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Reviewed, UniProtKB/Swiss-Prot O46406 (AOCY_BOVIN)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Primary amine oxidase, lung isozyme
    EC=1.4.3.21
Alternative name(s):
    Copper amine oxidase
    Amine oxidase [copper-containing]
    BOLAO
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length762 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Catalytic activity

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.

Cofactor

Binds 1 copper ion per subunit By similarity.

Binds 2 calcium ions per subunit By similarity.

Contains 1 topaquinone per subunit By similarity.

Subcellular location

Secreted › extracellular space By similarity.

Tissue specificity

Expressed in lung, spleen, heart and kidney.

Post-translational modification

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.

Miscellaneous

Inhibited by amiloride in a competitive manner By similarity.

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Copper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
TPQ
Gene Ontology (GO)
   Biological processcellular amine metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionamine oxidase activity

Inferred from electronic annotation. Source: EC

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

copper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

quinone binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 762746Primary amine oxidase, lung isozyme
PRO_0000035670

Sites

Active site3851Proton acceptor By similarity
Active site4701Schiff-base intermediate with substrate; via topaquinone By similarity
Metal binding5191Copper By similarity
Metal binding5211Copper By similarity
Metal binding5281Calcium 1 By similarity
Metal binding5291Calcium 1; via carbonyl oxygen By similarity
Metal binding5301Calcium 1 By similarity
Metal binding5711Calcium 2 By similarity
Metal binding6371Calcium 2 By similarity
Metal binding6621Calcium 2; via carbonyl oxygen By similarity
Metal binding6641Calcium 2 By similarity
Metal binding6661Calcium 2 By similarity
Metal binding6721Calcium 1 By similarity
Metal binding6731Calcium 1; via carbonyl oxygen By similarity
Metal binding6831Copper By similarity

Amino acid modifications

Modified residue47012',4',5'-topaquinone By similarity
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation6171N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
O46406-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: BB43D04776744AF2

FASTA76284,883
        10         20         30         40         50         60 
MFIFIFLSLW TLLVMGREEG GVGSEEGVGK QCHPSLPPRC PSRSPSDQPW THPDQSQLFA 

        70         80         90        100        110        120 
DLSREELTAV MSFLTQKLGP DLVDAAQARP SDNCIFSVEL QLPPKAAALA HLDRRSPPPA 

       130        140        150        160        170        180 
REALAIVFFG GQPQPNVTEL VVGPLPQPSY MRDVTVERHG GPLPYYRHTV LLREYLDIDQ 

       190        200        210        220        230        240 
MIFNRELPQA AGVLHHCCSY KQGGGNLVTM TTAPPGLQSG DRATWFGLYY NISKAGYYLH 

       250        260        270        280        290        300 
PVGLELLVDH KALDPAQWTI QKVFFQGRYY ESLVQLEEQF EAGRVNVVVI PNNGTGGSWS 

       310        320        330        340        350        360 
LKSQVPPGPT PPLQFHPQGT RFSVQGSRVT SSLWTFSFGL GAFSGPRIFD IRFQGERLAY 

       370        380        390        400        410        420 
EISLQEAVAI YGGNTPAAML TRYMDACFGM GKFATPLTRG VDCPYLATYV DWHFLLESQA 

       430        440        450        460        470        480 
PKTLHDAFCV FEQNKGLPLR RHHSDFISQY FGGVVETVLV FRSVSTLLNY DYVWDMVFHP 

       490        500        510        520        530        540 
NGAIEVKFHV TGYISSAFFF GTAQKYGNQV RENTLGTVHT HSAHYKVDLD VGGLENWVWA 

       550        560        570        580        590        600 
EDMAFVPTTV PWSPEHQIQR LQVIRKQLET EEQAAFPLGG GSPRYLYLAS KQSNKWGHPR 

       610        620        630        640        650        660 
GYRIQTVSFA GRPLPQNSST ERAISWGRYQ LAVTQRKETE PSSSSVFNQN DPWTPTVDFA 

       670        680        690        700        710        720 
DFINNETIAG KDLVAWVTAG FLHIPHAEDI PNTVTVGNGV GFFLRPYNFF DQEPSMDSAD 

       730        740        750        760 
SIYFREGQDA GSCEINPLAC LPQAATCAPD LPVFSHGGYP EY

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References

[1]"Structure and tissue-specific expression of genes encoding bovine copper amine oxidases."
Hogdall E.V.S., Houen G., Borre M., Bundgaard J.R., Larsson L.-I., Vuust J.
Eur. J. Biochem. 251:320-328(1998) [PubMed: 9492300] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.

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Cross-references

Sequence databases

Y15774 mRNA. Translation: CAA75776.1.
IPIIPI00709862.
UniGeneBt.4177
Bt.88366

3D structure databases

SMRO46406. Positions 57-717.
ModBaseSearch...

Proteomic databases

PRIDEO46406.

Genome annotation databases

EnsemblENSBTAG00000001041. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGENO46406.

Enzyme and pathway databases

BRENDA1.4.3.6. 251.

Family and domain databases

InterProIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR015800. Cu_amine_oxidase_N2.
IPR015801. Cu_amine_oxidase_N2/3.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
Gene3DG3DSA:3.10.450.40. CuNH_oxidase. 2 hits.
G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHERPTHR10638. CuNH_oxidase. 1 hit.
PfamPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSPR00766. CUDAOXIDASE.
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAOCY_BOVIN
AccessionPrimary (citable) accession number: O46406
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents