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Q8BW75 (AOFB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.

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 side By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Ontologies

Keywords
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainTransmembrane
Transmembrane helix
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of serotonin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

response to aluminum ion

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial inner membrane

Inferred from direct assay PubMed 12865426. Source: MGI

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: Ensembl

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 520519Amine oxidase [flavin-containing] B
PRO_0000099860

Regions

Topological domain2 – 489488Cytoplasmic By similarity
Transmembrane490 – 51627Helical; Anchor for type IV membrane protein; By similarity
Topological domain517 – 5204Mitochondrial intermembrane By similarity
Compositional bias36 – 5217Arg/Lys-rich (basic)

Sites

Site1561Important for catalytic activity By similarity
Site3651Important for catalytic activity By similarity
Site3821Important for catalytic activity By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue521N6-acetyllysine Ref.5
Modified residue2481N6-acetyllysine Ref.5
Modified residue3971S-8alpha-FAD cysteine By similarity

Experimental info

Sequence conflict4081T → S in BAC35634. Ref.1
Sequence conflict4821L → M in BAC27571. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BW75 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: A5982EBBF5C4BD62

FASTA52058,558
        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 YFPPGILTQY GRVLRQPVGK 

       430        440        450        460        470        480 
IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESL DVPARPITST 

       490        500        510        520 
FLERHLPSVP GLLKLFGLTT ILSATALGFL AHKRGLFVHF 

« Hide

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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Medulla oblongata and Oviduct.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-52 AND LYS-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK031833 mRNA. Translation: BAC27571.1.
AK054050 mRNA. Translation: BAC35634.1.
AL732321, AL831729 Genomic DNA. Translation: CAM16088.1.
AL831729, AL732321 Genomic DNA. Translation: CAM26633.1.
CH466584 Genomic DNA. Translation: EDL35718.1.
BC113182 mRNA. Translation: AAI13183.1.
BC113788 mRNA. Translation: AAI13789.1.
RefSeqNP_766366.2. NM_172778.2.
UniGeneMm.241656.

3D structure databases

ProteinModelPortalQ8BW75.
SMRQ8BW75. Positions 3-495.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BW75. 2 interactions.
MINTMINT-1861050.

Chemistry

BindingDBQ8BW75.
ChEMBLCHEMBL3050.

PTM databases

PhosphoSiteQ8BW75.

Proteomic databases

PaxDbQ8BW75.
PRIDEQ8BW75.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040820; ENSMUSP00000040550; ENSMUSG00000040147.
GeneID109731.
KEGGmmu:109731.
UCSCuc009ssb.2. mouse.

Organism-specific databases

CTD4129.
MGIMGI:96916. Maob.

Phylogenomic databases

eggNOGCOG1231.
GeneTreeENSGT00730000110903.
HOGENOMHOG000221615.
HOVERGENHBG004255.
InParanoidQ14CG9.
KOK00274.
OMALHQRMPS.
OrthoDBEOG7K6PTP.
TreeFamTF313314.

Enzyme and pathway databases

BRENDA1.4.3.4. 3474.

Gene expression databases

ArrayExpressQ8BW75.
BgeeQ8BW75.
CleanExMM_MAOB.
GenevestigatorQ8BW75.

Family and domain databases

InterProIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

Other

NextBio362651.
PROQ8BW75.
SOURCESearch...

Entry information

Entry nameAOFB_MOUSE
AccessionPrimary (citable) accession number: Q8BW75
Secondary accession number(s): Q14CG9, Q8C0B2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 89 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot