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P19643 (AOFB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Amine oxidase [flavin-containing] B

EC=1.4.3.4
Alternative name(s):
Monoamine oxidase type B
Short name=MAO-B
Gene names
Name:Maob
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of serotonin secretion

Inferred from mutant phenotype PubMed 12175458. Source: RGD

neurotransmitter catabolic process

Inferred from direct assay PubMed 18539264. Source: RGD

positive regulation of dopamine metabolic process

Inferred from mutant phenotype PubMed 12175458. Source: RGD

response to aluminum ion

Inferred from expression pattern PubMed 19526156. Source: RGD

response to corticosterone

Inferred from expression pattern PubMed 15919584. Source: RGD

response to drug

Inferred from expression pattern PubMed 18256746. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 20022592. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 19779138. Source: RGD

response to selenium ion

Inferred from expression pattern PubMed 18304392. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 18539264. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 16904659. Source: RGD

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial outer membrane

Inferred from direct assay PubMed 18502718. Source: RGD

   Molecular_functionflavin adenine dinucleotide binding

Inferred from direct assay PubMed 18424170. Source: RGD

primary amine oxidase activity

Inferred from direct assay PubMed 18424170. Source: RGD

protein homodimerization activity

Inferred from direct assay PubMed 18198902. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 520519Amine oxidase [flavin-containing] B
PRO_0000099863

Regions

Topological domain2 – 489488Cytoplasmic By similarity
Transmembrane490 – 51627Helical; Anchor for type IV membrane protein; By similarity
Topological domain517 – 5204Mitochondrial intermembrane By similarity
Compositional bias36 – 5217Arg/Lys-rich (basic)

Sites

Site1561Important for catalytic activity By similarity
Site3651Important for catalytic activity By similarity
Site3821Important for catalytic activity By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue521N6-acetyllysine By similarity
Modified residue3971S-8alpha-FAD cysteine By similarity

Experimental info

Mutagenesis1391L → H: No change in substrate affinity.
Mutagenesis1991I → F: Increased affinity for serotonin and tyramine. Ref.3
Sequence conflict381R → C in AAA41566. Ref.1
Sequence conflict335 – 3362GS → AG in AAA41566. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19643 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F2C230BC6CDE5840

FASTA52058,459
        10         20         30         40         50         60 
MSNKCDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN VKYVDLGGSY 

        70         80         90        100        110        120 
VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR GPFPPVWNPI TYLDYNNLWR 

       130        140        150        160        170        180 
TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE LLDKICWTNS TKQIATLFVN LCVTAETHEV 

       190        200        210        220        230        240 
SALWFLWYVK QCGGTTRIIS TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ 

       250        260        270        280        290        300 
TGENVVVKTL NHEIYEAKYV ISAIPPVLGM KIHHSPPLPI LRNQLITRVP LGSVIKCMVY 

       310        320        330        340        350        360 
YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGSCAAI MGFILAHKAR KLVRLTKEER 

       370        380        390        400        410        420 
LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTA YFPPGILTQY GRVLRQPVGK 

       430        440        450        460        470        480 
IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESV DVPARPITNT 

       490        500        510        520 
FLERHLPSVP GLLKLLGLTT ILSATALGFL AHKKGLFVRF 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ILE-199.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23601 mRNA. Translation: AAA41566.1.
BC089814 mRNA. Translation: AAH89814.1.
PIRA31870.
RefSeqNP_037330.1. NM_013198.1.
UniGeneRn.6656.

3D structure databases

ProteinModelPortalP19643.
SMRP19643. Positions 3-501.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP19643.
ChEMBLCHEMBL2993.

Proteomic databases

PaxDbP19643.
PRIDEP19643.

Protocols and materials databases

DNASU25750.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25750.
KEGGrno:25750.
UCSCRGD:3041. rat.

Organism-specific databases

CTD4129.
RGD3041. Maob.

Phylogenomic databases

eggNOGCOG1231.
HOGENOMHOG000221615.
HOVERGENHBG004255.
InParanoidP19643.
KOK00274.
PhylomeDBP19643.

Enzyme and pathway databases

BRENDA1.4.3.4. 5301.
SABIO-RKP19643.

Gene expression databases

GenevestigatorP19643.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Other

NextBio607939.
PROP19643.

Entry information

Entry nameAOFB_RAT
AccessionPrimary (citable) accession number: P19643
Secondary accession number(s): Q5EBB5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families