O75106 · AOC2_HUMAN
- ProteinAmine oxidase [copper-containing] 2
- GeneAOC2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids756 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:19588076).
Has a preference for 2-phenylethylamine, tryptamine and tyramine (PubMed:19588076).
Could also act on methylamine and benzylamine but much less efficiently (PubMed:19588076).
Has a preference for 2-phenylethylamine, tryptamine and tyramine (PubMed:19588076).
Could also act on methylamine and benzylamine but much less efficiently (PubMed:19588076).
Catalytic activity
- 2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 + NH4+This reaction proceeds in the forward direction.
- H2O + O2 + tryptamine = H2O2 + indole-3-acetaldehyde + NH4+This reaction proceeds in the forward direction.
- H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 + NH4+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 copper ion per subunit.
Note: Binds 2 calcium ions per subunit.
Note: Contains 1 topaquinone per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.056 mM | tryptamine | |||||
0.077 mM | 2-phenylethylamine | |||||
0.167 mM | benzylamine | |||||
0.178 mM | p-tyramine | |||||
1.7 mM | methylamine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
28 nmol/h/mg | with tryptamine as substrate | ||||
44 nmol/h/mg | with 2-phenylethylamine as substrate | ||||
11 nmol/h/mg | with benzylamine as substrate | ||||
43 nmol/h/mg | with p-tyramine as substrate | ||||
2.4 nmol/h/mg | with methylamine as substrate |
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 380 | Proton acceptor | ||||
Sequence: D | ||||||
Active site | 465 | Schiff-base intermediate with substrate; via topaquinone | ||||
Sequence: Y | ||||||
Binding site | 516 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 518 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 525 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 526 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 527 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 568 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 637 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 659 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 661 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 663 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 669 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 670 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 680 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | aliphatic amine oxidase activity | |
Molecular Function | copper ion binding | |
Molecular Function | electron transfer activity | |
Molecular Function | primary amine oxidase activity | |
Molecular Function | quinone binding | |
Biological Process | amine metabolic process | |
Biological Process | catecholamine metabolic process | |
Biological Process | visual perception | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAmine oxidase [copper-containing] 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO75106
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Cell membrane ; Single-pass type II membrane protein
Isoform 2
Note: Either not translocated to the plasma membrane or below detection level.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4 | Cytoplasmic | ||||
Sequence: MHLK | ||||||
Transmembrane | 5-25 | Helical | ||||
Sequence: IVLAFLALSLITIFALAYVLL | ||||||
Topological domain | 26-756 | Extracellular | ||||
Sequence: TSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLELLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRNSPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFINNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVYFEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_025022 | 5 | in dbSNP:rs34230945 | |||
Sequence: I → V | ||||||
Natural variant | VAR_025023 | 22 | in dbSNP:rs34435306 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_025024 | 141 | in dbSNP:rs35833794 | |||
Sequence: P → L | ||||||
Natural variant | VAR_025025 | 273 | in dbSNP:rs35508987 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_025026 | 427 | in dbSNP:rs34351794 | |||
Sequence: E → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 979 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000035671 | 1-756 | Amine oxidase [copper-containing] 2 | |||
Sequence: MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLELLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRNSPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLPGAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALEGRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDVVFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYRIQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFINNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVYFEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF | ||||||
Glycosylation | 133 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 198 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 226 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 398↔424 | |||||
Sequence: CPYQATMVDIHILVGKGAVQLLPGAVC | ||||||
Modified residue | 465 | 2',4',5'-topaquinone | ||||
Sequence: Y | ||||||
Glycosylation | 662 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 730↔737 | |||||
Sequence: CSINPVAC | ||||||
Disulfide bond | 744 | Interchain | ||||
Sequence: C |
Post-translational modification
Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer; disulfide-linked (Probable). Probably forms heterodimers with AOC3 (PubMed:19588076).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O75106 | AQP6 Q13520 | 3 | EBI-17685278, EBI-13059134 | |
BINARY | O75106 | ERGIC3 Q9Y282 | 3 | EBI-17685278, EBI-781551 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O75106-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsLong
- Length756
- Mass (Da)83,673
- Last updated2006-01-24 v2
- Checksum10263D8D56D3BD25
O75106-2
- Name2
- SynonymsShort
- Differences from canonical
- 599-625: Missing
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 181 | in Ref. 1 and 2 | ||||
Sequence: E → D | ||||||
Sequence conflict | 215-218 | in Ref. 1 and 2 | ||||
Sequence: GDRA → RERT | ||||||
Sequence conflict | 221-222 | in Ref. 1 | ||||
Sequence: MA → IG | ||||||
Alternative sequence | VSP_006549 | 599-625 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 610 | in Ref. 1 and 2 | ||||
Sequence: H → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D88213 EMBL· GenBank· DDBJ | BAA19001.1 EMBL· GenBank· DDBJ | mRNA | ||
AB012943 EMBL· GenBank· DDBJ | BAA32590.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB012943 EMBL· GenBank· DDBJ | BAA32589.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF081363 EMBL· GenBank· DDBJ | AAD39345.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ060035 EMBL· GenBank· DDBJ | AAY43129.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC016889 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471152 EMBL· GenBank· DDBJ | EAW60895.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC142641 EMBL· GenBank· DDBJ | AAI42642.1 EMBL· GenBank· DDBJ | mRNA |