AOC2_MOUSE
ID AOC2_MOUSE Reviewed; 757 AA.
AC Q812C9; A2A4J0; Q80WP3;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Retina-specific copper amine oxidase;
DE Short=RAO;
DE EC=1.4.3.21 {ECO:0000250|UniProtKB:P19801};
DE AltName: Full=Amine oxidase [copper-containing];
DE Flags: Precursor;
GN Name=Aoc2;
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].
RX PubMed=14585497; DOI=10.1016/s0378-1119(03)00753-4;
RA Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N.,
RA Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.;
RT "Characterization of AOC2 gene encoding a copper-binding amine oxidase
RT expressed specifically in retina.";
RL Gene 318:45-53(2003).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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).
CC -!- FUNCTION: Has a monoamine oxidase activity with substrate specificity
CC for 2-phenylethylamine and tryptamine. May play a role in adipogenesis.
CC May be a critical modulator of signal transmission in retina (By
CC 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 AOC3 (By similarity). {ECO:0000250|UniProtKB:O75106,
CC ECO:0000250|UniProtKB:P19801}.
CC -!- TISSUE SPECIFICITY: Significantly much highly expressed in retina.
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}.
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; AF350445; AAK58864.2; -; mRNA.
DR EMBL; AF350446; AAK58865.1; -; Genomic_DNA.
DR EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150843; AAI50844.1; -; mRNA.
DR EMBL; BC150848; AAI50849.1; -; mRNA.
DR CCDS; CCDS25464.1; -.
DR RefSeq; NP_849263.1; NM_178932.1.
DR AlphaFoldDB; Q812C9; -.
DR SMR; Q812C9; -.
DR STRING; 10090.ENSMUSP00000040255; -.
DR GlyConnect; 2684; 2 N-Linked glycans (1 site).
DR GlyGen; Q812C9; 5 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q812C9; -.
DR PhosphoSitePlus; Q812C9; -.
DR MaxQB; Q812C9; -.
DR PaxDb; Q812C9; -.
DR PRIDE; Q812C9; -.
DR ProteomicsDB; 296320; -.
DR Antibodypedia; 17156; 81 antibodies from 17 providers.
DR DNASU; 237940; -.
DR Ensembl; ENSMUST00000041095; ENSMUSP00000040255; ENSMUSG00000078651.
DR GeneID; 237940; -.
DR KEGG; mmu:237940; -.
DR UCSC; uc007loo.1; mouse.
DR CTD; 314; -.
DR MGI; MGI:2668431; Aoc2.
DR VEuPathDB; HostDB:ENSMUSG00000078651; -.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR InParanoid; Q812C9; -.
DR OMA; QDFSKFF; -.
DR OrthoDB; 1320015at2759; -.
DR PhylomeDB; Q812C9; -.
DR TreeFam; TF314750; -.
DR Reactome; R-MMU-211945; Phase I - Functionalization of compounds.
DR BioGRID-ORCS; 237940; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Aoc2; mouse.
DR PRO; PR:Q812C9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q812C9; protein.
DR Bgee; ENSMUSG00000078651; Expressed in bone marrow and 56 other tissues.
DR ExpressionAtlas; Q812C9; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR032952; AOC2.
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 PANTHER; PTHR10638:SF4; PTHR10638:SF4; 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; Catecholamine metabolism; Copper; Disulfide bond; Glycoprotein;
KW Metal-binding; Oxidoreductase; Reference proteome; Signal; TPQ.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..757
FT /note="Retina-specific copper amine oxidase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000035672"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT ACT_SITE 466
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 379..389
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 463..468
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 517
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 519
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 526
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 527
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 528
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 569
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 575..582
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 660
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 662
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="2"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 671
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT BINDING 681
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT MOD_RES 466
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000250|UniProtKB:P12807"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 589
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 399..425
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT DISULFID 731..738
FT /evidence="ECO:0000250|UniProtKB:Q16853"
FT DISULFID 745
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P19801"
FT CONFLICT 53
FT /note="S -> N (in Ref. 1; AAK58865)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> A (in Ref. 1; AAK58865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 83583 MW; 4D93D9839AD57159 CRC64;
MNLKVLLLLL GLSFLTVFAL VYVLLTRQGS FSQSPRCPSI PPRIHPWTHP SQSQLFADLT
PEELTAVMSF LTKHLGPGLV DAAQARPSDN CVFSVELQLP AKAAALAHLD RGGPPPVREA
LAIIFFGGQP KPNVSELVVG PLPHPSYMRD VTVERHGGPL PYYRRPMQKT EFVQIWRHLK
EVELPKAPTF LASVLNYNGS TLAPLHSTAS GFHAGDRATW IALYHNISGL GVFLHPVGLE
LLLDHGALDP ADWVVQQVFY LGHYYADLAQ LEWEFKVGRL EVIRVPLPTP GGASSLRPRV
TPDPPLPPLQ FSLQGPQYNI QGNSVTSPLW TFTFGHGVFS GLRIFDIRFK GERVAYEVSV
QECLTVYGAD SPKTMTIRYL DSSYGLGLNS RALVRGVDCP YQATMVDIHV LVGTGSVQLL
PGAVCVFEEA QGLPLRRHHN GIGGHFYGGL ASSSLVVRSV SSVGNYDYIW DFMLHPTGAL
EARVHATGYI NTAFMSGGAE SLLFGNRVGE RVLGAVHTHA FHFKLDLDVA GLKNWVIAED
AVFKPVAAPW NPELQLQRPQ LTRQVLSRED LAAFPWGSPL PRYLYLATNQ TNAWGHQRGY
RIQIHSPPGV HVPLESSEER ALSWGRYQLV VTQRKEAEPH SSSIYYQNDM RSPATVFADF
INNETLLGED LVAWVTASFL HIPHAEDIPN TVTVGNRVGF LLRPYNFFNE DPSIFSPGSV
YFERDQDAGL CSINPVACTQ QLADCVPNLP SFSYEGL
