Q7TT41 · MOXD2_MOUSE
- ProteinDBH-like monooxygenase protein 2
- GeneMoxd2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids619 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
Cofactor
Note: Binds 2 copper ions per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 209 | |||||
Sequence: Y | ||||||
Binding site | 241 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 242 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 309 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 390 | |||||
Sequence: H | ||||||
Binding site | 390 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 392 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 465 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: M |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | secretory granule membrane | |
Molecular Function | copper ion binding | |
Molecular Function | dopamine beta-monooxygenase activity | |
Biological Process | dopamine catabolic process | |
Biological Process | norepinephrine biosynthetic process | |
Biological Process | octopamine biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDBH-like monooxygenase protein 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ7TT41
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 22-594 | Extracellular | ||||
Sequence: KRLGPTSPLRYSRFLDPSRAVFLRWDFDYEAEIITFELQVQTTGWVGLGITDRYTFVGSDLVVGGVLPNGNVYFSDQHLLDEDTLEQDGSQDAELLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMRVLAAYGPDDIPKMSREHTFVKSIFLLQMLQYDDQDAPEDTIIHDLKISNFIIPEDDTTYACTFLPLPIVSKKHHIYKFEPILVERNETMVHHVLVYACGNSSVLPTGIGECYGSDPAFSLCSHVIAGWAVGGLSYQFPDDVGISIGTPFDPQWIRLEIHYSNFQNLPGIRDTSGMRLFYTSHLRKYDMGVLQLGISVFPIHFIPPGAEAFLSYGLCKTDKFEELNGAPVSDIYISACLLHTHLAGRSLQALQYRNGTQLQVVCKDFSYDFNLQESRDLPHPVVIKPGDELLIECHYQTLDRDFMTFGGASTINEMCLIFFFYYPRINISSCMGYPDIIYVTNELGEEASENPMENLMVLDNVEWTPENIKKAEKACKESQQTVLIKTIDEEVENTTGWIPDIIPTPRGPCLESTGGKVEPQDNTPAGFRAVPLALSGSNTATLR | ||||||
Transmembrane | 595-615 | Helical | ||||
Sequence: PLPMIAVLFLQGSLSCLLAML | ||||||
Topological domain | 616-619 | Cytoplasmic | ||||
Sequence: QTGV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MACVLLFRLFLLLVLAAFSQG | ||||||
Chain | PRO_0000305224 | 22-619 | DBH-like monooxygenase protein 2 | |||
Sequence: KRLGPTSPLRYSRFLDPSRAVFLRWDFDYEAEIITFELQVQTTGWVGLGITDRYTFVGSDLVVGGVLPNGNVYFSDQHLLDEDTLEQDGSQDAELLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMRVLAAYGPDDIPKMSREHTFVKSIFLLQMLQYDDQDAPEDTIIHDLKISNFIIPEDDTTYACTFLPLPIVSKKHHIYKFEPILVERNETMVHHVLVYACGNSSVLPTGIGECYGSDPAFSLCSHVIAGWAVGGLSYQFPDDVGISIGTPFDPQWIRLEIHYSNFQNLPGIRDTSGMRLFYTSHLRKYDMGVLQLGISVFPIHFIPPGAEAFLSYGLCKTDKFEELNGAPVSDIYISACLLHTHLAGRSLQALQYRNGTQLQVVCKDFSYDFNLQESRDLPHPVVIKPGDELLIECHYQTLDRDFMTFGGASTINEMCLIFFFYYPRINISSCMGYPDIIYVTNELGEEASENPMENLMVLDNVEWTPENIKKAEKACKESQQTVLIKTIDEEVENTTGWIPDIIPTPRGPCLESTGGKVEPQDNTPAGFRAVPLALSGSNTATLRPLPMIAVLFLQGSLSCLLAMLQTGV | ||||||
Disulfide bond | 211↔261 | |||||
Sequence: CTFLPLPIVSKKHHIYKFEPILVERNETMVHHVLVYACGNSSVLPTGIGEC | ||||||
Disulfide bond | 248↔271 | |||||
Sequence: CGNSSVLPTGIGECYGSDPAFSLC | ||||||
Glycosylation | 250 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 366↔481 | |||||
Sequence: CKTDKFEELNGAPVSDIYISACLLHTHLAGRSLQALQYRNGTQLQVVCKDFSYDFNLQESRDLPHPVVIKPGDELLIECHYQTLDRDFMTFGGASTINEMCLIFFFYYPRINISSC | ||||||
Glycosylation | 405 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 444↔466 | |||||
Sequence: CHYQTLDRDFMTFGGASTINEMC | ||||||
Glycosylation | 477 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 40-156 | DOMON | ||||
Sequence: RAVFLRWDFDYEAEIITFELQVQTTGWVGLGITDRYTFVGSDLVVGGVLPNGNVYFSDQHLLDEDTLEQDGSQDAELLRLTEDAVSTTMRFSRPFRTCDPHDRDITSDTMRVLAAYG |
Sequence similarities
Belongs to the copper type II ascorbate-dependent monooxygenase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length619
- Mass (Da)69,397
- Last updated2003-10-01 v1
- Checksum74518832AD5E1A63
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 289 | in Ref. 2; BAB62024 | ||||
Sequence: D → G | ||||||
Sequence conflict | 561 | in Ref. 2; BAB62024 | ||||
Sequence: L → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000663 EMBL· GenBank· DDBJ | AAB69054.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB065134 EMBL· GenBank· DDBJ | BAB62024.1 EMBL· GenBank· DDBJ | mRNA |