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P58028 (AOFB_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 83. 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
OrganismCavia porcellus (Guinea pig) [Reference proteome]
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

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_0000099858

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

Sequences

Sequence LengthMass (Da)Tools
P58028 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0AEBAE99A48BC206

FASTA52058,410
        10         20         30         40         50         60 
MNSKCDVVVV GGGISGLAAA KLLHDSGLNV VVLEARDCVG GRTYTLRNQN VKYVDLGGAY 

        70         80         90        100        110        120 
VGPTQNRILR LAKELGLETY RVNDVERQIH HVKGKSYPFR GPFPPAWNPI SYLDHNNLWR 

       130        140        150        160        170        180 
TMDDMGKEIP SDAPWKAPLA EEWDHMTMKE LLNKICWTNC PRQFGTLFVN LCFTAETHEV 

       190        200        210        220        230        240 
SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQISER IMNLLGDRVK LQRPVVYIDQ 

       250        260        270        280        290        300 
TGESVLVETL NHEIYEAKYV ISAIPPALGM KIHFKPPLPM MKNQLVSRVP LGSVIKCIVY 

       310        320        330        340        350        360 
YKDPFWRKKD FCGTMVIEGE EAPVLYTMDD TKPDGSYAAI IGFIAAHKAR KLARLTKEER 

       370        380        390        400        410        420 
LKKLCELYAK VLGSKEALKP VHYEEKNWCE EQYSGGCYTA YFPPGIMTQY GRFLRQPVGR 

       430        440        450        460        470        480 
IFFAGTETAT HWSGYMEGAV EAGERAAREV LNAIGKIPED EIWQPEPESV DVPAQPITTT 

       490        500        510        520 
FLERHLPSVP GLLRLIRLTT VVSAVALGFL AQKRGLLLRI 

« Hide

References

[1]"Nucleotide sequences of putative cDNAs for guinea-pig monoamine oxidase."
Yaekashiwa N., Tamate H.B., Takeuchi T., Sugimoto H., Shibata K., Kinemuchi H.
Inflammopharmacology 11:145-154(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain and Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB047271 mRNA. Translation: BAB40418.1.
RefSeqNP_001166452.1. NM_001172981.1.

3D structure databases

ProteinModelPortalP58028.
SMRP58028. Positions 4-496.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10141.ENSCPOP00000000879.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100135573.

Organism-specific databases

CTD4129.

Phylogenomic databases

eggNOGCOG1231.
HOGENOMHOG000221615.
HOVERGENHBG004255.
InParanoidP58028.

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...

Entry information

Entry nameAOFB_CAVPO
AccessionPrimary (citable) accession number: P58028
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 83 of the entry and version 2 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