ID AOC1_HUMAN Reviewed; 751 AA. AC P19801; C9J690; Q16683; Q16684; Q56II4; Q6GU42; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 07-JUL-2009, sequence version 4. DT 27-MAR-2024, entry version 220. DE RecName: Full=Diamine oxidase [copper-containing] {ECO:0000305|PubMed:12072962}; DE Short=Diamine oxidase {ECO:0000303|PubMed:8144586}; DE EC=1.4.3.22 {ECO:0000269|PubMed:12072962}; DE AltName: Full=Amiloride-binding protein {ECO:0000303|PubMed:2217167, ECO:0000303|PubMed:8144586}; DE AltName: Full=Amiloride-binding protein 1 {ECO:0000312|HGNC:HGNC:80}; DE AltName: Full=Amine oxidase copper domain-containing protein 1 {ECO:0000312|HGNC:HGNC:80}; DE AltName: Full=Histaminase {ECO:0000303|PubMed:8144586}; DE AltName: Full=Kidney amine oxidase {ECO:0000303|PubMed:2217167}; DE Short=KAO {ECO:0000303|PubMed:2217167}; DE Short=KDAO {ECO:0000303|PubMed:12072962}; DE Flags: Precursor; GN Name=AOC1 {ECO:0000303|PubMed:19764817, ECO:0000312|HGNC:HGNC:80}; GN Synonyms=ABP {ECO:0000303|PubMed:2217167, ECO:0000303|PubMed:8144586}, GN ABP1 {ECO:0000312|HGNC:HGNC:80}, DAO {ECO:0000303|PubMed:8144586}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT ASP-645. RC TISSUE=Kidney; RX PubMed=2217167; DOI=10.1073/pnas.87.19.7347; RA Barbry P., Champe M., Chassande O., Munemitsu S., Champigny G., RA Lingueglia E., Maes P., Frelin C., Tartar A., Ullrich A., Lazdunski M.; RT "Human kidney amiloride-binding protein: cDNA structure and functional RT expression."; RL Proc. Natl. Acad. Sci. U.S.A. 87:7347-7351(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8182053; DOI=10.1016/s0021-9258(17)36648-6; RA Chassande O., Renard S., Barbry P., Lazdunski M.; RT "The human gene for diamine oxidase, an amiloride binding protein. RT Molecular cloning, sequencing, and characterization of the promoter."; RL J. Biol. Chem. 269:14484-14489(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS PHE-332 AND RP ASP-645. RC TISSUE=Placenta; RX PubMed=8595053; DOI=10.1007/bf02401856; RA Zhang X., Kim J., McIntire W.S.; RT "cDNA sequences of variant forms of human placenta diamine oxidase."; RL Biochem. Genet. 33:261-268(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-16; PHE-332; ILE-479; RP ASP-645 AND HIS-659. RG NIEHS SNPs program; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-645. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 20-39, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION. RC TISSUE=Placenta; RX PubMed=8144586; DOI=10.1016/s0021-9258(17)36970-3; RA Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.; RT "Diamine oxidase is the amiloride-binding protein and is inhibited by RT amiloride analogues."; RL J. Biol. Chem. 269:9921-9925(1994). RN [8] RP FUNCTION. RX PubMed=239684; DOI=10.1042/bj1450373; RA Hoelttae E., Pulkkinen P., Elfving K., Jaenne J.; RT "Oxidation of polymines by diamine oxidase from human seminal plasma."; RL Biochem. J. 145:373-378(1975). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLYCOSYLATION, AND TISSUE RP SPECIFICITY. RX PubMed=12072962; DOI=10.1007/s00775-001-0331-1; RA Elmore B.O., Bollinger J.A., Dooley D.M.; RT "Human kidney diamine oxidase: heterologous expression, purification, and RT characterization."; RL J. Biol. Inorg. Chem. 7:565-579(2002). RN [10] {ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, ECO:0007744|PDB:3HII} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-751 IN COMPLEX WITH CALCIUM; RP COPPER AND INHIBITORS, FUNCTION, GLYCOSYLATION AT ASN-110; ASN-538 AND RP ASN-745, ACTIVE SITE, CALCIUM-BINDING SITES, COPPER-BINDING SITES, RP DISULFIDE BONDS, TOPAQUINONE AT TYR-461, SUBUNIT, ACTIVITY REGULATION, AND RP CATALYTIC ACTIVITY. RX PubMed=19764817; DOI=10.1021/bi9014192; RA McGrath A.P., Hilmer K.M., Collyer C.A., Shepard E.M., Elmore B.O., RA Brown D.E., Dooley D.M., Guss J.M.; RT "Structure and inhibition of human diamine oxidase."; RL Biochemistry 48:9810-9822(2009). CC -!- FUNCTION: Catalyzes the oxidative deamination of primary amines to the CC corresponding aldehydes with the concomitant production of hydrogen CC peroxide and ammonia (PubMed:8144586, PubMed:239684, PubMed:12072962, CC PubMed:19764817). Its preferred substrates are the diamines histamine CC and 1-methylhistamine and it could therefore play a role in allergic CC and immune responses (PubMed:12072962). Has a broad specificity for CC diamines and can also act on cadaverine and putrescine, two products of CC amino acid catabolism (PubMed:12072962). It could also act on CC polyamines, like spermidine and spermine though less efficiently, and CC regulate various biological processes (PubMed:239684, PubMed:12072962). CC {ECO:0000269|PubMed:12072962, ECO:0000269|PubMed:19764817, CC ECO:0000269|PubMed:239684, ECO:0000269|PubMed:8144586}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + histamine + O2 = H2O2 + imidazole-4-acetaldehyde + CC NH4(+); Xref=Rhea:RHEA:25625, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:27398, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:58432; EC=1.4.3.22; CC Evidence={ECO:0000269|PubMed:12072962}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25626; CC Evidence={ECO:0000305|PubMed:12072962}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O2 + putrescine = 4-aminobutanal + H2O2 + NH4(+); CC Xref=Rhea:RHEA:18273, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58264, CC ChEBI:CHEBI:326268; Evidence={ECO:0000269|PubMed:12072962, CC ECO:0000269|PubMed:19764817, ECO:0000269|PubMed:8144586}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18274; CC Evidence={ECO:0000305|PubMed:8144586}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cadaverine + H2O + O2 = 5-aminopentanal + H2O2 + NH4(+); CC Xref=Rhea:RHEA:69132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:58384, CC ChEBI:CHEBI:144896; Evidence={ECO:0000269|PubMed:12072962}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69133; CC Evidence={ECO:0000305|PubMed:12072962}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000269|PubMed:12072962, ECO:0000269|PubMed:19764817}; CC Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:19764817}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000269|PubMed:12072962, ECO:0000269|PubMed:19764817}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:19764817}; CC -!- COFACTOR: CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; CC Evidence={ECO:0000269|PubMed:12072962, ECO:0000269|PubMed:19764817}; CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:19764817}; CC -!- ACTIVITY REGULATION: Inhibited by amiloride and amiloride analogs CC (PubMed:8144586). Inhibited by isoniazid, cimetidine, clonidine, CC berenil and pentamidine (PubMed:19764817). CC {ECO:0000269|PubMed:19764817, ECO:0000269|PubMed:8144586}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8 uM for putrescine (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:8144586}; CC KM=2.8 uM for histamine (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:12072962}; CC KM=3.4 uM for 1-methylhistamine (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:12072962}; CC KM=30 uM for cadaverine (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:12072962}; CC KM=1100 uM for spermidine (at pH 7.5 and 37 degrees Celsius) CC {ECO:0000269|PubMed:12072962}; CC Note=kcat is 139 min(-1) with histamine as substrate (at pH 7.5 and CC 37 degrees Celsius) (PubMed:12072962). kcat is 103 min(-1) with CC 1-methylhistamine as substrate (at pH 7.5 and 37 degrees Celsius) CC (PubMed:12072962). kcat is 475 min(-1) with putrescine as substrate CC (at pH 7.5 and 37 degrees Celsius) (PubMed:12072962). kcat is 453 CC min(-1) with cadaverine as substrate (at pH 7.5 and 37 degrees CC Celsius) (PubMed:12072962). kcat is 187 min(-1) with spermidine as CC substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:12072962). CC {ECO:0000269|PubMed:12072962}; CC pH dependence: CC Optimum pH is 7.2. {ECO:0000269|PubMed:12072962}; CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:12072962, CC ECO:0000269|PubMed:19764817}. CC -!- INTERACTION: CC P19801; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12826295, EBI-724310; CC P19801; O75593: FOXH1; NbExp=3; IntAct=EBI-12826295, EBI-1759806; CC P19801; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12826295, EBI-10261141; CC P19801; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12826295, EBI-741158; CC P19801; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-12826295, EBI-1389308; CC P19801; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-12826295, EBI-11987469; CC P19801; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-12826295, EBI-11064654; CC P19801; O43711: TLX3; NbExp=3; IntAct=EBI-12826295, EBI-3939165; CC P19801; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-12826295, EBI-742550; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space CC {ECO:0000269|PubMed:8144586}. Cell membrane CC {ECO:0000269|PubMed:8144586}; Peripheral membrane protein CC {ECO:0000305|PubMed:8144586}; Extracellular side CC {ECO:0000305|PubMed:8144586}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=DAO1 {ECO:0000303|PubMed:8595053}; CC IsoId=P19801-1; Sequence=Displayed; CC Name=2; Synonyms=DAO2 {ECO:0000303|PubMed:8595053}; CC IsoId=P19801-2; Sequence=VSP_055190; CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in placenta CC and kidney. {ECO:0000269|PubMed:12072962}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12072962, CC ECO:0000269|PubMed:19764817}. CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}. CC -!- MISCELLANEOUS: Originally identified as an amiloride-binding protein CC (ABP) that could be related to amiloride-sensitive sodium channels, but CC later shown to function as a diamine oxidase (DAO). CC {ECO:0000269|PubMed:2217167, ECO:0000269|PubMed:8144586}. CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA58358.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/abp1/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M55602; AAA58358.1; ALT_FRAME; mRNA. DR EMBL; X78212; CAA55046.1; -; Genomic_DNA. DR EMBL; U11862; AAC50270.1; -; mRNA. DR EMBL; U11863; AAB60381.1; -; mRNA. DR EMBL; AY948960; AAX81409.1; -; Genomic_DNA. DR EMBL; AC006343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006479; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014093; AAH14093.1; -; mRNA. DR CCDS; CCDS43679.1; -. [P19801-1] DR CCDS; CCDS64797.1; -. [P19801-2] DR PIR; A54053; A54053. DR RefSeq; NP_001082.2; NM_001091.3. [P19801-1] DR RefSeq; NP_001259001.1; NM_001272072.1. [P19801-2] DR RefSeq; XP_016867433.1; XM_017011944.1. DR RefSeq; XP_016867434.1; XM_017011945.1. [P19801-2] DR RefSeq; XP_016867435.1; XM_017011946.1. [P19801-2] DR RefSeq; XP_016867436.1; XM_017011947.1. [P19801-1] DR PDB; 3HI7; X-ray; 1.80 A; A/B=21-751. DR PDB; 3HIG; X-ray; 2.09 A; A/B=21-751. DR PDB; 3HII; X-ray; 2.15 A; A/B=21-751. DR PDB; 3K5T; X-ray; 2.11 A; A=21-751. DR PDB; 3MPH; X-ray; 2.05 A; A/B=21-751. DR PDBsum; 3HI7; -. DR PDBsum; 3HIG; -. DR PDBsum; 3HII; -. DR PDBsum; 3K5T; -. DR PDBsum; 3MPH; -. DR AlphaFoldDB; P19801; -. DR SMR; P19801; -. DR BioGRID; 106544; 15. DR IntAct; P19801; 10. DR STRING; 9606.ENSP00000411613; -. DR BindingDB; P19801; -. DR ChEMBL; CHEMBL2118; -. DR DrugBank; DB00594; Amiloride. DR DrugBank; DB01373; Calcium. DR DrugBank; DB09130; Copper. DR DrugBank; DB03608; Diminazene. DR DrugBank; DB05383; Pimagedine. DR DrugCentral; P19801; -. DR GlyCosmos; P19801; 5 sites, 2 glycans. DR GlyGen; P19801; 6 sites, 4 O-linked glycans (2 sites). DR iPTMnet; P19801; -. DR PhosphoSitePlus; P19801; -. DR BioMuta; AOC1; -. DR DMDM; 251757489; -. DR CPTAC; CPTAC-2204; -. DR jPOST; P19801; -. DR MassIVE; P19801; -. DR PaxDb; 9606-ENSP00000411613; -. DR PeptideAtlas; P19801; -. DR ProteomicsDB; 53688; -. [P19801-1] DR ProteomicsDB; 53689; -. [P19801-2] DR ProteomicsDB; 8732; -. DR TopDownProteomics; P19801-1; -. [P19801-1] DR Antibodypedia; 10528; 420 antibodies from 28 providers. DR DNASU; 26; -. DR Ensembl; ENST00000360937.9; ENSP00000354193.4; ENSG00000002726.21. [P19801-1] DR Ensembl; ENST00000416793.6; ENSP00000411613.2; ENSG00000002726.21. [P19801-2] DR Ensembl; ENST00000467291.5; ENSP00000418328.1; ENSG00000002726.21. [P19801-1] DR Ensembl; ENST00000493429.5; ENSP00000418614.1; ENSG00000002726.21. [P19801-1] DR GeneID; 26; -. DR KEGG; hsa:26; -. DR MANE-Select; ENST00000360937.9; ENSP00000354193.4; NM_001091.4; NP_001082.2. DR UCSC; uc003whz.3; human. [P19801-1] DR AGR; HGNC:80; -. DR CTD; 26; -. DR DisGeNET; 26; -. DR GeneCards; AOC1; -. DR HGNC; HGNC:80; AOC1. DR HPA; ENSG00000002726; Group enriched (intestine, kidney, placenta). DR MIM; 104610; gene. DR neXtProt; NX_P19801; -. DR OpenTargets; ENSG00000002726; -. DR PharmGKB; PA24416; -. DR VEuPathDB; HostDB:ENSG00000002726; -. DR eggNOG; KOG1186; Eukaryota. DR GeneTree; ENSGT00950000183207; -. DR HOGENOM; CLU_015739_1_0_1; -. DR InParanoid; P19801; -. DR OMA; PYNSQDV; -. DR OrthoDB; 5490352at2759; -. DR PhylomeDB; P19801; -. DR TreeFam; TF314750; -. DR BioCyc; MetaCyc:HS00083-MONOMER; -. DR BRENDA; 1.4.3.22; 2681. DR PathwayCommons; P19801; -. DR Reactome; R-HSA-211945; Phase I - Functionalization of compounds. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P19801; -. DR BioGRID-ORCS; 26; 8 hits in 1115 CRISPR screens. DR ChiTaRS; AOC1; human. DR EvolutionaryTrace; P19801; -. DR GenomeRNAi; 26; -. DR Pharos; P19801; Tchem. DR PRO; PR:P19801; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P19801; Protein. DR Bgee; ENSG00000002726; Expressed in ileal mucosa and 104 other cell types or tissues. DR ExpressionAtlas; P19801; baseline and differential. DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB. DR GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB. DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB. DR GO; GO:0052598; F:histamine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0052599; F:methylputrescine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB. DR GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB. DR GO; GO:0048038; F:quinone binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central. DR GO; GO:0097185; P:cellular response to azide; IDA:UniProtKB. DR GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB. DR GO; GO:0035874; P:cellular response to copper ion starvation; IDA:UniProtKB. DR GO; GO:0071504; P:cellular response to heparin; TAS:UniProtKB. DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB. DR GO; GO:0009445; P:putrescine metabolic process; IMP:UniProtKB. DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB. DR Gene3D; 3.10.450.40; -; 2. DR Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1. DR InterPro; IPR000269; Cu_amine_oxidase. DR InterPro; IPR015798; Cu_amine_oxidase_C. DR InterPro; IPR036460; Cu_amine_oxidase_C_sf. DR InterPro; IPR016182; Cu_amine_oxidase_N-reg. DR InterPro; IPR015800; Cu_amine_oxidase_N2. DR InterPro; IPR015802; Cu_amine_oxidase_N3. DR PANTHER; PTHR10638:SF3; AMILORIDE-SENSITIVE AMINE OXIDASE [COPPER-CONTAINING]; 1. DR PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1. DR Pfam; PF01179; Cu_amine_oxid; 1. DR Pfam; PF02727; Cu_amine_oxidN2; 1. DR Pfam; PF02728; Cu_amine_oxidN3; 1. DR PRINTS; PR00766; CUDAOXIDASE. DR SUPFAM; SSF49998; Amine oxidase catalytic domain; 1. DR SUPFAM; SSF54416; Amine oxidase N-terminal region; 2. DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1. DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1. DR Genevisible; P19801; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Copper; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparin-binding; KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Secreted; KW Signal; TPQ. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:8144586" FT CHAIN 20..751 FT /note="Diamine oxidase [copper-containing]" FT /id="PRO_0000035666" FT ACT_SITE 373 FT /note="Proton acceptor" FT /evidence="ECO:0000269|PubMed:19764817" FT ACT_SITE 461 FT /note="Schiff-base intermediate with substrate; via FT topaquinone" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T" FT BINDING 510 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 512 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 519 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 520 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 521 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 562 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 653 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 656 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 658 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 664 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 665 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT BINDING 675 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT MOD_RES 461 FT /note="2',4',5'-topaquinone" FT /evidence="ECO:0000269|PubMed:19764817" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT CARBOHYD 168 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 538 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT CARBOHYD 745 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII, ECO:0007744|PDB:3K5T, FT ECO:0007744|PDB:3MPH" FT DISULFID 177..181 FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII" FT DISULFID 391..417 FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII" FT DISULFID 736 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:19764817, FT ECO:0007744|PDB:3HI7, ECO:0007744|PDB:3HIG, FT ECO:0007744|PDB:3HII" FT VAR_SEQ 618 FT /note="A -> ARTEGGQPRALSQAASPVPG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8595053" FT /id="VSP_055190" FT VARIANT 16 FT /note="T -> M (in dbSNP:rs10156191)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_025078" FT VARIANT 332 FT /note="S -> F (in dbSNP:rs1049742)" FT /evidence="ECO:0000269|PubMed:8595053, ECO:0000269|Ref.4" FT /id="VAR_025079" FT VARIANT 479 FT /note="M -> I (in dbSNP:rs45558339)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_025080" FT VARIANT 645 FT /note="H -> D (in dbSNP:rs1049793)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:2217167, ECO:0000269|PubMed:8595053, FT ECO:0000269|Ref.4" FT /id="VAR_007542" FT VARIANT 659 FT /note="N -> H (in dbSNP:rs35070995)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_025081" FT CONFLICT 28 FT /note="R -> A (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 280 FT /note="P -> A (in Ref. 1; AAA58358)" FT /evidence="ECO:0000305" FT CONFLICT 290 FT /note="D -> T (in Ref. 1; AAA58358)" FT /evidence="ECO:0000305" FT CONFLICT 572 FT /note="K -> R (in Ref. 1; AAA58358)" FT /evidence="ECO:0000305" FT CONFLICT 592 FT /note="T -> S (in Ref. 1; AAA58358, 2; CAA55046, 3; FT AAC50270/AAB60381 and 6; AAH14093)" FT /evidence="ECO:0000305" FT HELIX 29..33 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 38..49 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 64..75 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 79..88 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 96..103 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 110..117 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 137..140 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 145..158 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 163..170 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 178..186 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 198..205 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 210..212 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 214..222 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 232..238 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 246..254 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 316..320 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 322..329 FT /evidence="ECO:0007829|PDB:3HI7" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 333..341 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 344..359 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 364..368 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 370..372 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 373..376 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:3HI7" FT TURN 387..389 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 395..405 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 410..422 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 427..433 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 435..445 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 448..456 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 458..469 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 475..483 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 492..496 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 497..502 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 505..508 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 510..520 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 524..540 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 547..559 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 562..565 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 569..571 FT /evidence="ECO:0007829|PDB:3MPH" FT STRAND 575..584 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 590..598 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 610..619 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 621..626 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 629..631 FT /evidence="ECO:0007829|PDB:3HI7" FT TURN 637..641 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 643..645 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 652..655 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 661..675 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 679..681 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 691..704 FT /evidence="ECO:0007829|PDB:3HI7" FT HELIX 706..709 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 714..717 FT /evidence="ECO:0007829|PDB:3HI7" FT STRAND 720..723 FT /evidence="ECO:0007829|PDB:3K5T" FT STRAND 725..727 FT /evidence="ECO:0007829|PDB:3HI7" FT CONFLICT P19801-2:632 FT /note="A -> R (in Ref. 3; AAB60381)" FT /evidence="ECO:0000305" SQ SEQUENCE 751 AA; 85378 MW; 37114CD0D446639C CRC64; MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS KKELRLQPSS TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV IFFGDQEHPN VTEFAVGPLP GPCYMRALSP RPGYQSSWAS RPISTAEYAL LYHTLQEATK PLHQFFLNTT GFSFQDCHDR CLAFTDVAPR GVASGQRRSW LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG KFYGSPEELA RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV SVQEAVALYG GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT FHYYDADDPV HYPRALCLFE MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH ATGYVHATFY TPEGLRHGTR LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT NPWSPRHRVV QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF EQFLHNNENI ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN FFPEDPSLAS RDTVIVWPRD NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP V //