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0AOC3_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameAOC3
DescriptionMembrane copper amine oxidase (ec 1.4.3.6) (vascular adhesion protein 1) (vap-1) (hpao).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016021 integral to membrane (TAS)
0005886 plasma membrane (TAS)
0005489 electron transporter activity (TAS)
0009308 amine metabolism (TAS)
0007155 cell adhesion (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters.istamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing () and copper-containing ().Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes.ith the subsequent release of ammonia and hydrogen peroxide: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 which requires one copper ion per subunit and topaquinone as cofactor . Copper-containing amine oxidases are found in bacteria.ungi.lants and animals. In prokaryotes.he enzyme enables various amine substrates to be used as sources of carbon and nitrogen . In eukaryotes they have a broader range of functions.ncluding cell differentiation and growth.ound healing.etoxification and cell signalling .The copper amine oxidases occur as mushroom-shaped homodimers of 70-95 kDa.ach monomer containing a copper ion and a covalently bound redox cofactor.opaquinone (TPQ). TPQ is formed by post-translational modification of a conserved tyrosine residue. The copper ion is coordinated with three histidine residues and two water molecules in a distorted square pyramidal geometry.nd has a dual function in catalysis and TPQ biogenesis. The catalytic domain is the largest of the 3-4 domains found in copper amine oxidases.nd consists of a beta sandwich of 18 strands in two sheets. The active site is buried and requires a conformational change to allow the substrate access.
  IPR000269:Copper amine oxidase
IPR000269:Cu_amine_oxid 
Evalue:-228.552841186523 
Location:309-723IPR000269:Cu_amine_oxidN3 
Evalue:-34.1870880126953 
Location:168-268IPR000269:Cu_amine_oxidN2 
Evalue:-29.6020603179932 
Location:65-151
SequencesProtein: AOC3_HUMAN (763 aa)
mRNA: NM_003734
Local Annotation
Synapse Ontology
?
sdb:0328 transmitters release and endocytosis  (Evidence:domains)
KO assignmentK00276
  Level 3 annotation:
    copper amine oxidase
  Level 2 annotation:
    Glycine
     serine and threonine metabolism
    Arginine and proline metabolism
    Histidine metabolism
    Tyrosine metabolism
    Phenylalanine metabolism
    Tryptophan metabolism
    beta-Alanine metabolism
    Alkaloid biosynthesis II
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 587 residues, 38256726-38258486Exon2: 97 residues, 38259990-38260276Exon3: 45 residues, 38260986-38261116Exon4: 617 residues, 38261817-38263664Exon5: 2 residues, -Jump to AOC3_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4288 37562438-37586822 ~-24K 15872(KCNH4)(-)Loci: 4289 37589603-37590996 ~-1K 15873(HCRT)(-)Loci: 3002 37864387-37928122 ~-64K 15882(ATP6V0A1)(+)Loci: 3003 37941476-37949990 ~-9K 15887(NAGLU)(+)Loci: 3004 38064836-38072549 ~-8K 15898(TUBG2)(+)Loci: 3005 38088157-38105358 ~-17K 15903(CNTNAP1)(+)Loci: 4290 38105819-38150574 ~-45K 15904(EZH1)(-)Loci: 3006 38186221-38202605 ~-16K 15907(WNK4)(+)Loci: 4291 38215677-38229807 ~-14K 15912(BECN1)(-)Loci: 3007 38250134-38256248 ~-6K 15916(AOC2)(+)Loci: 3008 38256726-38263664 ~-7K 15917(AOC3)(+)Loci: 4292 38420147-38427921 ~-8K 15927(VAT1)(-)Loci: 4293 38449839-38530657 ~-81K 15931(BRCA1)(-)Loci: 4287 37530523-37560548 ~-30K 15871(RAB5C)(-)Link out to UCSC