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Protein

Amine oxidase [flavin-containing] B

Gene

MAOB

Organism
Cavia porcellus (Guinea pig)
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

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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
ProteomesiUP000005447: 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_0000099858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

STRINGi10141.ENSCPOP00000000879.

Structurei

3D structure databases

ProteinModelPortaliP58028.
SMRiP58028. Positions 4-496.
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.
InParanoidiP58028.

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.

P58028-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSKCDVVVV GGGISGLAAA KLLHDSGLNV VVLEARDCVG GRTYTLRNQN
60 70 80 90 100
VKYVDLGGAY VGPTQNRILR LAKELGLETY RVNDVERQIH HVKGKSYPFR
110 120 130 140 150
GPFPPAWNPI SYLDHNNLWR TMDDMGKEIP SDAPWKAPLA EEWDHMTMKE
160 170 180 190 200
LLNKICWTNC PRQFGTLFVN LCFTAETHEV SALWFLWYVK QCGGTTRIIS
210 220 230 240 250
TTNGGQERKF VGGSGQISER IMNLLGDRVK LQRPVVYIDQ TGESVLVETL
260 270 280 290 300
NHEIYEAKYV ISAIPPALGM KIHFKPPLPM MKNQLVSRVP LGSVIKCIVY
310 320 330 340 350
YKDPFWRKKD FCGTMVIEGE EAPVLYTMDD TKPDGSYAAI IGFIAAHKAR
360 370 380 390 400
KLARLTKEER LKKLCELYAK VLGSKEALKP VHYEEKNWCE EQYSGGCYTA
410 420 430 440 450
YFPPGIMTQY GRFLRQPVGR IFFAGTETAT HWSGYMEGAV EAGERAAREV
460 470 480 490 500
LNAIGKIPED EIWQPEPESV DVPAQPITTT FLERHLPSVP GLLRLIRLTT
510 520
VVSAVALGFL AQKRGLLLRI
Length:520
Mass (Da):58,410
Last modified:January 23, 2007 - v2
Checksum:i0AEBAE99A48BC206
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047271 mRNA. Translation: BAB40418.1.
RefSeqiNP_001166452.1. NM_001172981.1.

Genome annotation databases

GeneIDi100135573.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047271 mRNA. Translation: BAB40418.1.
RefSeqiNP_001166452.1. NM_001172981.1.

3D structure databases

ProteinModelPortaliP58028.
SMRiP58028. Positions 4-496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000000879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100135573.

Organism-specific databases

CTDi4129.

Phylogenomic databases

eggNOGiCOG1231.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiP58028.

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. "Nucleotide sequences of putative cDNAs for guinea-pig monoamine oxidase."
    Yaekashiwa N., Tamate H.B., Takeuchi T., Sugimoto H., Shibata K., Kinemuchi H.
    Inflammopharmacology 11:145-154(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Liver.

Entry informationi

Entry nameiAOFB_CAVPO
AccessioniPrimary (citable) accession number: P58028
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 88 of the entry and version 2 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.