Reviewed,
UniProtKB/Swiss-Prot P19643 (AOFB_RAT)
Last modified
June 16, 2009.
Version 74.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Amine oxidase [flavin-containing] B EC=1.4.3.4 Alternative name(s): Monoamine oxidase type B Short name=MAO-B | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 520 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine. |
| Catalytic activity | RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2. |
| Cofactor | FAD. |
| Subunit structure | Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer By similarity. |
| Subcellular location | Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side. |
| Sequence similarities | Belongs to the flavin monoamine oxidase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane Mitochondrion Mitochondrion outer membrane |
| Domain | Transmembrane |
| Ligand | FAD Flavoprotein |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological process | neurotransmitter catabolic process Traceable author statement. Source: RGD oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membraneTraceable author statement. Source: RGD |
| Molecular function | amine oxidase activity Traceable author statement. Source: RGD electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 520 | 519 | Amine oxidase [flavin-containing] B | PRO_0000099863 | |||||
Regions | |||||||||
| Topological domain | 2 – 489 | 488 | Cytoplasmic By similarity | ||||||
| Transmembrane | 490 – 516 | 27 | Anchor for type IV membrane protein By similarity | ||||||
| Topological domain | 517 – 520 | 4 | Mitochondrial intermembrane By similarity | ||||||
| Compositional bias | 36 – 52 | 17 | Arg/Lys-rich (basic) | ||||||
Sites | |||||||||
| Site | 156 | 1 | Important for catalytic activity By similarity | ||||||
| Site | 365 | 1 | Important for catalytic activity By similarity | ||||||
| Site | 382 | 1 | Important for catalytic activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylserine By similarity | ||||||
| Modified residue | 52 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 397 | 1 | S-8alpha-FAD cysteine By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 139 | 1 | L → H: No change in substrate affinity. | ||||||
| Mutagenesis | 199 | 1 | I → F: Increased affinity for serotonin and tyramine. Ref.3 | ||||||
| Sequence conflict | 38 | 1 | R → C in AAA41566. Ref.1 | ||||||
| Sequence conflict | 335 – 336 | 2 | GS → AG in AAA41566. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of a cDNA for rat liver monoamine oxidase B." Ito A., Kuwahara T., Inadome S., Sagara Y. Biochem. Biophys. Res. Commun. 157:970-976(1988) [PubMed: 2974701] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver. |
| [3] | "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B." Tsugeno Y., Ito A. J. Biol. Chem. 272:14033-14036(1997) [PubMed: 9162023] [Abstract] Cited for: MUTAGENESIS OF ILE-199. |
Cross-references
Sequence databases | |
|---|---|
| M23601 mRNA. Translation: AAA41566.1. BC089814 mRNA. Translation: AAH89814.1. | |
| IPI | IPI00231774. |
| PIR | A31870. |
| RefSeq | NP_037330.1. |
| UniGene | Rn.6656 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GOS based on UniProtKB P27338. |
| SMR | P19643. Positions 3-501. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOG00000029778. Rattus norvegicus. [Contig view] |
| GeneID | 25750. |
| KEGG | rno:25750. |
Organism-specific databases | |
| RGD | 3041. Maob. |
Phylogenomic databases | |
| HOVERGEN | P19643. |
Enzyme and pathway databases | |
| BRENDA | 1.4.3.4. 248. |
Gene expression databases | |
| ArrayExpress | P19643. |
| GermOnline | ENSRNOG00000029778. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view] |
| Pfam | PF01593. Amino_oxidase. 1 hit. [Graphical view] |
| PRINTS | PR00757. AMINEOXDASEF. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 607939. |
Entry information
| Entry name | AOFB_RAT | ||||||||
| Accession | Primary (citable) accession number: P19643 Secondary accession number(s): Q5EBB5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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