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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_RAT                Reviewed;         746 AA.
P36633; Q63973;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 131.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Colon, and Lung;
PubMed=8375402; DOI=10.1111/j.1432-1033.1993.tb18188.x;
Lingueglia E., Renard S., Voilley N., Waldmann R., Chassande O.,
Lazdunski M., Barbry P.;
"Molecular cloning and functional expression of different molecular
forms of rat amiloride-binding proteins.";
Eur. J. Biochem. 216:679-687(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8023885;
Verity K., Fuller P.J.;
"Isolation of a rat amiloride-binding protein cDNA clone: tissue
distribution and regulation of expression.";
Am. J. Physiol. 266:C1505-C1512(1994).
-!- 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.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAA52117.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X73911; CAA52116.1; -; mRNA.
EMBL; X73912; CAA52117.1; ALT_INIT; mRNA.
EMBL; S70383; AAB31157.1; -; mRNA.
PIR; S36847; S34656.
UniGene; Rn.54493; -.
ProteinModelPortal; P36633; -.
SMR; P36633; -.
STRING; 10116.ENSRNOP00000055909; -.
BindingDB; P36633; -.
ChEMBL; CHEMBL4648; -.
PhosphoSitePlus; P36633; -.
PaxDb; P36633; -.
PRIDE; P36633; -.
UCSC; RGD:61296; rat.
RGD; 61296; Aoc1.
eggNOG; KOG1186; Eukaryota.
eggNOG; COG3733; LUCA.
HOVERGEN; HBG004164; -.
InParanoid; P36633; -.
BRENDA; 1.4.3.22; 5301.
PRO; PR:P36633; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISO:RGD.
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:RGD.
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:0042803; F:protein homodimerization activity; ISO:RGD.
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; IDA: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; 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 23 746 Amiloride-sensitive amine oxidase
[copper-containing].
/FTId=PRO_0000035668.
REGION 366 376 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 453 458 Substrate binding.
{ECO:0000250|UniProtKB:P19801}.
REGION 563 570 Heparin-binding. {ECO:0000250}.
ACT_SITE 368 368 Proton acceptor.
{ECO:0000250|UniProtKB:P19801}.
ACT_SITE 456 456 Schiff-base intermediate with substrate;
via topaquinone.
{ECO:0000250|UniProtKB:P19801}.
METAL 505 505 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 507 507 Copper; via tele nitrogen.
{ECO:0000250|UniProtKB:P19801}.
METAL 514 514 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 516 516 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 557 557 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 648 648 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 651 651 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 653 653 Calcium 2.
{ECO:0000250|UniProtKB:P19801}.
METAL 659 659 Calcium 1.
{ECO:0000250|UniProtKB:P19801}.
METAL 660 660 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P19801}.
METAL 670 670 Copper; via pros nitrogen.
{ECO:0000250|UniProtKB:P19801}.
MOD_RES 456 456 2',4',5'-topaquinone.
{ECO:0000250|UniProtKB:P12807}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
CARBOHYD 740 740 N-linked (GlcNAc...) asparagine.
{ECO:0000250|UniProtKB:P19801}.
DISULFID 177 181 {ECO:0000250|UniProtKB:P19801}.
DISULFID 386 412 {ECO:0000250|UniProtKB:P19801}.
DISULFID 731 731 Interchain.
{ECO:0000250|UniProtKB:P19801}.
CONFLICT 587 587 S -> T (in Ref. 2; AAB31157).
{ECO:0000305}.
SEQUENCE 746 AA; 85021 MW; 6C564D044D07BCB2 CRC64;
MCLAFGWAAV ILVLQTVDTA SAVRTPYDKA RVFADLSPQE IKAVHSFLMN REELGLQPSK
EPTLAKNSVF LIEMLLPKKK HVLKFLDEGR KGPNREARAV IFFGAQDYPN VTEFAVGPLP
RPYYIRALSP RPGHHLSWSS RPISTAEYDL LYHTLKRATM PLHQFFLDTT GFSFLGCDDR
CLTFTDVAPR GVASGQRRSW FIVQRYVEGY FLHPTGLEIL LDHGSTDVQD WRVEQLWYNG
KFYNNPEELA RKYAVGEVDT VVLEDPLPNG TEKPPLFSSY KPRGEFHTPV NVAGPHVVQP
SGPRYKLEGN TVLYGGWSFS YRLRSSSGLQ IFNVLFGGER VAYEVSVQEA VALYGGHTPA
GMQTKYIDVG WGLGSVTHEL APGIDCPETA TFLDAFHYYD SDGPVHYPHA LCLFEMPTGV
PLRRHFNSNF KGGFNFYAGL KGYVLVLRTT STVYNYDYIW DFIFYSNGVM EAKMHATGYV
HATFYTPEGL RHGTRLQTHL LGNIHTHLVH YRVDMDVAGT KNSFQTLTMK LENLTNPWSP
SHSLVQPTLE QTQYSQEHQA AFRFGQTLPK YLLFSSPQKN CWGHRRSYRL QIHSMAEQVL
PPGWQEERAV TWARYPLAVT KYRESERYSS SLYNQNDPWD PPVVFEEFLR NNENIEDEDL
VAWVTVGFLH IPHSEDVPNT ATPGNSVGFL LRPFNFFPED PSLASRDTVI VWPQDKGLNR
VQRWIPEDRR CLVSPPFSYN GTYKPV


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