Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P21396 (AOFA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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] A

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

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
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. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.

Catalytic activity

RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.

Cofactor

FAD. Ref.4

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. Ref.4

Subcellular location

Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side Ref.4.

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Amine oxidase [flavin-containing] A
PRO_0000099854

Regions

Topological domain1 – 497497Cytoplasmic
Transmembrane498 – 51821Helical; Anchor for type IV membrane protein
Topological domain519 – 5268Mitochondrial intermembrane
Region520 – 5223Interaction with membrane phospholipid headgroups By similarity

Sites

Site3351Important for substrate specificity
Site3741Important for catalytic activity By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue4061S-8alpha-FAD cysteine

Experimental info

Mutagenesis2081F → A: Lower affinity for serotonin and tyramine; no change for tryptamine. Ref.3
Mutagenesis2081F → I: Lower affinity for serotonin and tyramine; no change for tryptamine. Ref.3
Mutagenesis2081F → V: Lower affinity for serotonin and tyramine; no change for tryptamine. Ref.3
Mutagenesis2081F → Y: No change in substrate affinity. Ref.3
Sequence conflict17 – 182GL → VV in AAB23355. Ref.2
Sequence conflict3611Q → L in AAB23355. Ref.2
Sequence conflict4061C → S in AAB23355. Ref.2
Sequence conflict4511A → R in AAB23355. Ref.2

Secondary structure

.................................................................................................... 526
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21396 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 381AE35D5A73E25B

FASTA52659,508
        10         20         30         40         50         60 
MTDLEKPNLA GHMFDVGLIG GGISGLAAAK LLSEYKINVL VLEARDRVGG RTYTVRNEHV 

        70         80         90        100        110        120 
KWVDVGGAYV GPTQNRILRL SKELGIETYK VNVNERLVQY VKGKTYPFRG AFPPVWNPLA 

       130        140        150        160        170        180 
YLDYNNLWRT MDEMGKEIPV DAPWQARHAQ EWDKMTMKDL IDKICWTKTA REFAYLFVNI 

       190        200        210        220        230        240 
NVTSEPHEVS ALWFLWYVRQ CGGTARIFSV TNGGQERKFV GGSGQVSEQI MGLLGDKVKL 

       250        260        270        280        290        300 
SSPVTYIDQT DDNIIVETLN HEHYECKYVI SAIPPILTAK IHFKPELPPE RNQLIQRLPM 

       310        320        330        340        350        360 
GAVIKCMVYY KEAFWKKKDY CGCMIIEDEE APIAITLDDT KPDGSLPAIM GFILARKADR 

       370        380        390        400        410        420 
QAKLHKDIRK RKICELYAKV LGSQEALYPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG 

       430        440        450        460        470        480 
RVIRQPVGRI YFAGTETATQ WSGYMEGAVE AGERAAREVL NALGKVAKKD IWVEEPESKD 

       490        500        510        520 
VPAIEITHTF LERNLPSVPG LLKITGVSTS VALLCFVLYK IKKLPC 

« Hide

References

[1]"Primary structure of rat monoamine oxidase A deduced from cDNA and its expression in rat tissues."
Kuwahara T., Takamoto S., Ito A.
Agric. Biol. Chem. 54:253-257(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"cDNA cloning and sequencing of rat monoamine oxidase A: comparison with the human and bovine enzymes."
Kwan S.W., Abell C.W.
Comp. Biochem. Physiol. 102B:143-147(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-526.
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 PHE-208.
[4]"Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors."
Ma J., Yoshimura M., Yamashita E., Nakagawa A., Ito A., Tsukihara T.
J. Mol. Biol. 338:103-114(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH INHIBITOR, SUBUNIT, COFACTOR, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00688 mRNA. Translation: BAA00592.1.
S45812 mRNA. Translation: AAB23355.2.
PIRJT0528.
UniGeneRn.224544.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1O5WX-ray3.20A/B/C/D1-526[»]
ProteinModelPortalP21396.
SMRP21396. Positions 10-521.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP21396.
ChEMBLCHEMBL2095196.

PTM databases

PhosphoSiteP21396.

Proteomic databases

PaxDbP21396.
PRIDEP21396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:61898. rat.

Organism-specific databases

RGD61898. Maoa.

Phylogenomic databases

eggNOGCOG1231.
HOGENOMHOG000221615.
HOVERGENHBG004255.
InParanoidP21396.
PhylomeDBP21396.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14994.
BRENDA1.4.3.4. 5301.
SABIO-RKP21396.

Gene expression databases

GenevestigatorP21396.

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

EvolutionaryTraceP21396.
PROP21396.

Entry information

Entry nameAOFA_RAT
AccessionPrimary (citable) accession number: P21396
Secondary accession number(s): Q63817
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 114 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references