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Protein

Amine oxidase [flavin-containing] A

Gene

Maoa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

FAD1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei335 – 3351Important for substrate specificity
Sitei374 – 3741Important for catalytic activityBy similarity

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: RGD
  2. primary amine oxidase activity Source: RGD
  3. serotonin binding Source: RGD

GO - Biological processi

  1. catecholamine catabolic process Source: RGD
  2. neurotransmitter catabolic process Source: UniProtKB-KW
  3. phenylethylamine metabolic process Source: RGD
  4. serotonin metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Catecholamine metabolism, Neurotransmitter degradation

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14994.
BRENDAi1.4.3.4. 5301.
SABIO-RKP21396.

Names & Taxonomyi

Protein namesi
Recommended name:
Amine oxidase [flavin-containing] A (EC:1.4.3.4)
Alternative name(s):
Monoamine oxidase type A
Short name:
MAO-A
Gene namesi
Name:Maoa
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61898. Maoa.

Subcellular locationi

  1. Mitochondrion outer membrane 1 Publication; Single-pass type IV membrane protein 1 Publication; Cytoplasmic side 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 497497CytoplasmicAdd
BLAST
Transmembranei498 – 51821Helical; Anchor for type IV membrane proteinAdd
BLAST
Topological domaini519 – 5268Mitochondrial intermembrane

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi208 – 2081F → A: Lower affinity for serotonin and tyramine; no change for tryptamine. 1 Publication
Mutagenesisi208 – 2081F → I: Lower affinity for serotonin and tyramine; no change for tryptamine. 1 Publication
Mutagenesisi208 – 2081F → V: Lower affinity for serotonin and tyramine; no change for tryptamine. 1 Publication
Mutagenesisi208 – 2081F → Y: No change in substrate affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 526526Amine oxidase [flavin-containing] APRO_0000099854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei406 – 4061S-8alpha-FAD cysteine

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP21396.
PRIDEiP21396.

PTM databases

PhosphoSiteiP21396.

Expressioni

Gene expression databases

GenevestigatoriP21396.

Interactioni

Subunit structurei

Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity).By similarity

Structurei

Secondary structure

1
526
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 197Combined sources
Helixi23 – 3412Combined sources
Beta strandi39 – 424Combined sources
Beta strandi44 – 485Combined sources
Turni58 – 603Combined sources
Beta strandi63 – 664Combined sources
Helixi75 – 839Combined sources
Beta strandi88 – 903Combined sources
Beta strandi94 – 10310Combined sources
Beta strandi105 – 1084Combined sources
Beta strandi110 – 1123Combined sources
Helixi118 – 13619Combined sources
Helixi143 – 1453Combined sources
Helixi149 – 1524Combined sources
Helixi157 – 1648Combined sources
Helixi168 – 18215Combined sources
Turni186 – 1883Combined sources
Helixi191 – 20010Combined sources
Helixi203 – 2086Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi216 – 2194Combined sources
Helixi225 – 2328Combined sources
Helixi235 – 2373Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi244 – 2485Combined sources
Beta strandi250 – 26112Combined sources
Beta strandi263 – 2719Combined sources
Helixi275 – 2806Combined sources
Beta strandi281 – 2855Combined sources
Helixi289 – 2946Combined sources
Beta strandi303 – 3097Combined sources
Helixi316 – 3183Combined sources
Beta strandi320 – 3278Combined sources
Beta strandi334 – 3385Combined sources
Beta strandi348 – 3547Combined sources
Helixi355 – 3628Combined sources
Helixi366 – 38116Combined sources
Helixi384 – 3874Combined sources
Beta strandi390 – 3967Combined sources
Turni397 – 3993Combined sources
Turni401 – 4033Combined sources
Beta strandi405 – 4073Combined sources
Turni413 – 4153Combined sources
Helixi416 – 4194Combined sources
Helixi420 – 4223Combined sources
Beta strandi428 – 4325Combined sources
Helixi435 – 4373Combined sources
Beta strandi439 – 4413Combined sources
Helixi445 – 46117Combined sources
Turni462 – 4643Combined sources
Beta strandi479 – 4813Combined sources
Helixi490 – 4945Combined sources
Helixi498 – 51922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O5WX-ray3.20A/B/C/D1-526[»]
ProteinModelPortaliP21396.
SMRiP21396. Positions 10-521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21396.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni520 – 5223Interaction with membrane phospholipid headgroupsBy similarity

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21396.
PhylomeDBiP21396.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

P21396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDLEKPNLA GHMFDVGLIG GGISGLAAAK LLSEYKINVL VLEARDRVGG
60 70 80 90 100
RTYTVRNEHV KWVDVGGAYV GPTQNRILRL SKELGIETYK VNVNERLVQY
110 120 130 140 150
VKGKTYPFRG AFPPVWNPLA YLDYNNLWRT MDEMGKEIPV DAPWQARHAQ
160 170 180 190 200
EWDKMTMKDL IDKICWTKTA REFAYLFVNI NVTSEPHEVS ALWFLWYVRQ
210 220 230 240 250
CGGTARIFSV TNGGQERKFV GGSGQVSEQI MGLLGDKVKL SSPVTYIDQT
260 270 280 290 300
DDNIIVETLN HEHYECKYVI SAIPPILTAK IHFKPELPPE RNQLIQRLPM
310 320 330 340 350
GAVIKCMVYY KEAFWKKKDY CGCMIIEDEE APIAITLDDT KPDGSLPAIM
360 370 380 390 400
GFILARKADR QAKLHKDIRK RKICELYAKV LGSQEALYPV HYEEKNWCEE
410 420 430 440 450
QYSGGCYTAY FPPGIMTQYG RVIRQPVGRI YFAGTETATQ WSGYMEGAVE
460 470 480 490 500
AGERAAREVL NALGKVAKKD IWVEEPESKD VPAIEITHTF LERNLPSVPG
510 520
LLKITGVSTS VALLCFVLYK IKKLPC
Length:526
Mass (Da):59,508
Last modified:May 1, 1991 - v1
Checksum:i381AE35D5A73E25B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 182GL → VV in AAB23355 (PubMed:1526120).Curated
Sequence conflicti361 – 3611Q → L in AAB23355 (PubMed:1526120).Curated
Sequence conflicti406 – 4061C → S in AAB23355 (PubMed:1526120).Curated
Sequence conflicti451 – 4511A → R in AAB23355 (PubMed:1526120).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00688 mRNA. Translation: BAA00592.1.
S45812 mRNA. Translation: AAB23355.2.
PIRiJT0528.
UniGeneiRn.224544.

Genome annotation databases

UCSCiRGD:61898. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00688 mRNA. Translation: BAA00592.1.
S45812 mRNA. Translation: AAB23355.2.
PIRiJT0528.
UniGeneiRn.224544.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O5WX-ray3.20A/B/C/D1-526[»]
ProteinModelPortaliP21396.
SMRiP21396. Positions 10-521.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP21396.
ChEMBLiCHEMBL2095196.

PTM databases

PhosphoSiteiP21396.

Proteomic databases

PaxDbiP21396.
PRIDEiP21396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:61898. rat.

Organism-specific databases

RGDi61898. Maoa.

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21396.
PhylomeDBiP21396.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14994.
BRENDAi1.4.3.4. 5301.
SABIO-RKP21396.

Miscellaneous databases

EvolutionaryTraceiP21396.
PROiP21396.

Gene expression databases

GenevestigatoriP21396.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiAOFA_RAT
AccessioniPrimary (citable) accession number: P21396
Secondary accession number(s): Q63817
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: March 4, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.