[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1368522 [NCBI, ExPASy, EBI, Israel, Japan] Kuwahara T., Takamoto S., Ito A.; "Primary structure of rat monoamine oxidase A deduced from cDNA and its expression in rat tissues."; Agric. Biol. Chem. 54:253-257(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 7-526. TISSUE=Liver; PubMed=1526120 [NCBI, ExPASy, EBI, Israel, Japan] Kwan S.W., Abell C.W.; "cDNA cloning and sequencing of rat monoamine oxidase A: comparison with the human and bovine enzymes."; Comp. Biochem. Physiol. 102B:143-147(1992).
[3]	MUTAGENESIS OF PHE-208. DOI=10.1074/jbc.272.22.14033; PubMed=9162023 [NCBI, ExPASy, EBI, Israel, Japan] Tsugeno Y., Ito A.; "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B."; J. Biol. Chem. 272:14033-14036(1997).
[4]	X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH INHIBITOR, SUBUNIT, AND SUBCELLULAR LOCATION. DOI=10.1016/j.jmb.2004.02.032; PubMed=15050826 [NCBI, ExPASy, EBI, Israel, Japan] Ma J., Yoshimura M., Yamashita E., Nakagawa A., Ito A., Tsukihara T.; "Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors."; J. Mol. Biol. 338:103-114(2004).

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.
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

D00688; BAA00592.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S45812; AAB23355.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JT0528; JT0528.

UniGene

Rn.163443

3D structure databases

PDB

1O5W; X-ray; 3.20 A; A/B/C/D=1-526.

[ExPASy / RCSB / EBI]

PDBsum

1O5W; -.

ModBase

P21396.

Organism-specific databases

RGD

61898; Maoa.

Gene expression databases

ArrayExpress

P21396; -.

GermOnline

ENSRNOG00000002848; Rattus norvegicus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0008131;	Molecular function: amine oxidase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0042135;	Biological process: neurotransmitter catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProtoNet

P21396.

Genome annotation databases

Ensembl

ENSRNOG00000002848; Rattus norvegicus. [Contig view]

Phylogenomic databases

HOVERGEN

P21396; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Catecholamine metabolism; FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Neurotransmitter degradation; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 526`	`526`	`Amine oxidase [flavin-containing] A.`	`PRO_0000099854`
`TOPO_DOM`	`1 497`	`497`	`Cytoplasmic (Potential).`
`TRANSMEM`	`498 518`	`21`	`Anchor for type IV membrane protein (Potential).`
`TOPO_DOM`	`519 526`	`8`	`Mitochondrial intermembrane (Potential).`
`SITE`	`335 335`	`1`	`Important for substrate specificity.`
`SITE`	`374 374`	`1`	`Important for catalytic activity (By similarity).`
`MOD_RES`	`406 406`		`S-8alpha-FAD cysteine.`
`MUTAGEN`	`208 208`		`F->A: Lower affinity for serotonin and tyramine; no change for tryptamine.`
`MUTAGEN`	`208 208`		`F->I: Lower affinity for serotonin and tyramine; no change for tryptamine.`
`MUTAGEN`	`208 208`		`F->V: Lower affinity for serotonin and tyramine; no change for tryptamine.`
`MUTAGEN`	`208 208`		`F->Y: No change in substrate affinity.`
`CONFLICT`	`17 18`		`GL -> VV (in Ref. 2; AAB23355).`
`CONFLICT`	`361 361`		`Q -> L (in Ref. 2; AAB23355).`
`CONFLICT`	`406 406`		`C -> S (in Ref. 2; AAB23355).`
`CONFLICT`	`451 451`		`A -> R (in Ref. 2; AAB23355).`
`STRAND`	`13 19`	`7`
`HELIX`	`23 34`	`12`
`STRAND`	`39 42`	`4`
`STRAND`	`44 48`	`5`
`TURN`	`58 60`	`3`
`STRAND`	`63 66`	`4`
`HELIX`	`75 83`	`9`
`STRAND`	`88 90`	`3`
`STRAND`	`94 103`	`10`
`STRAND`	`105 108`	`4`
`STRAND`	`110 112`	`3`
`HELIX`	`118 136`	`19`
`HELIX`	`143 145`	`3`
`HELIX`	`149 152`	`4`
`HELIX`	`157 164`	`8`
`HELIX`	`168 182`	`15`
`TURN`	`186 188`	`3`
`HELIX`	`191 200`	`10`
`HELIX`	`203 208`	`6`
`STRAND`	`210 213`	`4`
`STRAND`	`216 219`	`4`
`HELIX`	`225 232`	`8`
`HELIX`	`235 237`	`3`
`STRAND`	`238 241`	`4`
`STRAND`	`244 248`	`5`
`STRAND`	`250 261`	`12`
`STRAND`	`263 271`	`9`
`HELIX`	`275 280`	`6`
`STRAND`	`281 285`	`5`
`HELIX`	`289 294`	`6`
`STRAND`	`303 309`	`7`
`HELIX`	`316 318`	`3`
`STRAND`	`320 327`	`8`
`STRAND`	`334 338`	`5`
`STRAND`	`348 354`	`7`
`HELIX`	`355 362`	`8`
`HELIX`	`366 381`	`16`
`HELIX`	`384 387`	`4`
`STRAND`	`390 396`	`7`
`TURN`	`397 399`	`3`
`TURN`	`401 403`	`3`
`STRAND`	`405 407`	`3`
`TURN`	`413 415`	`3`
`HELIX`	`416 419`	`4`
`HELIX`	`420 422`	`3`
`STRAND`	`428 432`	`5`
`HELIX`	`435 437`	`3`
`STRAND`	`439 441`	`3`
`HELIX`	`445 461`	`17`
`TURN`	`462 464`	`3`
`STRAND`	`479 481`	`3`
`HELIX`	`490 494`	`5`
`HELIX`	`498 519`	`22`

Sequence information

Length: 526 AA [This is the length of the unprocessed precursor]

Molecular weight: 59508 Da [This is the MW of the unprocessed precursor]

CRC64: 381AE35D5A73E25B [This is a checksum on the sequence]

        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

P21396 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools