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Protein

Amine oxidase [flavin-containing] B

Gene

MAOB

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

FADBy similarity

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

  1. oxidoreductase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

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
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

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

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 520519Amine oxidase [flavin-containing] BPRO_0000099857Add
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

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

STRINGi9615.ENSCAFP00000030886.

Structurei

3D structure databases

ProteinModelPortaliQ7YRB7.
SMRiQ7YRB7. Positions 4-499.
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.
InParanoidiQ7YRB7.
KOiK00274.

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.

Q7YRB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKCDVVVV GGGISGMAAA KLLHDFGLNV VVLEARDRVG GRTYTIRNQK
60 70 80 90 100
VKYLDLGGSY VGPTQNCILR LAKELGLETY KVNEVERLIH HVKGKSYPFR
110 120 130 140 150
GPFPPVWNPI AYLDHNNLWR TMDDMGREIP SDAPWKAPLA EEWDHMTMKE
160 170 180 190 200
LLDKICWTES AKQLATLFVN LCVTAETHEV SALWFLWYVK QCGGTTRIIS
210 220 230 240 250
TTNGGQERKF VGGSGQVSER IMDLLGDQVK LERPVTHIDQ TGENVLVETL
260 270 280 290 300
NHEVYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQLITRVP LGSVIKCIVY
310 320 330 340 350
YKEPFWRKKD YCGTMIIEGE EAPIAYTLDD TKPDGNYAAI MGFILAHKAR
360 370 380 390 400
KLARLTKDER MKKLCELYAK VLGSQEALQP VHYEEKNWCE EQYSGGCYTT
410 420 430 440 450
YFPPGIMTQY GRVLRQPVGR IYFAGTETAT HWSGYMEGAV EAGERAAREI
460 470 480 490 500
LHAMGKIPED EIWQSEPESV DVPAQPITTT FLERHLPSVP GLLRLIGLTA
510 520
IFSATALGVL AHKRGLLVRV
Length:520
Mass (Da):58,384
Last modified:January 23, 2007 - v3
Checksum:iD5C6295875D7D8BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070958 mRNA. Translation: BAB86936.1.
RefSeqiNP_001002970.1. NM_001002970.1.
UniGeneiCfa.152.

Genome annotation databases

GeneIDi403451.
KEGGicfa:403451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB070958 mRNA. Translation: BAB86936.1.
RefSeqiNP_001002970.1. NM_001002970.1.
UniGeneiCfa.152.

3D structure databases

ProteinModelPortaliQ7YRB7.
SMRiQ7YRB7. Positions 4-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000030886.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403451.
KEGGicfa:403451.

Organism-specific databases

CTDi4129.

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiQ7YRB7.
KOiK00274.

Miscellaneous databases

NextBioi20816969.

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

  1. Hashizume C., Mori Y.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Beagle.
    Tissue: Brain.

Entry informationi

Entry nameiAOFB_CANFA
AccessioniPrimary (citable) accession number: Q7YRB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 78 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.