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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)DescriptionActionsGraphical viewLength
Sitei335Important for substrate specificity1
Sitei374Important for catalytic activityBy similarity1

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: RGD
  • primary amine oxidase activity Source: RGD
  • serotonin binding Source: RGD

GO - Biological processi

  • catecholamine catabolic process Source: RGD
  • neurotransmitter catabolic process Source: UniProtKB-KW
  • phenylethylamine metabolic process Source: RGD
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61898. Maoa.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 497CytoplasmicAdd BLAST497
Transmembranei498 – 518Helical; Anchor for type IV membrane proteinAdd BLAST21
Topological domaini519 – 526Mitochondrial intermembrane8

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi208F → A: Lower affinity for serotonin and tyramine; no change for tryptamine. 1 Publication1
Mutagenesisi208F → I: Lower affinity for serotonin and tyramine; no change for tryptamine. 1 Publication1
Mutagenesisi208F → V: Lower affinity for serotonin and tyramine; no change for tryptamine. 1 Publication1
Mutagenesisi208F → Y: No change in substrate affinity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3358.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000998541 – 526Amine oxidase [flavin-containing] AAdd BLAST526

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei383PhosphoserineCombined sources1
Modified residuei406S-8alpha-FAD cysteine1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP21396.
PRIDEiP21396.

PTM databases

iPTMnetiP21396.
PhosphoSitePlusiP21396.

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063784.

Chemistry databases

BindingDBiP21396.

Structurei

Secondary structure

1526
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 19Combined sources7
Helixi23 – 34Combined sources12
Beta strandi39 – 42Combined sources4
Beta strandi44 – 48Combined sources5
Turni58 – 60Combined sources3
Beta strandi63 – 66Combined sources4
Helixi75 – 83Combined sources9
Beta strandi88 – 90Combined sources3
Beta strandi94 – 103Combined sources10
Beta strandi105 – 108Combined sources4
Beta strandi110 – 112Combined sources3
Helixi118 – 136Combined sources19
Helixi143 – 145Combined sources3
Helixi149 – 152Combined sources4
Helixi157 – 164Combined sources8
Helixi168 – 182Combined sources15
Turni186 – 188Combined sources3
Helixi191 – 200Combined sources10
Helixi203 – 208Combined sources6
Beta strandi210 – 213Combined sources4
Beta strandi216 – 219Combined sources4
Helixi225 – 232Combined sources8
Helixi235 – 237Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi244 – 248Combined sources5
Beta strandi250 – 261Combined sources12
Beta strandi263 – 271Combined sources9
Helixi275 – 280Combined sources6
Beta strandi281 – 285Combined sources5
Helixi289 – 294Combined sources6
Beta strandi303 – 309Combined sources7
Helixi316 – 318Combined sources3
Beta strandi320 – 327Combined sources8
Beta strandi334 – 338Combined sources5
Beta strandi348 – 354Combined sources7
Helixi355 – 362Combined sources8
Helixi366 – 381Combined sources16
Helixi384 – 387Combined sources4
Beta strandi390 – 396Combined sources7
Turni397 – 399Combined sources3
Turni401 – 403Combined sources3
Beta strandi405 – 407Combined sources3
Turni413 – 415Combined sources3
Helixi416 – 419Combined sources4
Helixi420 – 422Combined sources3
Beta strandi428 – 432Combined sources5
Helixi435 – 437Combined sources3
Beta strandi439 – 441Combined sources3
Helixi445 – 461Combined sources17
Turni462 – 464Combined sources3
Beta strandi479 – 481Combined sources3
Helixi490 – 494Combined sources5
Helixi498 – 519Combined sources22

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP21396.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni520 – 522Interaction with membrane phospholipid headgroupsBy similarity3

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0029. Eukaryota.
ENOG410XSNC. LUCA.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21396.
PhylomeDBiP21396.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.

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)DescriptionActionsGraphical viewLength
Sequence conflicti17 – 18GL → VV in AAB23355 (PubMed:1526120).Curated2
Sequence conflicti361Q → L in AAB23355 (PubMed:1526120).Curated1
Sequence conflicti406C → S in AAB23355 (PubMed:1526120).Curated1
Sequence conflicti451A → R in AAB23355 (PubMed:1526120).Curated1

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

Web resourcesi

Protein Spotlight

Approaching happiness - Issue 172 of August 2015

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O5WX-ray3.20A/B/C/D1-526[»]
ProteinModelPortaliP21396.
SMRiP21396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000063784.

Chemistry databases

BindingDBiP21396.
ChEMBLiCHEMBL3358.

PTM databases

iPTMnetiP21396.
PhosphoSitePlusiP21396.

Proteomic databases

PaxDbiP21396.
PRIDEiP21396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:61898. rat.

Organism-specific databases

RGDi61898. Maoa.

Phylogenomic databases

eggNOGiKOG0029. Eukaryota.
ENOG410XSNC. LUCA.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP21396.
PhylomeDBiP21396.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP21396.
PROiP21396.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

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: November 2, 2016
This is version 126 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.