Amiloride-sensitive amine oxidase [copper-containing]

<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

Miscellaneous

<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

• H₂O

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  + histamine

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  + O₂

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  = H₂O₂

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  + imidazole-4-acetaldehyde

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  + NH₄⁺

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  1 Publication

  <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
  EC:1.4.3.22
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

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  H₂O

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  +

  histamine

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  zoom

  +

  O₂

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  =

  H₂O₂

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  +

  imidazole-4-acetaldehyde

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  zoom

  +

  NH₄⁺

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  zoom

<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

• Cu cation
  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
  Note: Binds 1 copper ion per subunit.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• Ca²⁺
  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
  Note: Binds 2 calcium ions per subunit.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• L-topaquinone
  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
  Note: Contains 1 topaquinone per subunit.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.

<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

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

• calcium ion binding Source: UniProtKB <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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Human kidney diamine oxidase: heterologous expression, purification, and characterization."
    Elmore B.O., Bollinger J.A., Dooley D.M.
    J Biol Inorg Chem 7:565-579(2002) [PubMed] [Europe PMC] [Abstract]
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• copper ion binding Source: UniProtKBInferred from direct assayⁱ
  • "Human kidney diamine oxidase: heterologous expression, purification, and characterization."
    Elmore B.O., Bollinger J.A., Dooley D.M.
    J Biol Inorg Chem 7:565-579(2002) [PubMed] [Europe PMC] [Abstract]
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• diamine oxidase activity Source: UniProtKBInferred from direct assayⁱ
  • "Human kidney diamine oxidase: heterologous expression, purification, and characterization."
    Elmore B.O., Bollinger J.A., Dooley D.M.
    J Biol Inorg Chem 7:565-579(2002) [PubMed] [Europe PMC] [Abstract]
  • "A comparative study of the binding and inhibition of four copper-containing amine oxidases by azide: implications for the role of copper during the oxidative half-reaction."
    Juda G.A., Shepard E.M., Elmore B.O., Dooley D.M.
    Biochemistry 45:8788-8800(2006) [PubMed] [Europe PMC] [Abstract]
  • Ref.7

    "Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues."
    Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.
    J. Biol. Chem. 269:9921-9925(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION.
  • "Plasma diamine oxidase activities in renal dialysis patients, a human with spontaneous copper deficiency and marginally copper deficient rats."
    DiSilvestro R.A., Jones A.A., Smith D., Wildman R.
    Clin Biochem 30:559-563(1997) [PubMed] [Europe PMC] [Abstract]
• heparin binding Source: UniProtKBInferred from direct assayⁱ
  • "Human kidney diamine oxidase: heterologous expression, purification, and characterization."
    Elmore B.O., Bollinger J.A., Dooley D.M.
    J Biol Inorg Chem 7:565-579(2002) [PubMed] [Europe PMC] [Abstract]
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• histamine oxidase activity Source: UniProtKB-EC
• methylputrescine oxidase activity Source: UniProtKB-EC
• primary amine oxidase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• propane-1,3-diamine oxidase activity Source: UniProtKB-EC
• protein-containing complex binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• protein homodimerization activity Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• quinone binding Source: UniProtKBInferred from direct assayⁱ
  • "Human kidney diamine oxidase: heterologous expression, purification, and characterization."
    Elmore B.O., Bollinger J.A., Dooley D.M.
    J Biol Inorg Chem 7:565-579(2002) [PubMed] [Europe PMC] [Abstract]
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• zinc ion binding Source: UniProtKBInferred from direct assayⁱ
  • "Human kidney diamine oxidase: heterologous expression, purification, and characterization."
    Elmore B.O., Bollinger J.A., Dooley D.M.
    J Biol Inorg Chem 7:565-579(2002) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• amine metabolic process Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cellular response to azide Source: UniProtKBInferred from direct assayⁱ
  • "A comparative study of the binding and inhibition of four copper-containing amine oxidases by azide: implications for the role of copper during the oxidative half-reaction."
    Juda G.A., Shepard E.M., Elmore B.O., Dooley D.M.
    Biochemistry 45:8788-8800(2006) [PubMed] [Europe PMC] [Abstract]
• cellular response to copper ion Source: UniProtKBInferred from direct assayⁱ
  • "Plasma diamine oxidase activities in renal dialysis patients, a human with spontaneous copper deficiency and marginally copper deficient rats."
    DiSilvestro R.A., Jones A.A., Smith D., Wildman R.
    Clin Biochem 30:559-563(1997) [PubMed] [Europe PMC] [Abstract]
• cellular response to copper ion starvation Source: UniProtKBInferred from direct assayⁱ
  • "Plasma diamine oxidase activities in renal dialysis patients, a human with spontaneous copper deficiency and marginally copper deficient rats."
    DiSilvestro R.A., Jones A.A., Smith D., Wildman R.
    Clin Biochem 30:559-563(1997) [PubMed] [Europe PMC] [Abstract]
• cellular response to heparin Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
• cellular response to histamine Source: UniProtKBInferred from direct assayⁱ
  • "Human kidney diamine oxidase: heterologous expression, purification, and characterization."
    Elmore B.O., Bollinger J.A., Dooley D.M.
    J Biol Inorg Chem 7:565-579(2002) [PubMed] [Europe PMC] [Abstract]
• neutrophil degranulation Source: Reactome
• oxidation-reduction process Source: UniProtKBInferred from direct assayⁱ
  • "A comparative study of the binding and inhibition of four copper-containing amine oxidases by azide: implications for the role of copper during the oxidative half-reaction."
    Juda G.A., Shepard E.M., Elmore B.O., Dooley D.M.
    Biochemistry 45:8788-8800(2006) [PubMed] [Europe PMC] [Abstract]
  • Ref.7

    "Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues."
    Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.
    J. Biol. Chem. 269:9921-9925(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION.
• putrescine metabolic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.7

    "Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues."
    Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.
    J. Biol. Chem. 269:9921-9925(1994) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 20-39, CHARACTERIZATION.
• response to antibiotic Source: UniProtKBInferred from direct assayⁱ
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.
  • "Inhibition of diamine oxidase activity by metronidazole."
    Befani O., Shiozaki T.S., Turini P., Gerosa P., Mondovi B.
    Biochem Biophys Res Commun 212:589-594(1995) [PubMed] [Europe PMC] [Abstract]
• xenobiotic metabolic process Source: Reactome

<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

<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

Organism-specific databases

<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

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation 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%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

Keywords - PTMⁱ

Proteomic databases

PTM 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

Organism-specific 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%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.8

    "Structure and inhibition of human diamine oxidase."
    McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., Brown D.E., Dooley D.M., Guss J.M.
    Biochemistry 48:9810-9822(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 ALONE AND IN COMPLEX WITH CALCIUM; COPPER AND IHIBITORS, GLYCOSYLATION AT ASN-110; ASN-538 AND ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, CATALYTIC ACTIVITY.

Protein-protein interaction databases

Chemistry databases

Miscellaneous 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

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%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>Sequences (2+)ⁱ

<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.

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS 
        60         70         80         90        100
KKELRLQPSS TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV 
       110        120        130        140        150
IFFGDQEHPN VTEFAVGPLP GPCYMRALSP RPGYQSSWAS RPISTAEYAL 
       160        170        180        190        200
LYHTLQEATK PLHQFFLNTT GFSFQDCHDR CLAFTDVAPR GVASGQRRSW 
       210        220        230        240        250
LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG KFYGSPEELA 
       260        270        280        290        300
RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP 
       310        320        330        340        350
RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV 
       360        370        380        390        400
SVQEAVALYG GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT 
       410        420        430        440        450
FHYYDADDPV HYPRALCLFE MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL 
       460        470        480        490        500
VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH ATGYVHATFY TPEGLRHGTR 
       510        520        530        540        550
LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT NPWSPRHRVV 
       560        570        580        590        600
QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM 
       610        620        630        640        650
ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF 
       660        670        680        690        700
EQFLHNNENI ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN 
       710        720        730        740        750
FFPEDPSLAS RDTVIVWPRD NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP 

V                                                      

        10         20         30         40         50
MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS 
        60         70         80         90        100
KKELRLQPSS TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV 
       110        120        130        140        150
IFFGDQEHPN VTEFAVGPLP GPCYMRALSP RPGYQSSWAS RPISTAEYAL 
       160        170        180        190        200
LYHTLQEATK PLHQFFLNTT GFSFQDCHDR CLAFTDVAPR GVASGQRRSW 
       210        220        230        240        250
LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG KFYGSPEELA 
       260        270        280        290        300
RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP 
       310        320        330        340        350
RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV 
       360        370        380        390        400
SVQEAVALYG GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT 
       410        420        430        440        450
FHYYDADDPV HYPRALCLFE MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL 
       460        470        480        490        500
VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH ATGYVHATFY TPEGLRHGTR 
       510        520        530        540        550
LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT NPWSPRHRVV 
       560        570        580        590        600
QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM 
       610        620        630        640        650
ADQVLPPGWQ EEQAITWART EGGQPRALSQ AASPVPGRYP LAVTKYRESE 
       660        670        680        690        700
LCSSSIYHQN DPWHPPVVFE QFLHNNENIE NEDLVAWVTV GFLHIPHSED 
       710        720        730        740        750
IPNTATPGNS VGFLLRPFNF FPEDPSLASR DTVIVWPRDN GPNYVQRWIP 
       760        770
EDRDCSMPPP FSYNGTYRPV                                  

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

• 100% Identity
• 90% Identity
• 50% Identity

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases