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Q29437 (AOCX_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

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

Protein attributes

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

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 copper ion per subunit.

Binds 2 calcium ions per subunit.

Contains 1 topaquinone per subunit.

Subcellular location

Secreted › extracellular space.

Tissue specificity

Liver.

Post-translational modification

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

Miscellaneous

Inhibited by amiloride in a competitive manner.

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616
Chain17 – 762746Primary amine oxidase, liver isozyme
PRO_0000035669

Sites

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

Amino acid modifications

Modified residue47012',4',5'-topaquinone
Glycosylation1361N-linked (GlcNAc...) Ref.3
Glycosylation2311N-linked (GlcNAc...) Ref.3
Glycosylation6651N-linked (GlcNAc...) Ref.3

Secondary structure

1 ......................................................................................................... 762
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q29437 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AA959771360295FE

FASTA76284,757
        10         20         30         40         50         60 
MFIFIFLSLW TLLVMGREEG GVGSEEGVGK QCHPSLPPRC PSRSPSDQPW THPDQSQLFA 

        70         80         90        100        110        120 
DLSREELTTV MSFLTQQLGP DLVDAAQARP SDNCVFSVEL QLPPKAAALA HLDRGSPPPA 

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

       190        200        210        220        230        240 
MIFNRELPQA AGVLHHCCSY KQGGQKLLTM NSAPRGVQSG DRSTWFGIYY NITKGGPYLH 

       250        260        270        280        290        300 
PVGLELLVDH KALDPADWTV QKVFFQGRYY ENLAQLEEQF EAGQVNVVVI PDDGTGGFWS 

       310        320        330        340        350        360 
LKSQVPPGPT PPLQFHPQGP RFSVQGNRVA SSLWTFSFGL GAFSGPRVFD VRFQGERLAY 

       370        380        390        400        410        420 
EISLQEAGAV YGGNTPAAML TRYMDSGFGM GYFATPLIRG VDCPYLATYM DWHFVVESQT 

       430        440        450        460        470        480 
PKTLHDAFCV FEQNKGLPLR RHHSDFLSHY FGGVAQTVLV FRSVSTMLNY DYVWDMVFYP 

       490        500        510        520        530        540 
NGAIEVKLHA TGYISSAFLF GAARRYGNQV GEHTLGPVHT HSAHYKVDLD VGGLENWVWA 

       550        560        570        580        590        600 
EDMAFVPTAI PWSPEHQIQR LQVTRKQLET EEQAAFPLGG ASPRYLYLAS KQSNKWGHPR 

       610        620        630        640        650        660 
GYRIQTVSFA GGPMPQNSPM ERAFSWGRYQ LAITQRKETE PSSSSVFNQN DPWTPTVDFS 

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

       730        740        750        760 
SIYFREGQDA GSCEINPLAC LPQAATCAPD LPVFSHGGYP EY

« Hide

References

[1]"Primary structures for a mammalian cellular and serum copper amine oxidase."
Mu D., Medzihradszky K.F., Adams G.W., Mayer P., Hines W.M., Burlingame A.L., Smith A.J., Cai D., Klinman J.P.
J. Biol. Chem. 269:9926-9932(1994) [PubMed: 8144587] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Identification of topaquinone and its consensus sequence in copper amine oxidases."
Janes S.M., Palcic M.M., Scaman C.H., Smith A.J., Brown D.E., Dooley D.M., Mure M., Klinman J.P.
Biochemistry 31:12147-12154(1992) [PubMed: 1457410] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[3]"Crystal structure of amine oxidase from bovine serum."
Lunelli M., Di Paolo M.L., Biadene M., Calderone V., Battistutta R., Scarpa M., Rigo A., Zanotti G.
J. Mol. Biol. 346:991-1004(2005) [PubMed: 15701511] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 17-762 IN COMPLEX WITH COPPER AND CALCIUM IONS, TOPAQUINONE AT TYR-470, GLYCOSYLATION AT ASN-136; ASN-231 AND ASN-665.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S69583 mRNA. Translation: AAB30397.1.
L27218 mRNA. Translation: AAA30525.1.
IPIIPI00706345.
PIRA54411.
RefSeqNP_001124236.1. NM_001130764.1.
UniGeneBt.52514.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TU5X-ray2.37A/B17-762[»]
2PNCX-ray2.40A/B17-762[»]
ProteinModelPortalQ29437.
SMRQ29437. Positions 57-759.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ29437.

Proteomic databases

PRIDEQ29437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000001383; ENSBTAP00000001383; ENSBTAG00000001041.
GeneID789307.
KEGGbta:789307.

Organism-specific databases

CTD789307.

Phylogenomic databases

GeneTreeENSGT00510000046461.
HOVERGENHBG004164.
InParanoidQ29437.
OMAGYIQSAF.
OrthoDBEOG4DZ1TS.
PhylomeDBQ29437.

Family and domain databases

InterProIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
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.
KOK00276.
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.
SUPFAMSSF54416. Cu_amine_oxidase_N-reg. 2 hits.
SSF49998. CuNH_oxidase. 1 hit.
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAOCX_BOVIN
AccessionPrimary (citable) accession number: Q29437
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 16, 2011
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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