ID   AOC3_MOUSE              Reviewed;         765 AA.
AC   O70423; A2A4I7; Q66JM4; Q9R055;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Amine oxidase [copper-containing] 3 {ECO:0000250|UniProtKB:Q16853};
DE            EC=1.4.3.21 {ECO:0000250|UniProtKB:Q16853};
DE   AltName: Full=Amine oxidase copper-containing 3 {ECO:0000312|MGI:MGI:1306797};
DE   AltName: Full=Copper amine oxidase;
DE   AltName: Full=Semicarbazide-sensitive amine oxidase;
DE            Short=SSAO;
DE   AltName: Full=Vascular adhesion protein 1 {ECO:0000303|PubMed:9743358};
DE            Short=VAP-1 {ECO:0000303|PubMed:9743358};
GN   Name=Aoc3 {ECO:0000312|MGI:MGI:1306797}; Synonyms=Vap1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=129/SvJ, and BALB/cJ;
RX   PubMed=9743358;
RA   Bono P., Salmi M., Smith D.J., Leppanen I., Horelli-Kuitunen N.,
RA   Palotie A., Jalkanen S.;
RT   "Isolation, structural characterization, and chromosomal mapping of the
RT   mouse vascular adhesion protein-1 gene and promoter.";
RL   J. Immunol. 161:2953-2960(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10092636; DOI=10.1074/jbc.274.14.9515;
RA   Moldes M., Feve B., Pairault J.;
RT   "Molecular cloning of a major mRNA species in murine 3T3 adipocyte lineage.
RT   differentiation-dependent expression, regulation, and identification as
RT   semicarbazide-sensitive amine oxidase.";
RL   J. Biol. Chem. 274:9515-9523(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the oxidative deamination of primary amines to the
CC       corresponding aldehydes with the concomitant production of hydrogen
CC       peroxide and ammonia. Has a preference for the primary monoamines
CC       methylamine and benzylamine. Could also act on 2-phenylethylamine but
CC       much less efficiently. At endothelial cells surface can also function
CC       as a cell adhesion protein that participates in lymphocyte
CC       extravasation and recirculation by mediating the binding of lymphocytes
CC       to peripheral lymph node vascular endothelial cells in an L-selectin-
CC       independent fashion. {ECO:0000250|UniProtKB:Q16853}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + methylamine + O2 = formaldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:59420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:59338; Evidence={ECO:0000250|UniProtKB:Q16853};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59421;
CC         Evidence={ECO:0000250|UniProtKB:Q16853};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=benzylamine + H2O + O2 = benzaldehyde + H2O2 + NH4(+);
CC         Xref=Rhea:RHEA:59424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17169, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:225238; Evidence={ECO:0000250|UniProtKB:Q16853};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425;
CC         Evidence={ECO:0000250|UniProtKB:Q16853};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:225237; EC=1.4.3.21;
CC         Evidence={ECO:0000250|UniProtKB:Q16853};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25266;
CC         Evidence={ECO:0000250|UniProtKB:Q16853};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q16853};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q16853};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:Q16853};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q16853};
CC   -!- COFACTOR:
CC       Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000250|UniProtKB:Q16853};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000250|UniProtKB:Q16853};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Probably forms heterodimers with
CC       AOC2. {ECO:0000250|UniProtKB:Q16853}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16853};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16853}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O70423-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70423-2; Sequence=VSP_016604;
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000250|UniProtKB:Q16853}.
CC   -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q16853}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AF054831; AAC23747.1; -; mRNA.
DR   EMBL; AF078705; AAC35839.1; -; Genomic_DNA.
DR   EMBL; AF115411; AAD09199.1; -; mRNA.
DR   EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC080857; AAH80857.1; -; mRNA.
DR   CCDS; CCDS25465.1; -. [O70423-1]
DR   RefSeq; NP_033805.1; NM_009675.2. [O70423-1]
DR   AlphaFoldDB; O70423; -.
DR   SMR; O70423; -.
DR   BioGRID; 198116; 1.
DR   IntAct; O70423; 1.
DR   STRING; 10090.ENSMUSP00000099394; -.
DR   BindingDB; O70423; -.
DR   ChEMBL; CHEMBL4727; -.
DR   GlyCosmos; O70423; 7 sites, No reported glycans.
DR   GlyGen; O70423; 7 sites.
DR   iPTMnet; O70423; -.
DR   PhosphoSitePlus; O70423; -.
DR   SwissPalm; O70423; -.
DR   jPOST; O70423; -.
DR   MaxQB; O70423; -.
DR   PaxDb; 10090-ENSMUSP00000099394; -.
DR   PeptideAtlas; O70423; -.
DR   ProteomicsDB; 296321; -. [O70423-1]
DR   ProteomicsDB; 296322; -. [O70423-2]
DR   Pumba; O70423; -.
DR   Antibodypedia; 611; 505 antibodies from 39 providers.
DR   DNASU; 11754; -.
DR   Ensembl; ENSMUST00000103105.10; ENSMUSP00000099394.4; ENSMUSG00000019326.15. [O70423-1]
DR   GeneID; 11754; -.
DR   KEGG; mmu:11754; -.
DR   UCSC; uc007lop.2; mouse. [O70423-1]
DR   AGR; MGI:1306797; -.
DR   CTD; 8639; -.
DR   MGI; MGI:1306797; Aoc3.
DR   VEuPathDB; HostDB:ENSMUSG00000019326; -.
DR   eggNOG; KOG1186; Eukaryota.
DR   GeneTree; ENSGT00950000183207; -.
DR   HOGENOM; CLU_015739_1_0_1; -.
DR   InParanoid; O70423; -.
DR   OMA; CMFEIDK; -.
DR   OrthoDB; 5490352at2759; -.
DR   PhylomeDB; O70423; -.
DR   TreeFam; TF314750; -.
DR   Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR   BioGRID-ORCS; 11754; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Aoc3; mouse.
DR   PRO; PR:O70423; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O70423; Protein.
DR   Bgee; ENSMUSG00000019326; Expressed in epididymal fat pad and 127 other cell types or tissues.
DR   ExpressionAtlas; O70423; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005902; C:microvillus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR   GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008131; F:primary amine oxidase activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0048038; F:quinone binding; ISS:UniProtKB.
DR   GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0042755; P:eating behavior; ISO:MGI.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISO:MGI.
DR   GO; GO:0002675; P:positive regulation of acute inflammatory response; ISO:MGI.
DR   GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISO:MGI.
DR   GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR   GO; GO:0046677; P:response to antibiotic; ISO:MGI.
DR   GO; GO:0035902; P:response to immobilization stress; ISO:MGI.
DR   Gene3D; 3.10.450.40; -; 2.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 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; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF23; MEMBRANE PRIMARY AMINE OXIDASE; 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; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
DR   Genevisible; O70423; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane; Copper;
KW   Disulfide bond; Glycoprotein; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome; Signal-anchor; TPQ; Transmembrane; Transmembrane helix.
FT   CHAIN           1..765
FT                   /note="Amine oxidase [copper-containing] 3"
FT                   /id="PRO_0000064103"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..765
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   ACT_SITE        471
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         520
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         522
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         529
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         530
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         531
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         572
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         641
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         663
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         667
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         673
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         674
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   BINDING         684
FT                   /ligand="Cu(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29036"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   MOD_RES         471
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        232
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        659
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        666
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        198..199
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   DISULFID        404..430
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   DISULFID        734..741
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   DISULFID        748
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q16853"
FT   VAR_SEQ         630..765
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016604"
FT   CONFLICT        659
FT                   /note="N -> D (in Ref. 2; AAD09199)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   765 AA;  84534 MW;  7489ED67D3DBB44D CRC64;
     MTQKTTLVLL ALAVITIFAL VCVLLAGRSG DGGGLSQPLH CPSVLPSVQP RTHPSQSQPF
     ADLSPEELTA VMSFLTKHLG PGLVDAAQAR PSDNCVFSVE LQLPAKAAAL AHLDRGGPPP
     VREALAIIFF GGQPKPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYYRRP VLDREYQDIE
     EMIFHRELPQ ASGLLHHCCF YKHQGQNLLT MTTAPRGLQS GDRATWFGLY YNLSGAGFYP
     HPIGLELLID HKALDPALWT IQKVFYQGRY YESLTQLEDQ FEAGLVNVVL VPNNGTGGSW
     SLKSSVPPGP APPLQFHPQG PRFSVQGSQV SSSLWAFSFG LGAFSGPRIF DIRFQGERVA
     YEISVQEAIA LYGGNSPASM STCYVDGSFG IGKYSTPLIR GVDCPYLATY VDWHFLLESQ
     APKTLRDAFC VFEQNQGLPL RRHHSDFYSH YFGGVVGTVL VVRSVSTLLN YDYIWDMVFH
     PNGAIEVKFH ATGYISSAFF FGAGEKFGNR VGAHTLGTVH THSAHFKVDL DVAGLKNWAW
     AEDMAFVPTI VPWQPEYQMQ RLQVTRKLLE TEEEAAFPLG GATPRYLYLA SNHSNKWGHR
     RGYRIQILSF AGKPLPQESP IEKAFTWGRY HLAVTQRKEE EPSSSSIFNQ NDPWTPTVNF
     TDFISNETIA GEDLVAWVTA GFLHIPHAED IPNTVTAGNS VGFFLRPYNF FDEDPSFHSA
     DSIYFREGQD ATACEVNPLA CLSQTATCAP EIPAFSHGGF AYRDN
//