AOC3_MOUSE
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 03-AUG-2022, entry version 172.
DE RecName: Full=Membrane primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P19801};
DE AltName: Full=Copper amine oxidase;
DE AltName: Full=Semicarbazide-sensitive amine oxidase;
DE Short=SSAO;
DE AltName: Full=Vascular adhesion protein 1;
DE Short=VAP-1;
GN Name=Aoc3; 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, and
RC 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: Cell adhesion protein that participates in lymphocyte
CC recirculation by mediating the binding of lymphocytes to peripheral
CC lymph node vascular endothelial cells in an L-selectin-independent
CC fashion. Has a monoamine oxidase activity. May play a role in
CC adipogenesis (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
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 (By similarity). Forms a
CC heterodimer with AOC2 (By similarity). {ECO:0000250|UniProtKB:P19801,
CC ECO:0000250|UniProtKB:Q16853}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
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: N- and O-glycosylated. {ECO:0000250}.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000250|UniProtKB:P12807}.
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 GlyGen; O70423; 7 sites.
DR iPTMnet; O70423; -.
DR PhosphoSitePlus; O70423; -.
DR jPOST; O70423; -.
DR MaxQB; O70423; -.
DR PaxDb; O70423; -.
DR PeptideAtlas; O70423; -.
DR PRIDE; O70423; -.
DR ProteomicsDB; 296321; -. [O70423-1]
DR ProteomicsDB; 296322; -. [O70423-2]
DR Antibodypedia; 611; 435 antibodies from 39 providers.
DR DNASU; 11754; -.
DR Ensembl; ENSMUST00000103105; ENSMUSP00000099394; ENSMUSG00000019326. [O70423-1]
DR GeneID; 11754; -.
DR KEGG; mmu:11754; -.
DR UCSC; uc007lop.2; mouse. [O70423-1]
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; 1320015at2759; -.
DR PhylomeDB; O70423; -.
DR TreeFam; TF314750; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 11754; 2 hits in 71 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 tissues.
DR ExpressionAtlas; O70423; baseline and differential.
DR Genevisible; O70423; MM.
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:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005902; C:microvillus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
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:1902283; P:negative regulation of primary amine oxidase activity; 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; 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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Copper; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Oxidoreductase; Reference proteome;
KW Signal-anchor; TPQ; Transmembrane; Transmembrane helix.
FT CHAIN 1..765
FT /note="Membrane primary amine oxidase"
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:P19801"
FT BINDING 384..394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 468..473
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 520
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 522
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 572
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 578..585
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 663
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 667
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 673
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 684
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT MOD_RES 471
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 212
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
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:0000250|UniProtKB:Q16853"
FT DISULFID 198..199
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 404..430
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 734..741
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 748
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
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
