ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P58028

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AOFB_CAVPO
Primary accession number P58028
Secondary accession numbers None
Integrated into Swiss-Prot on April 27, 2001
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 45)
Name and origin of the protein
Protein name Amine oxidase [flavin-containing] B
Synonyms EC 1.4.3.4
Monoamine oxidase type B
MAO-B
Gene name
Name: MAOB
From
Cavia porcellus (Guinea pig) [TaxID: 10141] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Hystricognathi; Caviidae; Cavia.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain, and Liver;
DOI=10.1163/156856003765764317; PubMed=15035816 [NCBI, ExPASy, EBI, Israel, Japan]
Yaekashiwa N., Tamate H.B., Takeuchi T., Sugimoto H., Shibata K., Kinemuchi H.;
"Nucleotide sequences of putative cDNAs for guinea-pig monoamine oxidase.";
Inflammopharmacology 11:145-154(2003).
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: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
  • COFACTOR: FAD.
  • SUBUNIT: 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.
  • SIMILARITY: Belongs to the flavin monoamine oxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB047271; BAB40418.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
HSSP P27338; 1GOS. [HSSP ENTRY / PDB]
SMR P58028; 3-501.
ModBase P58028.
Family and domain databases
InterPro IPR001613; Amineoxid_fl.
IPR002937; Amino_oxidase.
Graphical view of domain structure.
Pfam PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00757; AMINEOXDASEF.
BLOCKS P58028.
Phylogenomic databases
HOVERGEN P58028; -.
Other
ProtoNet P58028.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   520  519     Amine oxidase [flavin-containing] B. PRO_0000099858
TOPO_DOM   2   489  488     Cytoplasmic (By similarity). 
TRANSMEM   490   516  27     Anchor for type IV membrane protein (By similarity). 
TOPO_DOM   517   520  4     Mitochondrial intermembrane (By similarity). 
COMPBIAS   36    52  17     Arg/Lys-rich (basic). 
SITE   156   156  1     Important for catalytic activity (By similarity). 
SITE   365   365  1     Important for catalytic activity (By similarity). 
SITE   382   382  1     Important for catalytic activity (By similarity). 
MOD_RES   52    52        N6-acetyllysine (By similarity). 
MOD_RES   397   397        S-8alpha-FAD cysteine (By similarity). 
Sequence information
Length: 520 AA [This is the length of the unprocessed precursor] Molecular weight: 58410 Da [This is the MW of the unprocessed precursor] CRC64: 0AEBAE99A48BC206 [This is a checksum on the sequence] 
        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
P58028 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!