[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/S0006-291X(88)80969-0; PubMed=2974701 [NCBI, ExPASy, EBI, Israel, Japan] Ito A., Kuwahara T., Inadome S., Sagara Y.; "Molecular cloning of a cDNA for rat liver monoamine oxidase B."; Biochem. Biophys. Res. Commun. 157:970-976(1988).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; 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).
[3]	MUTAGENESIS OF ILE-199. 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).

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. MAOB preferentially degrades benzylamine and phenylethylamine.
CATALYTIC ACTIVITY: RCH₂NH₂ + H₂O + O₂ = RCHO + NH₃ + 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

M23601; AAA41566.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC089814; AAH89814.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A31870; A31870.

NP_037330.1; -.

3D structure databases

HSSP

P27338; 1GOS. [HSSP ENTRY / PDB]

SMR

P19643; 3-501.

ModBase

P19643.

Organism-specific databases

RGD

3041; Maob.

Gene expression databases

ArrayExpress

P19643; -.

GermOnline

ENSRNOG00000029778; Rattus norvegicus.

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.

BLOCKS

P19643.

Genome annotation databases

Ensembl

ENSRNOG00000029778; Rattus norvegicus. [Contig view]

GeneID

25750; -.

KEGG

rno:25750; -.

Phylogenomic databases

HOVERGEN

P19643; -.

Other

ProtoNet

P19643.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 520`	`519`	`Amine oxidase [flavin-containing] B.`	`PRO_0000099863`
`TOPO_DOM`	`2 489`	`488`	`Cytoplasmic (By similarity).`
`TRANSMEM`	`490 516`	`27`	`Anchor for type IV membrane protein (By similarity).`
`TOPO_DOM`	`517 520`	`4`	`Mitochondrial intermembrane (By similarity).`
`COMPBIAS`	`36 52`	`17`	`Arg/Lys-rich (basic).`
`SITE`	`156 156`	`1`	`Important for catalytic activity (By similarity).`
`SITE`	`365 365`	`1`	`Important for catalytic activity (By similarity).`
`SITE`	`382 382`	`1`	`Important for catalytic activity (By similarity).`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`MOD_RES`	`52 52`		`N6-acetyllysine (By similarity).`
`MOD_RES`	`397 397`		`S-8alpha-FAD cysteine (By similarity).`
`MUTAGEN`	`139 139`		`L->H: No change in substrate affinity.`
`MUTAGEN`	`199 199`		`I->F: Increased affinity for serotonin and tyramine.`
`CONFLICT`	`38 38`		`R -> C (in Ref. 1; AAA41566).`
`CONFLICT`	`335 336`		`GS -> AG (in Ref. 1; AAA41566).`

Sequence information

Length: 520 AA [This is the length of the unprocessed precursor]

Molecular weight: 58459 Da [This is the MW of the unprocessed precursor]

CRC64: F2C230BC6CDE5840 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNKCDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN VKYVDLGGSY 

        70         80         90        100        110        120 
VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR GPFPPVWNPI TYLDYNNLWR 

       130        140        150        160        170        180 
TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE LLDKICWTNS TKQIATLFVN LCVTAETHEV 

       190        200        210        220        230        240 
SALWFLWYVK QCGGTTRIIS TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ 

       250        260        270        280        290        300 
TGENVVVKTL NHEIYEAKYV ISAIPPVLGM KIHHSPPLPI LRNQLITRVP LGSVIKCMVY 

       310        320        330        340        350        360 
YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGSCAAI MGFILAHKAR KLVRLTKEER 

       370        380        390        400        410        420 
LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTA YFPPGILTQY GRVLRQPVGK 

       430        440        450        460        470        480 
IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESV DVPARPITNT 

       490        500        510        520 
FLERHLPSVP GLLKLLGLTT ILSATALGFL AHKKGLFVRF

P19643 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