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Amiloride-sensitive amine oxidase [copper-containing] (DAO) (Diamine oxidase) (EC 1.4.3.22) (Amiloride-binding protein 1) (Amine oxidase copper domain-containing protein 1) (Histaminase)

 AOC1_PIG                Reviewed;         755 AA.
Q9TRC7; F1SSL3; Q29317;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
04-FEB-2015, sequence version 3.
22-NOV-2017, entry version 96.
RecName: Full=Amiloride-sensitive amine oxidase [copper-containing] {ECO:0000305};
Short=DAO {ECO:0000303|PubMed:8144586};
Short=Diamine oxidase {ECO:0000303|PubMed:8144586};
EC=1.4.3.22 {ECO:0000269|PubMed:1457410, ECO:0000269|PubMed:8144586};
AltName: Full=Amiloride-binding protein 1 {ECO:0000303|PubMed:8144586};
AltName: Full=Amine oxidase copper domain-containing protein 1 {ECO:0000305};
AltName: Full=Histaminase {ECO:0000305};
Flags: Precursor;
Name=AOC1; Synonyms=ABP1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Porcine genome sequencing project;
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 30-49, AND CATALYTIC ACTIVITY.
TISSUE=Kidney;
PubMed=8144586;
Novotny W.F., Chassande O., Baker M., Lazdunski M., Barbry P.;
"Diamine oxidase is the amiloride-binding protein and is inhibited by
amiloride analogues.";
J. Biol. Chem. 269:9921-9925(1994).
[3]
PROTEIN SEQUENCE OF 457-475, CATALYTIC ACTIVITY, COFACTOR, ACTIVE
SITE, AND TOPAQUINONE AT TYR-464.
TISSUE=Kidney;
PubMed=1457410; DOI=10.1021/bi00163a025;
Janes S.M., Palcic M.M., Scaman C.H., Smith A.J., Brown D.E.,
Dooley D.M., Mure M., Klinman J.P.;
"Identification of topaquinone and its consensus sequence in copper
amine oxidases.";
Biochemistry 31:12147-12154(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 508-610.
TISSUE=Small intestine;
PubMed=8672129; DOI=10.1007/s003359900153;
Winteroe A.K., Fredholm M., Davies W.;
"Evaluation and characterization of a porcine small intestine cDNA
library: analysis of 839 clones.";
Mamm. Genome 7:509-517(1996).
[5]
GLYCAN STRUCTURE, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Kidney;
PubMed=10782293; DOI=10.1016/S0008-6215(99)00254-2;
Huang Y., Mechref Y., Novotny M.V.;
"N-linked oligosaccharide structures in the diamine oxidase from
porcine kidney.";
Carbohydr. Res. 323:111-125(2000).
-!- FUNCTION: Catalyzes the degradation of compounds such as
putrescine, histamine, spermine, and spermidine, substances
involved in allergic and immune responses, cell proliferation,
tissue differentiation, tumor formation, and possibly apoptosis.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Histamine + H(2)O + O(2) = (imidazol-4-
yl)acetaldehyde + NH(3) + H(2)O(2). {ECO:0000269|PubMed:1457410,
ECO:0000269|PubMed:8144586}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Evidence={ECO:0000250|UniProtKB:P19801};
Note=Binds 1 copper ion per subunit.
{ECO:0000250|UniProtKB:P19801};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P19801};
Note=Binds 2 calcium ions per subunit.
{ECO:0000250|UniProtKB:P19801};
-!- COFACTOR:
Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
Evidence={ECO:0000250|UniProtKB:P19801};
Note=Contains 1 topaquinone per subunit.
{ECO:0000250|UniProtKB:P19801};
-!- ENZYME REGULATION: Inhibited by amiloride in a competitive manner.
{ECO:0000250|UniProtKB:P19801}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000250|UniProtKB:P19801}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
-!- PTM: N-glycosylated; the glycans are primarily linear, di-, or
tribranched fucosylated complex type.
{ECO:0000269|PubMed:10782293}.
-!- PTM: Topaquinone (TPQ) is generated by copper-dependent
autoxidation of a specific tyrosyl residue.
{ECO:0000250|UniProtKB:P12807}.
-!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CU928555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; F14708; CAA23203.1; -; mRNA.
PIR; B54410; B54410.
RefSeq; XP_003134601.1; XM_003134553.3.
UniGene; Ssc.21957; -.
SMR; Q9TRC7; -.
STRING; 9823.ENSSSCP00000017422; -.
BindingDB; Q9TRC7; -.
ChEMBL; CHEMBL3108636; -.
DrugBank; DB00594; Amiloride.
UniCarbKB; Q9TRC7; -.
PaxDb; Q9TRC7; -.
PeptideAtlas; Q9TRC7; -.
Ensembl; ENSSSCT00000017903; ENSSSCP00000017422; ENSSSCG00000016442.
Ensembl; ENSSSCT00000037065; ENSSSCP00000038000; ENSSSCG00000016442.
Ensembl; ENSSSCT00000046126; ENSSSCP00000041021; ENSSSCG00000016442.
Ensembl; ENSSSCT00000054228; ENSSSCP00000042527; ENSSSCG00000016442.
GeneID; 100517436; -.
KEGG; ssc:100517436; -.
CTD; 26; -.
eggNOG; KOG1186; Eukaryota.
eggNOG; COG3733; LUCA.
GeneTree; ENSGT00510000046461; -.
InParanoid; Q9TRC7; -.
KO; K11182; -.
OMA; PLRRHFN; -.
OrthoDB; EOG091G0C1O; -.
BioCyc; MetaCyc:MONOMER-14652; -.
BRENDA; 1.4.3.22; 6170.
Reactome; R-SSC-211945; Phase I - Functionalization of compounds.
Reactome; R-SSC-6798695; Neutrophil degranulation.
SABIO-RK; Q9TRC7; -.
Proteomes; UP000008227; Chromosome 18.
Bgee; ENSSSCG00000016442; -.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0052597; F:diamine oxidase activity; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0052598; F:histamine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0052599; F:methylputrescine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0008131; F:primary amine oxidase activity; ISS:UniProtKB.
GO; GO:0052600; F:propane-1,3-diamine oxidase activity; IEA:UniProtKB-EC.
GO; GO:0032403; F:protein complex binding; ISS:UniProtKB.
GO; GO:0048038; F:quinone binding; ISS:UniProtKB.
GO; GO:0004872; F:receptor activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
GO; GO:0097185; P:cellular response to azide; ISS:UniProtKB.
GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB.
GO; GO:0035874; P:cellular response to copper ion starvation; ISS:UniProtKB.
GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
Gene3D; 2.70.98.20; -; 1.
InterPro; IPR000269; Cu_amine_oxidase.
InterPro; IPR015798; Cu_amine_oxidase_C.
InterPro; IPR036460; Cu_amine_oxidase_C_sf.
InterPro; IPR016182; Cu_amine_oxidase_N-reg.
InterPro; IPR015800; Cu_amine_oxidase_N2.
InterPro; IPR015802; Cu_amine_oxidase_N3.
PANTHER; PTHR10638; PTHR10638; 1.
Pfam; PF01179; Cu_amine_oxid; 1.
Pfam; PF02727; Cu_amine_oxidN2; 1.
Pfam; PF02728; Cu_amine_oxidN3; 1.
PRINTS; PR00766; CUDAOXIDASE.
SUPFAM; SSF49998; SSF49998; 1.
SUPFAM; SSF54416; SSF54416; 2.
PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Copper; Direct protein sequencing;
Disulfide bond; Glycoprotein; Heparin-binding; Metal-binding;
Oxidoreductase; Reference proteome; Secreted; Signal; TPQ.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 755 Amiloride-sensitive amine oxidase
[copper-containing]. {ECO:0000255}.
/FTId=PRO_0000064100.
REGION 374 384 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 461 466 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 571 578 Heparin-binding. {ECO:0000250}.
ACT_SITE 376 376 Proton acceptor.
{ECO:0000250|UniProtKB:P19801}.
ACT_SITE 464 464 Schiff-base intermediate with substrate;
via topaquinone.
{ECO:0000269|PubMed:1457410}.
METAL 513 513 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 515 515 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 522 522 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 523 523 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 524 524 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 565 565 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 656 656 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 659 659 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 661 661 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 667 667 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 668 668 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 678 678 Copper; via pros nitrogen.
{ECO:0000250|UniProtKB:P19801}.
MOD_RES 464 464 2',4',5'-topaquinone.
{ECO:0000269|PubMed:1457410}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
CARBOHYD 749 749 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
DISULFID 182 186 {ECO:0000250|UniProtKB:P19801}.
DISULFID 394 420 {ECO:0000250|UniProtKB:P19801}.
DISULFID 740 740 Interchain.
{ECO:0000250|UniProtKB:P19801}.
CONFLICT 33 33 G -> P (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 40 42 DLS -> AGV (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 44 45 QE -> ED (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 474 474 P -> Y (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 593 593 Missing (in Ref. 4; CAA23203).
{ECO:0000305}.
CONFLICT 595 597 SYR -> AVP (in Ref. 4; CAA23203).
{ECO:0000305}.
CONFLICT 602 602 S -> F (in Ref. 4; CAA23203).
{ECO:0000305}.
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


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