Reviewed, UniProtKB/Swiss-Prot Q8BW75 (AOFB_MOUSE)

Names and origin

Protein names

Recommended name:
    Amine oxidase [flavin-containing] B
    EC=1.4.3.4
Alternative name(s):
    Monoamine oxidase type B
      Short name=MAO-B

Gene names

Name:

Maob

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. MAOB preferentially degrades benzylamine and phenylethylamine By similarity.
Catalytic activity	RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + H(2)O(2).
Cofactor	FAD By similarity.
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.
Subcellular location	Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic sideBy similarity.
Sequence similarities	Belongs to the flavin monoamine oxidase family.

Ontologies

Keywords
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Acetylation
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from direct assay. Source: MGI mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amine oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 520	519	Amine oxidase [flavin-containing] B		PRO_0000099860
Regions
	Topological domain	2 – 489	488	Cytoplasmic By similarity
	Transmembrane	490 – 516	27	Anchor for type IV membrane protein By similarity
	Topological domain	517 – 520	4	Mitochondrial intermembrane By similarity
	Compositional bias	36 – 52	17	Arg/Lys-rich (basic)
Sites
	Site	156	1	Important for catalytic activity By similarity
	Site	365	1	Important for catalytic activity By similarity
	Site	382	1	Important for catalytic activity By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	52	1	N6-acetyllysine
	Modified residue	397	1	S-8alpha-FAD cysteine By similarity
Experimental info
	Sequence conflict	408	1	S → T in BAC27571. Ref.1
	Sequence conflict	482	1	L → M in BAC27571. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BW75-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: D7CD7EBBF5C4B837	FASTA	520	58,544
	10 20 30 40 50 60 MSNKSDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN VKYVDLGGSY 70 80 90 100 110 120 VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR GPFPPVWNPI TYLDNNNLWR 130 140 150 160 170 180 TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE LLDKICWTKS TKQIATLFVN LCVTAETHEV 190 200 210 220 230 240 SALWFLWYVK QCGGTTRIIS TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ 250 260 270 280 290 300 TGENVIVKTL NHEIYEAKYV ISAIPPALGM KIHYSPPLPM LRNQLISRVP LGSVIKCMVY 310 320 330 340 350 360 YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGTYAAI MGFILAHKAR KLVRLTKEER 370 380 390 400 410 420 LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTT YFPPGILSQY GRVLRQPVGK 430 440 450 460 470 480 IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESL DVPARPITST 490 500 510 520 FLERHLPSVP GLLKLFGLTT ILSATALGFL AHKRGLFVHF

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Medulla oblongata and Oviduct.
[2]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK031833 mRNA. Translation: BAC27571.1. AK054050 mRNA. Translation: BAC35634.1.
RefSeq	NP_766366.1.
UniGene	Mm.465301
3D structure databases
HSSP	HSSP built from PDB template 1GOS based on UniProtKB P27338.
SMR	Q8BW75. Positions 2-500, 3-501.
ModBase	Search...
PTM databases
PhosphoSite	Q8BW75.
Genome annotation databases
Ensembl	ENSMUSG00000040147. Mus musculus. [Contig view]
GeneID	109731.
KEGG	mmu:109731.
Organism-specific databases
MGI	MGI:96916. Maob.
Phylogenomic databases
HOGENOM	Q8BW75.
HOVERGEN	Q8BW75.
Gene expression databases
ArrayExpress	Q8BW75.
CleanEx	MM_MAOB.
GermOnline	ENSMUSG00000040147. Mus musculus.
Family and domain databases
InterPro	IPR001613. Amineoxid_fl. IPR002937. Amino_oxidase. [Graphical view]
Pfam	PF01593. Amino_oxidase. 1 hit. [Graphical view]
PRINTS	PR00757. AMINEOXDASEF.
ProtoNet	Search...
Other Resources
NextBio	362651.
SOURCE	Search...

Entry information

Entry name

AOFB_MOUSE

Accession

Primary (citable) accession number: Q8BW75
Secondary accession number(s): Q8C0B2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2004
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 43 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)