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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_MOUSE              Reviewed;         751 AA.
Q8JZQ5; Q8R229; Q8VC36;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-APR-2018, entry version 113.
RecName: Full=Amiloride-sensitive amine oxidase [copper-containing];
Short=DAO;
Short=Diamine oxidase;
EC=1.4.3.22 {ECO:0000250|UniProtKB:P19801};
AltName: Full=Amiloride-binding protein 1;
AltName: Full=Amine oxidase copper domain-containing protein 1;
AltName: Full=Histaminase;
Flags: Precursor;
Name=Aoc1; Synonyms=Abp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- 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:0000250|UniProtKB:P19801}.
-!- 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};
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000250|UniProtKB:P19801}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
-!- PTM: Topaquinone (TPQ) is generated by copper-dependent
autoxidation of a specific tyrosyl residue.
{ECO:0000250|UniProtKB:P12807}.
-!- MISCELLANEOUS: Inhibited by amiloride in a competitive manner.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC021880; AAH21880.1; -; mRNA.
EMBL; BC022627; AAH22627.1; -; mRNA.
EMBL; BC034215; AAH34215.1; -; mRNA.
UniGene; Mm.213898; -.
ProteinModelPortal; Q8JZQ5; -.
SMR; Q8JZQ5; -.
IntAct; Q8JZQ5; 1.
MINT; Q8JZQ5; -.
STRING; 10090.ENSMUSP00000031835; -.
iPTMnet; Q8JZQ5; -.
PhosphoSitePlus; Q8JZQ5; -.
MaxQB; Q8JZQ5; -.
PaxDb; Q8JZQ5; -.
PRIDE; Q8JZQ5; -.
MGI; MGI:1923757; Aoc1.
eggNOG; KOG1186; Eukaryota.
eggNOG; COG3733; LUCA.
HOVERGEN; HBG004164; -.
InParanoid; Q8JZQ5; -.
PRO; PR:Q8JZQ5; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISO:MGI.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:0052597; F:diamine oxidase activity; ISS:UniProtKB.
GO; GO:0008144; F:drug binding; ISS: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:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0044877; F:protein-containing 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:0015898; P:amiloride transport; ISO:MGI.
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; ISS:UniProtKB.
GO; GO:0046677; P:response to antibiotic; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; ISS: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.
2: Evidence at transcript level;
Calcium; Complete proteome; Copper; Disulfide bond; Glycoprotein;
Heparin-binding; Metal-binding; Oxidoreductase; Reference proteome;
Secreted; Signal; TPQ.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 751 Amiloride-sensitive amine oxidase
[copper-containing]. {ECO:0000250}.
/FTId=PRO_0000035667.
REGION 371 381 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 458 463 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 568 575 Heparin-binding. {ECO:0000250}.
ACT_SITE 373 373 Proton acceptor.
{ECO:0000250|UniProtKB:P19801}.
ACT_SITE 461 461 Schiff-base intermediate with substrate;
via topaquinone.
{ECO:0000250|UniProtKB:P19801}.
METAL 510 510 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 512 512 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 519 519 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 520 520 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 521 521 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 562 562 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 653 653 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 656 656 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 658 658 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 664 664 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 665 665 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 675 675 Copper; via pros nitrogen.
{ECO:0000250|UniProtKB:P19801}.
MOD_RES 461 461 2',4',5'-topaquinone.
{ECO:0000250|UniProtKB:P12807}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
CARBOHYD 745 745 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
DISULFID 391 417 {ECO:0000250|UniProtKB:P19801}.
DISULFID 736 736 Interchain.
{ECO:0000250|UniProtKB:P19801}.
CONFLICT 20 20 A -> P (in Ref. 1; AAH21880).
{ECO:0000305}.
SEQUENCE 751 AA; 85424 MW; 4E9682DA7C967AC7 CRC64;
MSLAFGWAAV ILLLQTADTA SAVTTPHDKA RIFADLSPQE IKAVHSFLMS RKELGLESSK
NLTLAKNSVF LIEMLLPKKK NVLKFLDEGR KSPVREARAI IFFGAQDHPN VTEFAVGPLP
RPCYVQALSP RPGHHLSWSS RPISTAEYDL LYHMLNRAIT PLHQFFLDTT GFSFLGCDDR
FLTFTDVAPR GVESGQRRSW LIVQRYVEGY FLHPTGLEIL VDHSSTDVQD WRVEQLWYNG
KFYNSPEELA QKYAVGEVEA VVLEEVVLED PLPGATEQPP LFSSYKPRGE FHTPVTVAGP
HVVQPSGPRY KLEGNVVLYG DWSFSYRLRS SSGLQIFNVL FGGERVAYEV SVQEAVALYG
GHTPAGMQTK YIDVGWGLGS VTHELAPGID CPETATFLDA FHYYDSDGPV LYPRALCLFE
MPTGVPLRRH FDSNFKGGFN FYAGLKGYVL VLRTTSTVYN YDYIWDFIFY PNGVMETKMH
ATGYVHATFY TPEGLRHGTR LQTHLLGNIH THLVHYRVDL DVAGTKNSFR TLKTKLENIT
NPWSPSHSLV QPTLEQTQYS HEHQAAFRFG QTLPKYLLFS SPQKNRWGHR RSYRLQIHSM
AEQVLPPGWQ EERAVTWARY PLAVTKYRES ERYSSSLYNQ NDPWDPPVVF EEFLRNNENI
ENEDLVAWVT VGFLHIPHSE DVPNTATPGN CVGFLIRPFN FFEEDPSLAS RDTVIVWPQD
NGLNHVQRWI PENRDCLVSP PFSYNGTYKP V


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