[1]	NUCLEOTIDE SEQUENCE [MRNA], AND ACTIVITY. TISSUE=Liver; PubMed=7808446 [NCBI, ExPASy, EBI, Israel, Japan] Chen K., Wu H.-F., Grimsby J., Shih J.C.; "Cloning of a novel monoamine oxidase cDNA from trout liver."; Mol. Pharmacol. 46:1226-1233(1994).

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).
CATALYTIC ACTIVITY: RCH₂NHR' + H₂O + O₂ = RCHO + R'NH₂ + H₂O₂.
COFACTOR: FAD.
SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.
SIMILARITY: Belongs to the flavin monoamine oxidase family.
SEQUENCE CAUTION:
- Sequence=AAA64302.1; Type=Frameshift; Positions=500; Note=Probable frameshift identified on the basis of homology with other members of this 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

L37878; AAA64302.1; ALT_FRAME; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I51346; I51346.

RefSeq

NP_001118160.1; -.

3D structure databases

HSSP

P27338; 1GOS. [HSSP ENTRY / PDB]

SMR

P49253; 5-503.

ModBase

P49253.

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: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

P49253.

Genome annotation databases

GeneID

100136729; -.

Phylogenomic databases

HOVERGEN

P49253; -.

Other

UniRef

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

Keywords

FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane; Oxidoreductase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 522`	`522`	`Amine oxidase [flavin-containing].`	`PRO_0000099864`
`TOPO_DOM`	`1 492`	`492`	`Cytoplasmic (By similarity).`
`TRANSMEM`	`493 513`	`21`	`Anchor for type IV membrane protein (By similarity).`
`TOPO_DOM`	`514 522`	`9`	`Mitochondrial intermembrane (By similarity).`
`SITE`	`158 158`	`1`	`Important for catalytic activity (By similarity).`
`SITE`	`367 367`	`1`	`Important for catalytic activity (By similarity).`
`SITE`	`384 384`	`1`	`Important for catalytic activity (By similarity).`
`MOD_RES`	`399 399`		`S-8alpha-FAD cysteine (By similarity).`

Sequence information

Length: 522 AA [This is the length of the unprocessed precursor]

Molecular weight: 58937 Da [This is the MW of the unprocessed precursor]

CRC64: F82D6D15364D646D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAQNTFDVI VIGGGISGLS AAKLLKEKGL SPVVLEARDR VGGRTFTVQN EQTKYVDLGG 

        70         80         90        100        110        120 
AYVGPTQNRI LRLAKECGVK TIKVNEEERL VHYVKGKSYP FKGSFPPMWN PFALMDYNNL 

       130        140        150        160        170        180 
WRKMDEMGSE IPREAPWKAP HAEEWDKMTM KQLFDKICWT SSARRFATLF VNVNVTSEPH 

       190        200        210        220        230        240 
EVSALWFLWY VKQCGGTMRI FSTTNGGQER KFLGGSSQIS ECMAKELGER VKMESPVYKI 

       250        260        270        280        290        300 
DQTGDMVEVE TLNKETYKAK YVIVATPPGL NLKMHFNPEL PPLRNQLIHR VPMGSVIKCI 

       310        320        330        340        350        360 
VYYRENFWRK KGYCGTMVIE EEEAPIGLTL DDTKPDGTVP AIMGFILARK CRKLCGLTKE 

       370        380        390        400        410        420 
ERKKRICEIY SRVLGSEEAL HPVHYEEKNW CEEEYSGGCY TAYFPPGILT QYGKVLREPV 

       430        440        450        460        470        480 
GRLYFAGTET ATEWSGYMEG AVQAGERAAR EVMYEMGRIP QSQIWQTEPE SVEVPALPFV 

       490        500        510        520 
TTFWERNLPS VGGFINFLAA SVLSVATAAG MLAYQKGLLT RS

P49253 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