AOC1_RAT
ID AOC1_RAT Reviewed; 746 AA.
AC P36633; Q63973;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 148.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Colon, and Lung;
RX PubMed=8375402; DOI=10.1111/j.1432-1033.1993.tb18188.x;
RA Lingueglia E., Renard S., Voilley N., Waldmann R., Chassande O.,
RA Lazdunski M., Barbry P.;
RT "Molecular cloning and functional expression of different molecular forms
RT of rat amiloride-binding proteins.";
RL Eur. J. Biochem. 216:679-687(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8023885; DOI=10.1152/ajpcell.1994.266.6.c1505;
RA Verity K., Fuller P.J.;
RT "Isolation of a rat amiloride-binding protein cDNA clone: tissue
RT distribution and regulation of expression.";
RL Am. J. Physiol. 266:C1505-C1512(1994).
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.
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 -!- SEQUENCE CAUTION:
CC Sequence=CAA52117.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X73911; CAA52116.1; -; mRNA.
DR EMBL; X73912; CAA52117.1; ALT_INIT; mRNA.
DR EMBL; S70383; AAB31157.1; -; mRNA.
DR PIR; S36847; S34656.
DR AlphaFoldDB; P36633; -.
DR SMR; P36633; -.
DR STRING; 10116.ENSRNOP00000055909; -.
DR BindingDB; P36633; -.
DR ChEMBL; CHEMBL4648; -.
DR DrugCentral; P36633; -.
DR GlyGen; P36633; 4 sites.
DR PhosphoSitePlus; P36633; -.
DR PaxDb; P36633; -.
DR UCSC; RGD:61296; rat.
DR RGD; 61296; Aoc1.
DR eggNOG; KOG1186; Eukaryota.
DR InParanoid; P36633; -.
DR BRENDA; 1.4.3.22; 5301.
DR Reactome; R-RNO-211945; Phase I - Functionalization of compounds.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P36633; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IDA:RGD.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
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:RGD.
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:0097159; F:organic cyclic compound binding; IPI:RGD.
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:RGD.
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; IDA: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; IDA: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; 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 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..746
FT /note="Amiloride-sensitive amine oxidase [copper-
FT containing]"
FT /id="PRO_0000035668"
FT ACT_SITE 368
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 456
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 366..376
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 453..458
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 505
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 507
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 514
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 563..570
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
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 659
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 660
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 670
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT MOD_RES 456
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 177..181
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 386..412
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 731
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CONFLICT 587
FT /note="S -> T (in Ref. 2; AAB31157)"
FT /evidence="ECO:0000305"
SQ 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
