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Amine oxidase [flavin-containing] A (EC 1.4.3.4) (Monoamine oxidase type A) (MAO-A)

 AOFA_HUMAN              Reviewed;         527 AA.
P21397; B4DF46; Q16426;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
30-AUG-2017, entry version 197.
RecName: Full=Amine oxidase [flavin-containing] A;
EC=1.4.3.4;
AltName: Full=Monoamine oxidase type A;
Short=MAO-A;
Name=MAOA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3418353; DOI=10.1111/j.1471-4159.1988.tb03105.x;
Hsu Y.-P.P., Weyler W., Chen S., Sims K.B., Rinehart W.B.,
Utterback M.C., Powell J.F., Breakefield X.O.;
"Structural features of human monoamine oxidase A elucidated from cDNA
and peptide sequences.";
J. Neurochem. 51:1321-1324(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=3387449; DOI=10.1073/pnas.85.13.4934;
Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E.,
Kwan S.W., Seeburg P.H., Shih J.C.;
"cDNA cloning of human liver monoamine oxidase A and B: molecular
basis of differences in enzymatic properties.";
Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1886775; DOI=10.1093/nar/19.16.4537;
Chen Z.-Y., Hotamisligil G.S., Huang J.-K., Wen L., Ezzeddine D.,
Aydin-Muderrisoglu N., Powell J.F., Huang R.H., Breakefield X.O.,
Craig I., Hsu Y.-P.P.;
"Structure of the human gene for monoamine oxidase type A.";
Nucleic Acids Res. 19:4537-4541(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2023912; DOI=10.1073/pnas.88.9.3637;
Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C.;
"Human monoamine oxidase A and B genes exhibit identical exon-intron
organization.";
Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=1432104;
Zhu Q.S., Grimsby J.S., Chen K., Shih J.C.;
"Promoter organization and activity of human monoamine oxidase (MAO) A
and B genes.";
J. Neurosci. 12:4437-4446(1992).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
PubMed=8584674;
Denney R.M.;
"The promoter of the human monoamine oxidase A gene.";
Prog. Brain Res. 106:57-66(1995).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
PubMed=7519662;
Denney R.M., Sharma A., Dave S.K., Waguespack A.;
"A new look at the promoter of the human monoamine oxidase A gene:
mapping transcription initiation sites and capacity to drive
luciferase expression.";
J. Neurochem. 63:843-856(1994).
[11]
PROTEIN SEQUENCE OF 31-45; 62-78; 109-129; 268-288; 298-315; 318-332;
336-352; 372-412; 430-440 AND 458-493.
TISSUE=Placenta;
PubMed=3178846; DOI=10.1016/S0006-291X(88)80861-1;
Chen S.-Y., Weyler W.;
"Partial amino acid sequence analysis of human placenta monoamine
oxidase A and bovine liver monoamine oxidase B.";
Biochem. Biophys. Res. Commun. 156:445-450(1988).
[12]
DETERMINATION OF PROTEIN-FAD RATIO.
TISSUE=Placenta;
PubMed=2764901; DOI=10.1042/bj2600725;
Weyler W.;
"Monoamine oxidase A from human placenta and monoamine oxidase B from
bovine liver both have one FAD per subunit.";
Biochem. J. 260:725-729(1989).
[13]
PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
PubMed=11812236; DOI=10.1006/prep.2001.1546;
Li M., Hubalek F., Newton-Vinson P., Edmondson D.E.;
"High-level expression of human liver monoamine oxidase A in Pichia
pastoris: comparison with the enzyme expressed in Saccharomyces
cerevisiae.";
Protein Expr. Purif. 24:152-162(2002).
[14]
MUTAGENESIS OF CYS-165; CYS-266; CYS-306; CYS-321; CYS-323; CYS-374;
CYS-398 AND CYS-406.
PubMed=8316221;
Wu H.F., Chen K., Shih J.C.;
"Site-directed mutagenesis of monoamine oxidase A and B: role of
cysteines.";
Mol. Pharmacol. 43:888-893(1993).
[15]
INVOLVEMENT IN BRNRS.
PubMed=8211186; DOI=10.1126/science.8211186;
Brunner H.G., Nelen M., Breakefield X.O., Ropers H.-H., van Oost B.A.;
"Abnormal behavior associated with a point mutation in the structural
gene for monoamine oxidase A.";
Science 262:578-580(1993).
[16]
POLYMORPHISM IN THE PROMOTER REGION.
PubMed=9799080; DOI=10.1007/s004390050816;
Sabol S.Z., Hu S., Hamer D.;
"A functional polymorphism in the monoamine oxidase A gene promoter.";
Hum. Genet. 103:273-279(1998).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), COFACTOR, AND SUBUNIT.
PubMed=16129825; DOI=10.1073/pnas.0505975102;
De Colibus L., Li M., Binda C., Lustig A., Edmondson D.E., Mattevi A.;
"Three-dimensional structure of human monoamine oxidase A (MAO A):
relation to the structures of rat MAO A and human MAO B.";
Proc. Natl. Acad. Sci. U.S.A. 102:12684-12689(2005).
[19]
X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 12-524 IN COMPLEX WITH FAD
AND THE INHIBITOR HARMINE, COFACTOR, AND TOPOLOGY.
PubMed=18391214; DOI=10.1073/pnas.0710626105;
Son S.-Y., Ma J., Kondou Y., Yoshimura M., Yamashita E., Tsukihara T.;
"Structure of human monoamine oxidase A at 2.2-A resolution: the
control of opening the entry for substrates/inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 105:5739-5744(2008).
[20]
VARIANT [LARGE SCALE ANALYSIS] GLU-15.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[21]
VARIANT LYS-188.
PubMed=21179162; DOI=10.1038/nature09629;
Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T.,
Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A.,
Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J.,
Peltonen L., Virkkunen M., Goldman D.;
"A population-specific HTR2B stop codon predisposes to severe
impulsivity.";
Nature 468:1061-1066(2010).
[22]
VARIANT PHE-266, AND CHARACTERIZATION OF VARIANT PHE-266.
PubMed=24169519; DOI=10.1038/ejhg.2013.243;
Piton A., Poquet H., Redin C., Masurel A., Lauer J., Muller J.,
Thevenon J., Herenger Y., Chancenotte S., Bonnet M., Pinoit J.M.,
Huet F., Thauvin-Robinet C., Jaeger A.S., Le Gras S., Jost B.,
Gerard B., Peoc'h K., Launay J.M., Faivre L., Mandel J.L.;
"20 ans apres: a second mutation in MAOA identified by targeted high-
throughput sequencing in a family with altered behavior and
cognition.";
Eur. J. Hum. Genet. 22:776-783(2014).
-!- 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: RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) +
H(2)O(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:16129825,
ECO:0000269|PubMed:18391214};
-!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
similar size). Each subunit contains a covalently bound flavin.
Enzymatically active as monomer. {ECO:0000269|PubMed:16129825,
ECO:0000269|PubMed:18391214}.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
type IV membrane protein; Cytoplasmic side.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P21397-1; Sequence=Displayed;
Name=2;
IsoId=P21397-2; Sequence=VSP_045173;
-!- TISSUE SPECIFICITY: Heart, liver, duodenum, blood vessels and
kidney.
-!- MASS SPECTROMETRY: Mass=60512; Mass_error=6; Method=Electrospray;
Range=1-527; Evidence={ECO:0000269|PubMed:11812236};
-!- POLYMORPHISM: A polymorphism 1.2 kb upstream of the MAOA coding
sequences consists of a 30-bp repeated sequence present in 3, 3.5,
4, or 5 copies. The polymorphism affect transcriptional activity
of the MAOA gene promoter. Alleles with 3.5 or 4 copies of the
repeat sequence are transcribed 2 to 10 times more efficiently
than those with 3 or 5 copies of the repeat.
-!- DISEASE: Brunner syndrome (BRNRS) [MIM:300615]: A form of X-linked
non-dysmorphic mild mental retardation. Male patients are affected
by borderline mental retardation and exhibit abnormal behavior,
including disturbed regulation of impulsive aggression. Obligate
female carriers have normal intelligence and behavior.
{ECO:0000269|PubMed:8211186}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Monoamine oxidase entry;
URL="https://en.wikipedia.org/wiki/Monoamine_oxidase";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Approaching happiness
- Issue 172 of August 2015;
URL="http://web.expasy.org/spotlight/back_issues/172/";
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EMBL; M69226; AAA59549.1; -; mRNA.
EMBL; M68840; AAA59548.1; -; mRNA.
EMBL; X60806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60817; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X60819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M68857; AAA59547.1; -; Genomic_DNA.
EMBL; M68843; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68844; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68845; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68846; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68847; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68848; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68849; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68850; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68851; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68852; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68853; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68854; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68855; AAA59547.1; JOINED; Genomic_DNA.
EMBL; M68856; AAA59547.1; JOINED; Genomic_DNA.
EMBL; AK293926; BAG57307.1; -; mRNA.
EMBL; AL109855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX530072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX537147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX537148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008064; AAH08064.1; -; mRNA.
EMBL; M89636; AAB46385.1; -; Genomic_DNA.
EMBL; S81371; AAD14361.1; -; Genomic_DNA.
EMBL; S72704; AAD14113.1; -; Genomic_DNA.
CCDS; CCDS14260.1; -. [P21397-1]
CCDS; CCDS59163.1; -. [P21397-2]
PIR; A36175; A36175.
RefSeq; NP_000231.1; NM_000240.3. [P21397-1]
RefSeq; NP_001257387.1; NM_001270458.1. [P21397-2]
UniGene; Hs.183109; -.
PDB; 1H8Q; Model; -; A=14-468.
PDB; 2BXR; X-ray; 3.00 A; A/B=1-527.
PDB; 2BXS; X-ray; 3.15 A; A/B=1-527.
PDB; 2Z5X; X-ray; 2.20 A; A=12-524.
PDB; 2Z5Y; X-ray; 2.17 A; A=12-524.
PDBsum; 1H8Q; -.
PDBsum; 2BXR; -.
PDBsum; 2BXS; -.
PDBsum; 2Z5X; -.
PDBsum; 2Z5Y; -.
ProteinModelPortal; P21397; -.
SMR; P21397; -.
BioGrid; 110301; 5.
IntAct; P21397; 2.
MINT; MINT-4054607; -.
STRING; 9606.ENSP00000340684; -.
BindingDB; P21397; -.
ChEMBL; CHEMBL1951; -.
DrugBank; DB01472; 4-Methoxyamphetamine.
DrugBank; DB07919; 7-METHOXY-1-METHYL-9H-BETA-CARBOLINE.
DrugBank; DB00918; Almotriptan.
DrugBank; DB00182; Amphetamine.
DrugBank; DB01445; Bufotenine.
DrugBank; DB06774; Capsaicin.
DrugBank; DB05205; CX157.
DrugBank; DB07641; DECYL(DIMETHYL)PHOSPHINE OXIDE.
DrugBank; DB00988; Dopamine.
DrugBank; DB01363; Ephedra.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB00614; Furazolidone.
DrugBank; DB01247; Isocarboxazid.
DrugBank; DB00601; Linezolid.
DrugBank; DB01577; Methamphetamine.
DrugBank; DB00805; Minaprine.
DrugBank; DB01442; MMDA.
DrugBank; DB01171; Moclobemide.
DrugBank; DB08804; Nandrolone decanoate.
DrugBank; DB00952; Naratriptan.
DrugBank; DB04820; Nialamide.
DrugBank; DB00184; Nicotine.
DrugBank; DB04821; Nomifensine.
DrugBank; DB06412; Oxymetholone.
DrugBank; DB01626; Pargyline.
DrugBank; DB00780; Phenelzine.
DrugBank; DB00191; Phentermine.
DrugBank; DB00388; Phenylephrine.
DrugBank; DB00397; Phenylpropanolamine.
DrugBank; DB04850; Posizolid.
DrugBank; DB00721; Procaine.
DrugBank; DB01168; Procarbazine.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB00140; Riboflavin.
DrugBank; DB00953; Rizatriptan.
DrugBank; DB06654; Safinamide.
DrugBank; DB01037; Selegiline.
DrugBank; DB01104; Sertraline.
DrugBank; DB00669; Sumatriptan.
DrugBank; DB00624; Testosterone.
DrugBank; DB00752; Tranylcypromine.
DrugBank; DB04832; Zimelidine.
DrugBank; DB00315; Zolmitriptan.
DrugBank; DB00909; Zonisamide.
GuidetoPHARMACOLOGY; 2489; -.
iPTMnet; P21397; -.
PhosphoSitePlus; P21397; -.
SwissPalm; P21397; -.
BioMuta; MAOA; -.
DMDM; 113978; -.
EPD; P21397; -.
PaxDb; P21397; -.
PeptideAtlas; P21397; -.
PRIDE; P21397; -.
DNASU; 4128; -.
Ensembl; ENST00000338702; ENSP00000340684; ENSG00000189221. [P21397-1]
Ensembl; ENST00000542639; ENSP00000440846; ENSG00000189221. [P21397-2]
GeneID; 4128; -.
KEGG; hsa:4128; -.
UCSC; uc011mkw.3; human. [P21397-1]
CTD; 4128; -.
DisGeNET; 4128; -.
GeneCards; MAOA; -.
HGNC; HGNC:6833; MAOA.
HPA; CAB009437; -.
HPA; HPA054807; -.
HPA; HPA059299; -.
MalaCards; MAOA; -.
MIM; 300615; phenotype.
MIM; 309850; gene.
neXtProt; NX_P21397; -.
OpenTargets; ENSG00000189221; -.
Orphanet; 3057; Monoamine oxidase A deficiency.
PharmGKB; PA236; -.
eggNOG; KOG0029; Eukaryota.
eggNOG; ENOG410XSNC; LUCA.
GeneTree; ENSGT00730000110903; -.
HOGENOM; HOG000221615; -.
HOVERGEN; HBG004255; -.
InParanoid; P21397; -.
KO; K00274; -.
OMA; EWTRGAY; -.
OrthoDB; EOG091G0G7P; -.
PhylomeDB; P21397; -.
TreeFam; TF313314; -.
BioCyc; MetaCyc:HS01798-MONOMER; -.
BRENDA; 1.4.3.4; 2681.
Reactome; R-HSA-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-HSA-379397; Enzymatic degradation of dopamine by COMT.
Reactome; R-HSA-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
Reactome; R-HSA-380612; Metabolism of serotonin.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SABIO-RK; P21397; -.
ChiTaRS; MAOA; human.
EvolutionaryTrace; P21397; -.
GeneWiki; Monoamine_oxidase_A; -.
GenomeRNAi; 4128; -.
PRO; PR:P21397; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000189221; -.
CleanEx; HS_MAOA; -.
ExpressionAtlas; P21397; baseline and differential.
Genevisible; P21397; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0008131; F:primary amine oxidase activity; TAS:Reactome.
GO; GO:0006576; P:cellular biogenic amine metabolic process; TAS:ProtInc.
GO; GO:0042420; P:dopamine catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
GO; GO:0042133; P:neurotransmitter metabolic process; TAS:Reactome.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR002937; Amino_oxidase.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR001613; Flavin_amine_oxidase.
Pfam; PF01593; Amino_oxidase; 1.
PRINTS; PR00757; AMINEOXDASEF.
SUPFAM; SSF51905; SSF51905; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Catecholamine metabolism; Complete proteome;
Direct protein sequencing; Disease mutation; FAD; Flavoprotein;
Membrane; Mental retardation; Mitochondrion;
Mitochondrion outer membrane; Neurotransmitter degradation;
Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 527 Amine oxidase [flavin-containing] A.
/FTId=PRO_0000099850.
TOPO_DOM 1 497 Cytoplasmic.
{ECO:0000269|PubMed:18391214}.
TRANSMEM 498 518 Helical; Anchor for type IV membrane
protein.
TOPO_DOM 519 527 Mitochondrial intermembrane.
{ECO:0000269|PubMed:18391214}.
REGION 520 522 Interaction with membrane phospholipid
headgroups. {ECO:0000305}.
SITE 335 335 Important for substrate specificity.
{ECO:0000250}.
SITE 374 374 Important for catalytic activity.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:11812236}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000250|UniProtKB:P21396}.
MOD_RES 406 406 S-8alpha-FAD cysteine.
VAR_SEQ 1 133 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045173.
VARIANT 15 15 D -> E (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036545.
VARIANT 188 188 E -> K (in dbSNP:rs77698881).
{ECO:0000269|PubMed:21179162}.
/FTId=VAR_064573.
VARIANT 266 266 C -> F (probable disease-associated
mutation found in a family with Brunner
syndrome-like behavioral disturbances;
reduced activity; dbSNP:rs587777457).
{ECO:0000269|PubMed:24169519}.
/FTId=VAR_071963.
VARIANT 314 314 F -> V (in dbSNP:rs1799835).
/FTId=VAR_014795.
VARIANT 520 520 K -> R (in dbSNP:rs1800466).
/FTId=VAR_014796.
MUTAGEN 165 165 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 266 266 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 306 306 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 321 321 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 323 323 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 374 374 C->S: Complete loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 398 398 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 406 406 C->S: Complete loss of activity.
{ECO:0000269|PubMed:8316221}.
CONFLICT 397 397 W -> M (in Ref. 11; AA sequence).
{ECO:0000305}.
STRAND 15 19 {ECO:0000244|PDB:2Z5Y}.
HELIX 23 34 {ECO:0000244|PDB:2Z5Y}.
STRAND 39 42 {ECO:0000244|PDB:2Z5Y}.
STRAND 44 49 {ECO:0000244|PDB:2Z5Y}.
STRAND 54 57 {ECO:0000244|PDB:2Z5X}.
TURN 58 60 {ECO:0000244|PDB:2Z5Y}.
STRAND 61 66 {ECO:0000244|PDB:2Z5Y}.
HELIX 75 83 {ECO:0000244|PDB:2Z5Y}.
STRAND 88 90 {ECO:0000244|PDB:2Z5Y}.
STRAND 94 101 {ECO:0000244|PDB:2Z5Y}.
STRAND 104 108 {ECO:0000244|PDB:2Z5Y}.
STRAND 110 112 {ECO:0000244|PDB:2Z5Y}.
HELIX 118 136 {ECO:0000244|PDB:2Z5Y}.
HELIX 143 145 {ECO:0000244|PDB:2Z5Y}.
HELIX 149 154 {ECO:0000244|PDB:2Z5Y}.
HELIX 157 164 {ECO:0000244|PDB:2Z5Y}.
HELIX 168 182 {ECO:0000244|PDB:2Z5Y}.
TURN 186 188 {ECO:0000244|PDB:2Z5Y}.
HELIX 191 199 {ECO:0000244|PDB:2Z5Y}.
TURN 200 202 {ECO:0000244|PDB:2Z5Y}.
HELIX 204 208 {ECO:0000244|PDB:2Z5Y}.
STRAND 211 213 {ECO:0000244|PDB:2BXS}.
STRAND 216 219 {ECO:0000244|PDB:2Z5Y}.
HELIX 224 234 {ECO:0000244|PDB:2Z5Y}.
HELIX 235 237 {ECO:0000244|PDB:2Z5Y}.
STRAND 238 241 {ECO:0000244|PDB:2Z5Y}.
STRAND 244 248 {ECO:0000244|PDB:2Z5Y}.
STRAND 250 258 {ECO:0000244|PDB:2Z5Y}.
STRAND 263 271 {ECO:0000244|PDB:2Z5Y}.
HELIX 275 278 {ECO:0000244|PDB:2Z5Y}.
STRAND 281 285 {ECO:0000244|PDB:2Z5Y}.
HELIX 289 295 {ECO:0000244|PDB:2Z5Y}.
STRAND 303 309 {ECO:0000244|PDB:2Z5Y}.
HELIX 314 317 {ECO:0000244|PDB:2Z5Y}.
STRAND 320 327 {ECO:0000244|PDB:2Z5Y}.
STRAND 334 338 {ECO:0000244|PDB:2Z5Y}.
STRAND 348 354 {ECO:0000244|PDB:2Z5Y}.
HELIX 355 361 {ECO:0000244|PDB:2Z5Y}.
HELIX 366 381 {ECO:0000244|PDB:2Z5Y}.
HELIX 385 387 {ECO:0000244|PDB:2Z5Y}.
STRAND 390 397 {ECO:0000244|PDB:2Z5Y}.
TURN 401 403 {ECO:0000244|PDB:2Z5Y}.
STRAND 405 407 {ECO:0000244|PDB:2Z5Y}.
HELIX 415 418 {ECO:0000244|PDB:2Z5Y}.
HELIX 420 422 {ECO:0000244|PDB:2Z5Y}.
STRAND 430 432 {ECO:0000244|PDB:2Z5Y}.
HELIX 435 437 {ECO:0000244|PDB:2Z5Y}.
STRAND 439 441 {ECO:0000244|PDB:2Z5Y}.
HELIX 445 462 {ECO:0000244|PDB:2Z5Y}.
STRAND 464 466 {ECO:0000244|PDB:2BXS}.
HELIX 469 471 {ECO:0000244|PDB:2Z5Y}.
STRAND 479 481 {ECO:0000244|PDB:2Z5Y}.
HELIX 490 494 {ECO:0000244|PDB:2Z5Y}.
HELIX 498 520 {ECO:0000244|PDB:2Z5Y}.
SEQUENCE 527 AA; 59682 MW; 4270E346928AE832 CRC64;
MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG RTYTIRNEHV
DYVDVGGAYV GPTQNRILRL SKELGIETYK VNVSERLVQY VKGKTYPFRG AFPPVWNPIA
YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD KWDKMTMKEL IDKICWTKTA RRFAYLFVNI
NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL
NHPVTHVDQS SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM
GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM GFILARKADR
LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG
RVIRQPVGRI FFAGTETATK WSGYMEGAVE AGERAAREVL NGLGKVTEKD IWVQEPESKD
VPAVEITHTF WERNLPSVSG LLKIIGFSTS VTALGFVLYK YKLLPRS


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