Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Amine oxidase [flavin-containing] B

Gene

Maob

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei156 – 1561Important for catalytic activityBy similarity
Sitei365 – 3651Important for catalytic activityBy similarity
Sitei382 – 3821Important for catalytic activityBy similarity

GO - Molecular functioni

  • flavin adenine dinucleotide binding Source: RGD
  • primary amine oxidase activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • negative regulation of serotonin secretion Source: RGD
  • neurotransmitter catabolic process Source: RGD
  • positive regulation of dopamine metabolic process Source: RGD
  • response to aluminum ion Source: RGD
  • response to corticosterone Source: RGD
  • response to drug Source: RGD
  • response to ethanol Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to selenium ion Source: RGD
  • response to steroid hormone Source: RGD
  • response to toxic substance Source: RGD
  • substantia nigra development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.4. 5301.
ReactomeiREACT_344337. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
SABIO-RKP19643.

Names & Taxonomyi

Protein namesi
Recommended name:
Amine oxidase [flavin-containing] B (EC:1.4.3.4)
Alternative name(s):
Monoamine oxidase type B
Short name:
MAO-B
Gene namesi
Name:Maob
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3041. Maob.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 489488CytoplasmicBy similarityAdd
BLAST
Transmembranei490 – 51627Helical; Anchor for type IV membrane proteinBy similarityAdd
BLAST
Topological domaini517 – 5204Mitochondrial intermembraneBy similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi139 – 1391L → H: No change in substrate affinity.
Mutagenesisi199 – 1991I → F: Increased affinity for serotonin and tyramine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 520519Amine oxidase [flavin-containing] BPRO_0000099863Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei397 – 3971S-8alpha-FAD cysteineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP19643.
PRIDEiP19643.

Expressioni

Gene expression databases

ExpressionAtlasiP19643. baseline and differential.
GenevisibleiP19643. RN.

Interactioni

Subunit structurei

Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043466.

Structurei

3D structure databases

ProteinModelPortaliP19643.
SMRiP19643. Positions 3-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 5217Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP19643.
KOiK00274.
PhylomeDBiP19643.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P19643-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKCDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN
60 70 80 90 100
VKYVDLGGSY VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR
110 120 130 140 150
GPFPPVWNPI TYLDYNNLWR TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE
160 170 180 190 200
LLDKICWTNS TKQIATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS
210 220 230 240 250
TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ TGENVVVKTL
260 270 280 290 300
NHEIYEAKYV ISAIPPVLGM KIHHSPPLPI LRNQLITRVP LGSVIKCMVY
310 320 330 340 350
YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGSCAAI MGFILAHKAR
360 370 380 390 400
KLVRLTKEER LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTA
410 420 430 440 450
YFPPGILTQY GRVLRQPVGK IFFAGTETAS HWSGYMEGAV EAGERAAREI
460 470 480 490 500
LHAIGKIPED EIWQPEPESV DVPARPITNT FLERHLPSVP GLLKLLGLTT
510 520
ILSATALGFL AHKKGLFVRF
Length:520
Mass (Da):58,459
Last modified:January 23, 2007 - v3
Checksum:iF2C230BC6CDE5840
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381R → C in AAA41566 (PubMed:2974701).Curated
Sequence conflicti335 – 3362GS → AG in AAA41566 (PubMed:2974701).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23601 mRNA. Translation: AAA41566.1.
BC089814 mRNA. Translation: AAH89814.1.
PIRiA31870.
RefSeqiNP_037330.1. NM_013198.1.
UniGeneiRn.6656.

Genome annotation databases

GeneIDi25750.
KEGGirno:25750.
UCSCiRGD:3041. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23601 mRNA. Translation: AAA41566.1.
BC089814 mRNA. Translation: AAH89814.1.
PIRiA31870.
RefSeqiNP_037330.1. NM_013198.1.
UniGeneiRn.6656.

3D structure databases

ProteinModelPortaliP19643.
SMRiP19643. Positions 3-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000043466.

Chemistry

BindingDBiP19643.
ChEMBLiCHEMBL2095196.
GuidetoPHARMACOLOGYi2490.

Proteomic databases

PaxDbiP19643.
PRIDEiP19643.

Protocols and materials databases

DNASUi25750.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25750.
KEGGirno:25750.
UCSCiRGD:3041. rat.

Organism-specific databases

CTDi4129.
RGDi3041. Maob.

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP19643.
KOiK00274.
PhylomeDBiP19643.

Enzyme and pathway databases

BRENDAi1.4.3.4. 5301.
ReactomeiREACT_344337. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
SABIO-RKP19643.

Miscellaneous databases

NextBioi607939.
PROiP19643.

Gene expression databases

ExpressionAtlasiP19643. baseline and differential.
GenevisibleiP19643. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a cDNA for rat liver monoamine oxidase B."
    Ito A., Kuwahara T., Inadome S., Sagara Y.
    Biochem. Biophys. Res. Commun. 157:970-976(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "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].
    Tissue: Liver.
  3. "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B."
    Tsugeno Y., Ito A.
    J. Biol. Chem. 272:14033-14036(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ILE-199.

Entry informationi

Entry nameiAOFB_RAT
AccessioniPrimary (citable) accession number: P19643
Secondary accession number(s): Q5EBB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.