Amine oxidase [flavin-containing] - Danio rerio (Zebrafish)

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Q6NSN2 (AOF_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Amine oxidase [flavin-containing]
EC=1.4.3.4

Alternative name(s):
Monoamine oxidase
Short name=MAO
Short name=Z-MAO

Gene names

Name:	mao
ORF Names:	zgc:85761

Organism

Danio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	522 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Oxidizes both 5-hydroxytryptamine (5-HT) and beta-phenylethylamine (PEA). Ref.1 Ref.2 UniProtKB P21397
Catalytic activity	RCH₂NHR' + H₂O + O₂ = RCHO + R'NH₂ + H₂O₂. Ref.1 Ref.2
Cofactor	FAD.
Enzyme regulation	Inhibited by both clorgyline (selective MAOA inhibitor) and deprenyl (selective MAOB inhibitor). Ref.1 Ref.2
Subunit structure	Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer By similarity. UniProtKB P21397
Subcellular location	Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.
Tissue specificity	Strongest expression in brain and intestine, followed by liver, heart and gill. Little expression in spleen, eye or muscle. In brain, highest activity in noradrenergic and serotonergic cell groups and those of the habenulointerpeduncular pathway; moderate levels in dopaminergic cell clusters. Ref.2
Miscellaneous	There appears to be only one form of this enzyme in zebrafish, whereas in mammals two forms (MAOA and MAOB) exist. Ref.1 Ref.2
Sequence similarities	Belongs to the flavin monoamine oxidase family.

Ontologies

Keywords
Biological process	Catecholamine metabolism Neurotransmitter degradation
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW cellular biogenic amine catabolic process Inferred from direct assay Ref.1 Ref.2. Source: UniProtKB neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro primary amine oxidase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 522

522

Amine oxidase [flavin-containing]

PRO_0000283788

Regions

Topological domain

1 – 492

492

Cytoplasmic Potential

Transmembrane

493 – 513

Helical; Anchor for type IV membrane protein; Potential

Topological domain

514 – 522

Mitochondrial intermembrane Potential

Sites

Site

157

Important for catalytic activity By similarity UniProtKB P27338

Site

366

Important for catalytic activity By similarity UniProtKB P27338

Site

383

Important for catalytic activity By similarity UniProtKB P27338

Amino acid modifications

Modified residue

398

S-8alpha-FAD cysteine By similarity UniProtKB P27338

Experimental info

Sequence conflict

223 – 224

AR → QK in AAO16681. Ref.1

Sequence conflict

234

R → K in AAO16681. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q6NSN2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8FC58B2A13BFE15C
Show »

FASTA

522

58,765

        10         20         30         40         50         60 
MTANAYDVIV IGGGISGLSA AKLLVDSGLN PVVLEARSRV GGRTYTVQNK ETKWVDLGGA 

        70         80         90        100        110        120 
YIGPTQNRIL RIAKQYGVKT YKVNEEESLV HYVKGKSYPF KGPFPPMWNP FAYMDYNNLW 

       130        140        150        160        170        180 
RTMDKMGMEI PKEAPWRAPH AEEWDKMTMQ QLFDKICWTR SARRFATLFV NVNVTSEPHE 

       190        200        210        220        230        240 
VSALWFLWYV KQCGGTMRIF STTNGGQERK FAGGANQISE GMARELGDRV KLSRAVCSID 

       250        260        270        280        290        300 
QTGDLVEVRT VNEEVYKAKY VILAIPPGLN LKIHFNPELP PLRNQLIHRV PMGSVIKCMV 

       310        320        330        340        350        360 
YYKENFWRKK GYCGSMVIEE EDAPIGLTLD DTKPDGSVPA IMGFILARKS RKLANLTRDE 

       370        380        390        400        410        420 
RKRRICEIYA RVLGSEEALY PVHYEEKNWC EEEYSGGCYT AYFPPGIMTQ FGRVLREPVG 

       430        440        450        460        470        480 
RLYFAGTETA TEWSGYMEGA VQAGERASRE VMCAMGKLHA SQIWQSEPES MDVPARPFVT 

       490        500        510        520 
TFWERNLPSV GGFLKFMGVS SFLAAATAAG LVACKKGLLP RC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of monoamine oxidase in zebrafish (Danio rerio)." Setini A., Pierucci F., Senatori O., Nicotra A. Comp. Biochem. Physiol. 140B:153-161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, 3D-STRUCTURE MODELING. Tissue: Liver.
[2]	"Distinct structure and activity of monoamine oxidase in the brain of zebrafish (Danio rerio)." Anichtchik O., Sallinen V., Peitsaro N., Panula P. J. Comp. Neurol. 498:593-610(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY. Tissue: Brain.
[3]	NIH - Zebrafish Gene Collection (ZGC) project Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY185211 mRNA. Translation: AAO16681.3. BC070013 mRNA. Translation: AAH70013.1.
IPI	IPI00510954.
RefSeq	NP_997992.2. NM_212827.2.
UniGene	Dr.77508.
3D structure databases
HSSP	HSSP built from PDB template 2BXR based on UniProtKB P21397.
ProteinModelPortal	Q6NSN2.
SMR	Q6NSN2. Positions 6-504.
ModBase	Search...
Protocols and materials databases
DNASU	404730.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSDART00000028225; ENSDARP00000032834; ENSDARG00000023712.
GeneID	404730.
KEGG	dre:404730.
Organism-specific databases
CTD	404730.
ZFIN	ZDB-GENE-040329-3. mao.
Phylogenomic databases
eggNOG	COG1231.
GeneTree	ENSGT00530000063101.
HOGENOM	HOG000221615.
HOVERGEN	HBG004255.
InParanoid	Q6NSN2.
KO	K00274.
OMA	LHQRMPS.
OrthoDB	EOG412M55.
Enzyme and pathway databases
BRENDA	1.4.3.4. 1832.
Gene expression databases
ArrayExpress	Q6NSN2.
Bgee	Q6NSN2.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002937. Amino_oxidase. IPR001613. Flavin_amine_oxidase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00757. AMINEOXDASEF.
ProtoNet	Search...
Other
BindingDB	Q6NSN2.
ChEMBL	CHEMBL1681610.
NextBio	20817705.

Entry information

Entry name

AOF_DANRE

Accession

Primary (citable) accession number: Q6NSN2
Secondary accession number(s): Q804D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents