AOC1_PIG
ID AOC1_PIG Reviewed; 755 AA.
AC Q9TRC7; F1SSL3; Q29317;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Amiloride-sensitive amine oxidase [copper-containing] {ECO:0000305};
DE Short=DAO {ECO:0000303|PubMed:8144586};
DE Short=Diamine oxidase {ECO:0000303|PubMed:8144586};
DE EC=1.4.3.22 {ECO:0000269|PubMed:1457410, ECO:0000269|PubMed:8144586};
DE AltName: Full=Amiloride-binding protein 1 {ECO:0000303|PubMed:8144586};
DE AltName: Full=Amine oxidase copper domain-containing protein 1 {ECO:0000305};
DE AltName: Full=Histaminase {ECO:0000305};
DE Flags: Precursor;
GN Name=AOC1; Synonyms=ABP1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 30-49, AND CATALYTIC ACTIVITY.
RC TISSUE=Kidney;
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 [3]
RP PROTEIN SEQUENCE OF 457-475, CATALYTIC ACTIVITY, COFACTOR, ACTIVE SITE, AND
RP TOPAQUINONE AT TYR-464.
RC TISSUE=Kidney;
RX PubMed=1457410; DOI=10.1021/bi00163a025;
RA Janes S.M., Palcic M.M., Scaman C.H., Smith A.J., Brown D.E., Dooley D.M.,
RA Mure M., Klinman J.P.;
RT "Identification of topaquinone and its consensus sequence in copper amine
RT oxidases.";
RL Biochemistry 31:12147-12154(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 508-610.
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [5]
RP GLYCAN STRUCTURE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Kidney;
RX PubMed=10782293; DOI=10.1016/s0008-6215(99)00254-2;
RA Huang Y., Mechref Y., Novotny M.V.;
RT "N-linked oligosaccharide structures in the diamine oxidase from porcine
RT kidney.";
RL Carbohydr. Res. 323:111-125(2000).
CC -!- FUNCTION: Catalyzes the degradation of compounds such as putrescine,
CC histamine, spermine, and spermidine, substances involved in allergic
CC and immune responses, cell proliferation, tissue differentiation, tumor
CC formation, and possibly apoptosis. {ECO:0000250}.
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; Evidence={ECO:0000269|PubMed:1457410,
CC ECO:0000269|PubMed:8144586};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P19801};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000250|UniProtKB:P19801};
CC Note=Contains 1 topaquinone per subunit.
CC {ECO:0000250|UniProtKB:P19801};
CC -!- ACTIVITY REGULATION: Inhibited by amiloride in a competitive manner.
CC {ECO:0000250|UniProtKB:P19801}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P19801}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- PTM: N-glycosylated; the glycans are primarily linear, di-, or
CC tribranched fucosylated complex type. {ECO:0000269|PubMed:10782293}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; CU928555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; F14708; CAA23203.1; -; mRNA.
DR PIR; B54410; B54410.
DR RefSeq; XP_003134601.1; XM_003134553.3.
DR AlphaFoldDB; Q9TRC7; -.
DR SMR; Q9TRC7; -.
DR STRING; 9823.ENSSSCP00000017422; -.
DR BindingDB; Q9TRC7; -.
DR ChEMBL; CHEMBL3108636; -.
DR DrugBank; DB00594; Amiloride.
DR GlyConnect; 46; 17 N-Linked glycans.
DR PaxDb; Q9TRC7; -.
DR PeptideAtlas; Q9TRC7; -.
DR PRIDE; Q9TRC7; -.
DR Ensembl; ENSSSCT00025044925; ENSSSCP00025019136; ENSSSCG00025032943.
DR Ensembl; ENSSSCT00035019360; ENSSSCP00035006878; ENSSSCG00035015210.
DR Ensembl; ENSSSCT00055038288; ENSSSCP00055030417; ENSSSCG00055019473.
DR GeneID; 100517436; -.
DR KEGG; ssc:100517436; -.
DR CTD; 26; -.
DR eggNOG; KOG1186; Eukaryota.
DR InParanoid; Q9TRC7; -.
DR OMA; HRTEHKT; -.
DR OrthoDB; 1320015at2759; -.
DR TreeFam; TF314750; -.
DR BioCyc; MetaCyc:MON-14652; -.
DR BRENDA; 1.4.3.22; 6170.
DR Reactome; R-SSC-211945; Phase I - Functionalization of compounds.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR SABIO-RK; Q9TRC7; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0048038; F:quinone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0097185; P:cellular response to azide; ISS:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB.
DR GO; GO:0035874; P:cellular response to copper ion starvation; ISS:UniProtKB.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0009445; P:putrescine metabolic process; IMP:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
DR Gene3D; 2.70.98.20; -; 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; PTHR10638; 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; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Copper; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Heparin-binding; Metal-binding; Oxidoreductase; Reference proteome;
KW Secreted; Signal; TPQ.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..755
FT /note="Amiloride-sensitive amine oxidase [copper-
FT containing]"
FT /evidence="ECO:0000255"
FT /id="PRO_0000064100"
FT ACT_SITE 376
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 464
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000269|PubMed:1457410"
FT BINDING 374..384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 461..466
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 513
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 515
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 524
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 571..578
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 659
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 667
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 678
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT MOD_RES 464
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:1457410"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 182..186
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 394..420
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 740
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CONFLICT 33
FT /note="G -> P (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40..42
FT /note="DLS -> AGV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 44..45
FT /note="QE -> ED (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="P -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="Missing (in Ref. 4; CAA23203)"
FT /evidence="ECO:0000305"
FT CONFLICT 595..597
FT /note="SYR -> AVP (in Ref. 4; CAA23203)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="S -> F (in Ref. 4; CAA23203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 85475 MW; 3859049D87819255 CRC64;
MGRGTLALGW AGAALLLLQM LAAAERSPRT PGGKAGVFAD LSAQELKAVH SFLWSQKELK
LEPSGTLTMA KNSVFLIEML LPKKQHVLKF LDKGHRRPVR EARAVIFFGA QEQPNVTEFA
VGPLPTPRYM RDLPPRPGHQ VSWASRPISK AEYALLSHKL QEATQPLRQF FRRTTGSSFG
DCHEQCLTFT DVAPRGLASG QRRTWFILQR QMPGYFLHPT GLELLVDHGS TNAQDWTVEQ
VWYNGKFYRS PEELAQKYND GEVDVVILED PLAKGKDGES LPEPALFSFY QPRGDFAVTM
HGPHVVQPQG PRYSLEGNRV MYGGWSFAFR LRSSSGLQIL DVHFGGERIA YEVSVQEAVA
LYGGHTPAGM QTKYIDVGWG LGSVTHELAP DIDCPETATF LDALHHYDAD GPVLYPRALC
LFEMPTGVPL RRHFNSNFSG GFNFYAGLKG QVLVLRTTST VYNYDYIWDF IFYPNGVMEA
KMHATGYVHA TFYTPEGLRY GTRLHTHLIG NMHTHLVNYR VDLDVAGTTN SFQTLQMELE
NITNPWSPRH RLVQPTLKQT RYSRERQAAF RFGQPLPKYL LITSPKENPW GHTRSYRLQL
HSMADQVLPP GWQEERAVTW ARYPLAVTRY RESELSSSSI YNQNDPWDPP VVFEEFLRNN
ENIEDEDLVA WVTVGFLHIP HSEDIPNTAT PGNSVGFLLR PFNFFPEDPA LASRDLVVVW
PLENGSTYAQ RWIPEEDQSC LKPPPFSYNG SYRPV
