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Q5R9I0 (AOC3_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Membrane primary amine oxidase
EC=1.4.3.21
Alternative name(s):
Copper amine oxidase
Semicarbazide-sensitive amine oxidase
Short name=SSAO
Vascular adhesion protein 1
Short name=VAP-1
Gene names
Name:AOC3
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length763 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis By similarity.

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.

Subunit structure

Homodimer; disulfide-linked. Forms heterodimer with AOC2 By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein By similarity.

Post-translational modification

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

N- and O-glycosylated By similarity.

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 763762Membrane primary amine oxidase
PRO_0000064104

Regions

Topological domain2 – 54Cytoplasmic Potential
Transmembrane6 – 2621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 763737Extracellular Potential

Sites

Active site3861Proton acceptor By similarity
Active site4711Schiff-base intermediate with substrate; via topaquinone By similarity
Metal binding5201Copper By similarity
Metal binding5221Copper By similarity
Metal binding5291Calcium 1 By similarity
Metal binding5301Calcium 1; via carbonyl oxygen By similarity
Metal binding5311Calcium 1 By similarity
Metal binding5721Calcium 2 By similarity
Metal binding6381Calcium 2 By similarity
Metal binding6631Calcium 2; via carbonyl oxygen By similarity
Metal binding6651Calcium 2 By similarity
Metal binding6671Calcium 2 By similarity
Metal binding6731Calcium 1 By similarity
Metal binding6741Calcium 1; via carbonyl oxygen By similarity
Metal binding6841Copper By similarity

Amino acid modifications

Modified residue47112',4',5'-topaquinone By similarity
Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation2121O-linked (GalNAc...) By similarity
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation5921N-linked (GlcNAc...) Potential
Glycosylation6181N-linked (GlcNAc...) Potential
Glycosylation6661N-linked (GlcNAc...) Potential
Disulfide bond198 ↔ 199 By similarity
Disulfide bond734 ↔ 741 By similarity
Disulfide bond748Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R9I0 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AB73B9807646D707

FASTA76384,602
        10         20         30         40         50         60 
MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSISPSAQP WTHPGQSQLF 

        70         80         90        100        110        120 
ADLSREELTA VMRFLTQRLG PGLVDAAQAQ PSDNCIFSVE LQLPPKAAAL AHLDRGSPPP 

       130        140        150        160        170        180 
AREALAIILF GRQPQPNVSE LVVGPLPHPS YMRDVTVEHH GGPLPYHRRP VLFQEYLDID 

       190        200        210        220        230        240 
QMIFDRELPQ ASGLLHHCCF YKRRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL 

       250        260        270        280        290        300 
HHVGLELLVN HKALDPAHWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW 

       310        320        330        340        350        360 
SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF DVRFQGERLV 

       370        380        390        400        410        420 
YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYATPLTR GVDCPYLATY VDWHFLLESR 

       430        440        450        460        470        480 
APKTIRDAFC VFEQNQGLPL RRHHSDLYSH YFGGLAETVQ VIRSMSTLLN YDYVWDMVFH 

       490        500        510        520        530        540 
PSGAIEIRFY ATGYISSAFL FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DIAGLENWVW 

       550        560        570        580        590        600 
AEDMVFVPMA VPWSPEHQLQ RLQVTRKLLE TEEQAAFLMG SATPRYLYLA SNHSNKWGHP 

       610        620        630        640        650        660 
RGYRIQMLSF AGKPLPQNSS MAKGFSWERY QLAVTQRKEE EPSSSSVFNQ NDPWAATVDF 

       670        680        690        700        710        720 
SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG VGFFLRPYNF FDEDPSFYSA 

       730        740        750        760 
DSIYFRGDQD AGACEVNPLA CLPQAAACAP DLPAFSHGGF SHN

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR859408 mRNA. Translation: CAH91580.1.
RefSeqNP_001125929.1. NM_001132457.1.
UniGenePab.12072.

3D structure databases

ProteinModelPortalQ5R9I0.
SMRQ5R9I0. Positions 58-761.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100172863.
KEGGpon:100172863.

Organism-specific databases

CTD8639.

Phylogenomic databases

HOVERGENHBG004164.
InParanoidQ5R9I0.

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.
PROSITEPS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAOC3_PONAB
AccessionPrimary (citable) accession number: Q5R9I0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 55 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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