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UniProtKB/Swiss-Prot entry P21397


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AOFA_HUMAN
Primary accession number P21397
Secondary accession number Q16426
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on May 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 104)
Name and origin of the protein
Protein name Amine oxidase [flavin-containing] A
Synonyms EC 1.4.3.4
Monoamine oxidase type A
MAO-A
Gene name
Name: MAOA
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1111/j.1471-4159.1988.tb03105.x; PubMed=3418353 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Liver;
PubMed=3387449 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1093/nar/19.16.4537; PubMed=1886775 [NCBI, ExPASy, EBI, Israel, Japan]
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 [LARGE SCALE MRNA].
TISSUE=Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
PubMed=1432104 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
PubMed=8584674 [NCBI, ExPASy, EBI, Israel, Japan]
Denney R.M.;
"The promoter of the human monoamine oxidase A gene.";
Prog. Brain Res. 106:57-66(1995).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
PubMed=7519662 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
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;
DOI=10.1016/S0006-291X(88)80861-1; PubMed=3178846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
DETERMINATION OF PROTEIN-FAD RATIO.
TISSUE=Placenta;
PubMed=2764901 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
PARTIAL PROTEIN SEQUENCE, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
DOI=10.1006/prep.2001.1546; PubMed=11812236 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
MUTAGENESIS OF CYS-165; CYS-266; CYS-306; CYS-321; CYS-323; CYS-374; CYS-398 AND CYS-406.
PubMed=8316221 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT.
DOI=10.1073/pnas.0505975102; PubMed=16129825 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
INVOLVEMENT IN BRUNNER SYNDROME.
PubMed=8211186 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
VARIANT [LARGE SCALE ANALYSIS] GLU-15.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
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
M68840; AAA59548.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68857; AAA59547.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68843; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68844; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68845; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68846; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68847; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68848; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68849; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68850; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68851; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68852; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68853; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68854; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68855; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M68856; AAA59547.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M69226; AAA59549.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60806; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60807; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60808; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60809; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60810; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60811; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60812; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60813; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60814; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60815; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60816; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60817; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60818; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
X60819; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC008064; AAH08064.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M89636; AAB46385.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S81371; AAD14361.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S72704; AAD14113.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A36175; A36175.
RefSeq NP_000231.1; -.
UniGene Hs.183109
3D structure databases
PDB
1H8Q; Model; -; A=14-468.[ExPASy / RCSB / EBI]
2BXR; X-ray; 3.00 A; A/B=1-527.[ExPASy / RCSB / EBI]
2BXS; X-ray; 3.15 A; A/B=1-527.[ExPASy / RCSB / EBI]
2Z5X; X-ray; 2.20 A; A=12-524.[ExPASy / RCSB / EBI]
2Z5Y; X-ray; 2.17 A; A=12-524.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1H8Q; -.
2BXR; -.
2BXS; -.
2Z5X; -.
2Z5Y; -.
ModBase P21397.
Protein-protein interaction databases
IntAct P21397; -.
PTM databases
PhosphoSite P21397; -.
Enzyme and pathway databases
BioCyc MetaCyc:ENSG00000094598-MON; -.
Reactome REACT_2063; Metabolism of xenobiotics.
Organism-specific databases
H-InvDB HIX0021483; -.
HGNC HGNC:6833; MAOA.
GenAtlas MAOA.
MIM 300615; phenotype. [NCBI / EBI]
309850; gene+phenotype. [NCBI / EBI]
Orphanet 3065; Mental retardation x linked borderline maoa metabolism anomaly.
3057; Monoamine oxidase-A deficiency.
PharmGKB PA236; -.
GeneCards P21397.
Gene expression databases
ArrayExpress P21397; -.
CleanEx HS_MAOA; -.
GermOnline ENSG00000189221; Homo sapiens.
Ontologies
GO
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:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007610; Biological process: behavior (traceable author statement from ProtInc).
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 P21397.
Proteomic databases
PeptideAtlas P21397; -.
Genome annotation databases
Ensembl ENSG00000189221; Homo sapiens. [Contig view]
GeneID 4128; -.
KEGG hsa:4128; -.
Phylogenomic databases
HOGENOM P21397; -.
HOVERGEN P21397; -.
Other
DrugBank DB00918; Almotriptan.
DB00190; Carbidopa.
DB01068; Clonazepam.
DB00988; Dopamine.
DB00176; Fluvoxamine.
DB01381; Ginkgo biloba.
DB00458; Imipramine.
DB01247; Isocarboxazid.
DB01235; Levodopa.
DB00601; Linezolid.
DB00186; Lorazepam.
DB01171; Moclobemide.
DB00184; Nicotine.
DB00368; Norepinephrine.
DB00780; Phenelzine.
DB00830; Phenmetrazine.
DB00191; Phentermine.
DB00388; Phenylephrine.
DB00397; Phenylpropanolamine.
DB00852; Pseudoephedrine.
DB01367; Rasagiline.
DB00140; Riboflavin.
DB00953; Rizatriptan.
DB01037; Selegiline.
DB00669; Sumatriptan.
DB00624; Testosterone.
DB00752; Tranylcypromine.
DB00315; Zolmitriptan.
NextBio 16206; -.
SOURCE MAOA; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Catecholamine metabolism; Direct protein sequencing; FAD; Flavoprotein; Membrane; Mental retardation; Mitochondrion; Mitochondrion outer membrane; Neurotransmitter degradation; Oxidoreductase; Polymorphism; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   527  527     Amine oxidase [flavin-containing] A. PRO_0000099850
TOPO_DOM   1   497  497     Cytoplasmic (Potential). 
TRANSMEM   498   518  21     Anchor for type IV membrane protein (Potential). 
TOPO_DOM   519   527  9     Mitochondrial intermembrane (Potential). 
SITE   335   335  1     Important for substrate specificity (By similarity). 
SITE   374   374  1     Important for catalytic activity. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   406   406        S-8alpha-FAD cysteine. 
VARIANT   15    15  1     D -> E (in a breast cancer sample; somatic mutation). VAR_036545 [3D]
VARIANT   314   314  1     F -> V (in dbSNP:rs1799835 [NCBI]). VAR_014795 [3D]
VARIANT   520   520  1     K -> R (in dbSNP:rs1800466 [NCBI]). VAR_014796 [3D]
MUTAGEN   165   165        C->S: No loss of activity. 
MUTAGEN   266   266        C->S: No loss of activity. 
MUTAGEN   306   306        C->S: No loss of activity. 
MUTAGEN   321   321        C->S: No loss of activity. 
MUTAGEN   323   323        C->S: No loss of activity. 
MUTAGEN   374   374        C->S: Complete loss of activity. 
MUTAGEN   398   398        C->S: No loss of activity. 
MUTAGEN   406   406        C->S: Complete loss of activity. 
CONFLICT   111   111        Missing (in Ref. 4). 
CONFLICT   138   138        I -> R (in Ref. 4). 
CONFLICT   397   397        W -> M (in Ref. 8; AA sequence). 
STRAND   15    19  5      
HELIX   23    34  12      
STRAND   39    42  4      
STRAND   44    49  6      
STRAND   54    57  4      
TURN   58    60  3      
STRAND   61    66  6      
HELIX   75    83  9      
STRAND   88    90  3      
STRAND   94   101  8      
STRAND   104   108  5      
STRAND   110   112  3      
HELIX   118   136  19      
HELIX   143   145  3      
HELIX   149   154  6      
HELIX   157   164  8      
HELIX   168   182  15      
TURN   186   188  3      
HELIX   191   199  9      
TURN   200   202  3      
HELIX   204   208  5      
STRAND   216   219  4      
HELIX   224   234  11      
HELIX   235   237  3      
STRAND   238   241  4      
STRAND   244   248  5      
STRAND   250   258  9      
STRAND   263   271  9      
HELIX   275   278  4      
STRAND   281   285  5      
HELIX   289   296  8      
STRAND   303   309  7      
HELIX   314   317  4      
STRAND   320   327  8      
STRAND   334   338  5      
STRAND   348   354  7      
HELIX   355   361  7      
HELIX   366   381  16      
HELIX   384   387  4      
STRAND   390   396  7      
HELIX   397   399  3      
TURN   401   403  3      
STRAND   405   407  3      
HELIX   415   419  5      
HELIX   420   422  3      
STRAND   430   432  3      
HELIX   435   437  3      
STRAND   439   441  3      
HELIX   445   462  18      
HELIX   468   470  3      
STRAND   479   481  3      
HELIX   490   494  5      
HELIX   498   520  23      
Sequence information
Length: 527 AA [This is the length of the unprocessed precursor] Molecular weight: 59682 Da [This is the MW of the unprocessed precursor] CRC64: 4270E346928AE832 [This is a checksum on the sequence]