AOC1_MOUSE
ID AOC1_MOUSE Reviewed; 751 AA.
AC Q8JZQ5; Q8R229; Q8VC36;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Amiloride-sensitive amine oxidase [copper-containing];
DE Short=DAO;
DE Short=Diamine oxidase;
DE EC=1.4.3.22 {ECO:0000250|UniProtKB:P19801};
DE AltName: Full=Amiloride-binding protein 1;
DE AltName: Full=Amine oxidase copper domain-containing protein 1;
DE AltName: Full=Histaminase;
DE Flags: Precursor;
GN Name=Aoc1; Synonyms=Abp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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;
CC Evidence={ECO:0000250|UniProtKB:P19801};
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 -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P19801}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}.
CC -!- MISCELLANEOUS: Inhibited by amiloride in a competitive manner.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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; BC021880; AAH21880.1; -; mRNA.
DR EMBL; BC022627; AAH22627.1; -; mRNA.
DR EMBL; BC034215; AAH34215.1; -; mRNA.
DR AlphaFoldDB; Q8JZQ5; -.
DR SMR; Q8JZQ5; -.
DR STRING; 10090.ENSMUSP00000124085; -.
DR GlyGen; Q8JZQ5; 4 sites.
DR iPTMnet; Q8JZQ5; -.
DR PhosphoSitePlus; Q8JZQ5; -.
DR MaxQB; Q8JZQ5; -.
DR PaxDb; Q8JZQ5; -.
DR PRIDE; Q8JZQ5; -.
DR ProteomicsDB; 281778; -.
DR MGI; MGI:1923757; Aoc1.
DR eggNOG; KOG1186; Eukaryota.
DR InParanoid; Q8JZQ5; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR ChiTaRS; Aoc1; mouse.
DR PRO; PR:Q8JZQ5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8JZQ5; protein.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0052597; F:diamine oxidase activity; ISS: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:0097159; F:organic cyclic compound binding; ISO:MGI.
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; ISO:MGI.
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:0015898; P:amiloride transport; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0046677; P:response to antibiotic; ISS: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 2: Evidence at transcript level;
KW Calcium; Copper; Disulfide bond; Glycoprotein; Heparin-binding;
KW Metal-binding; Oxidoreductase; Reference proteome; Secreted; Signal; TPQ.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..751
FT /note="Amiloride-sensitive amine oxidase [copper-
FT containing]"
FT /evidence="ECO:0000250"
FT /id="PRO_0000035667"
FT ACT_SITE 373
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 461
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 371..381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 458..463
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 510
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 512
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 520
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 521
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 568..575
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
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 658
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 664
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 665
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 675
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT MOD_RES 461
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 391..417
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 736
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CONFLICT 20
FT /note="A -> P (in Ref. 1; AAH21880)"
FT /evidence="ECO:0000305"
SQ 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
