsin inhibitor SFTI-1 isolated from sunflower seeds and its analogues."
    Zablotna E., Kazmierczak K., Jaskiewicz A., Stawikowski M., Kupryszewski G., Rolka K.
    Biochem. Biophys. Res. Commun. 292:855-859(2002) [PubMed] [Europe PMC] [Abstract]
  • "Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)."
    Vincent J.P., Lazdunski M.
    FEBS Lett. 63:240-244(1976) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

<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

Secondary structure

3D structure databases

Miscellaneous databases

<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

Region

<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

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

        10         20         30         40         50
MKTFIFLALL GAAVAFPVDD DDKIVGGYTC GANTVPYQVS LNSGYHFCGG 
        60         70         80         90        100
SLINSQWVVS AAHCYKSGIQ VRLGEDNINV VEGNEQFISA SKSIVHPSYN 
       110        120        130        140        150
SNTLNNDIML IKLKSAASLN SRVASISLPT SCASAGTQCL ISGWGNTKSS 
       160        170        180        190        200
GTSYPDVLKC LKAPILSDSS CKSAYPGQIT SNMFCAGYLE GGKDSCQGDS 
       210        220        230        240 
GGPVVCSGKL QGIVSWGSGC AQKNKPGVYT KVCNYVSWIK QTIASN     

Sequence databases

Genome annotation databases

<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

• 90% Identity
• 50% Identity