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UniProtKB/Swiss-Prot entry Q16853


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AOC3_HUMAN
Primary accession number Q16853
Secondary accession number Q45F94
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 91)
Name and origin of the protein
Protein name Membrane primary amine oxidase
Synonyms EC 1.4.3.21
Copper amine oxidase
Semicarbazide-sensitive amine oxidase
SSAO
Vascular adhesion protein 1
VAP-1
HPAO
Gene name
Name: AOC3
Synonyms: VAP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
DOI=10.1016/S0378-1119(96)00387-3; PubMed=8972912 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang X., McIntire W.S.;
"Cloning and sequencing of a copper-containing, topaquinone-containing monoamine oxidase from human placenta.";
Gene 179:279-286(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Lung;
DOI=10.1084/jem.188.1.17; PubMed=9653080 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.J., Salmi M., Bono P., Hellman J., Leu T., Jalkanen S.;
"Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule.";
J. Exp. Med. 188:17-27(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0378-1119(03)00753-4; PubMed=14585497 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N., Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.;
"Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina.";
Gene 318:45-53(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-5; TYR-167; THR-371; SER-408; HIS-426; TRP-441; THR-582; SER-700 AND VAL-749.
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 79-90 AND 123-132.
TISSUE=Adipocyte;
DOI=10.1042/BJ20040647; PubMed=15242332 [NCBI, ExPASy, EBI, Israel, Japan]
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COPPER AND CALCIUM IONS, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, AND GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
DOI=10.1110/ps.051438105; PubMed=16046623 [NCBI, ExPASy, EBI, Israel, Japan]
Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M., Salmi M., Jalkanen S., Johnson M.S., Salminen T.A.;
"Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.";
Protein Sci. 14:1964-1974(2005).
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.
  • CATALYTIC ACTIVITY: RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
  • COFACTOR: Binds 1 copper ion per subunit.
  • COFACTOR: Binds 2 calcium ions per subunit.
  • COFACTOR: Contains 1 topaquinone per subunit.
  • SUBUNIT: Homodimer; disulfide-linked.
  • SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
  • TISSUE SPECIFICITY: Strongly expressed on the high endothelial venules of peripheral lymph nodes and on hepatic endothelia. Also highly expressed in appendix, lung and small intestine. Expressed at lower levels in bone marrow, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, spleen and testis.
  • PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
  • PTM: N- and O-glycosylated.
  • SIMILARITY: Belongs to the copper/topaquinone oxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U39447; AAC50919.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF067406; AAC25170.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB050502; BAB18866.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ143944; AAZ38716.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050549; AAH50549.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC5234; JC5234.
RefSeq NP_003725.1; -.
UniGene Hs.198241
3D structure databases
PDB
1PU4; X-ray; 3.20 A; A/B=1-763.[ExPASy / RCSB / EBI]
1US1; X-ray; 2.90 A; A/B=1-763.[ExPASy / RCSB / EBI]
2C10; X-ray; 2.50 A; A/B/C/D=29-763.[ExPASy / RCSB / EBI]
2C11; X-ray; 2.90 A; A/B/C/D=29-763.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1PU4; -.
1US1; -.
2C10; -.
2C11; -.
ModBase Q16853.
Polymorphism databases
NIEHS-SNPs AOC3.
Organism-specific databases
H-InvDB HIX0013857; -.
HIX0059743; -.
HGNC HGNC:550; AOC3.
GenAtlas AOC3.
HPA HPA000980; -.
MIM 603735; gene. [NCBI / EBI]
PharmGKB PA24840; -.
GeneCards Q16853.
Gene expression databases
ArrayExpress Q16853; -.
CleanEx HS_AOC3; -.
GermOnline ENSG00000131471; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005794; Cellular component: Golgi apparatus (inferred from direct assay from HPA).
GO:0016021; Cellular component: integral to membrane (inferred from direct assay from UniProtKB).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from UniProtKB).
GO:0008131; Molecular function: amine oxidase activity (inferred from direct assay from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005507; Molecular function: copper ion binding (traceable author statement from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (traceable author statement from UniProtKB).
GO:0048038; Molecular function: quinone binding (inferred from direct assay from UniProtKB).
GO:0007155; Biological process: cell adhesion (inferred from direct assay from UniProtKB).
GO:0009308; Biological process: cellular amine metabolic process (inferred from direct assay from UniProtKB).
GO:0006954; Biological process: inflammatory response (traceable author statement from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000269; 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 of domain structure.
Gene3D G3DSA:3.10.450.40; CuNH_oxidase; 2.
G3DSA:2.70.98.20; Lyase_8_central; 1.
PANTHER PTHR10638; CuNH_oxidase; 1.
Pfam PF01179; Cu_amine_oxid; 1.
PF02727; Cu_amine_oxidN2; 1.
PF02728; Cu_amine_oxidN3; 1.
Pfam graphical view of domain structure.
PRINTS PR00766; CUDAOXIDASE.
PROSITE PS01164; COPPER_AMINE_OXID_1; 1.
PS01165; COPPER_AMINE_OXID_2; 1.
ProtoNet Q16853.
Proteomic databases
PeptideAtlas Q16853; -.
Genome annotation databases
Ensembl ENSG00000131471; Homo sapiens. [Contig view]
GeneID 8639; -.
KEGG hsa:8639; -.
NMPDR fig|9606.3.peg.13801; -.
Phylogenomic databases
HOGENOM Q16853; -.
HOVERGEN Q16853; -.
Other
DrugBank DB01275; Hydralazine.
DB00780; Phenelzine.
LinkHub Q16853; -.
NextBio 32389; -.
SOURCE AOC3; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Calcium; Cell adhesion; Copper; Direct protein sequencing; Glycoprotein; Membrane; Metal-binding; Oxidoreductase; Polymorphism; Signal-anchor; TPQ; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   763  762     Membrane primary amine oxidase. PRO_0000064102
TOPO_DOM   2     5  4     Cytoplasmic (Potential). 
TRANSMEM   6    26  21     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   27   763  737     Extracellular (Potential). 
ACT_SITE   386   386        Proton acceptor (By similarity). 
ACT_SITE   471   471        Schiff-base intermediate with substrate; via topaquinone (By similarity). 
METAL   520   520        Copper. 
METAL   522   522        Copper. 
METAL   529   529        Calcium 1. 
METAL   530   530        Calcium 1; via carbonyl oxygen. 
METAL   531   531        Calcium 1. 
METAL   572   572        Calcium 2. 
METAL   638   638        Calcium 2. 
METAL   663   663        Calcium 2; via carbonyl oxygen. 
METAL   665   665        Calcium 2. 
METAL   667   667        Calcium 2. 
METAL   673   673        Calcium 1. 
METAL   674   674        Calcium 1; via carbonyl oxygen. 
METAL   684   684        Copper. 
MOD_RES   471   471        2',4',5'-topaquinone. 
CARBOHYD   137   137        N-linked (GlcNAc...). 
CARBOHYD   212   212        O-linked (GalNAc...) (Probable). 
CARBOHYD   232   232        N-linked (GlcNAc...). 
CARBOHYD   294   294        N-linked (GlcNAc...). 
CARBOHYD   592   592        N-linked (GlcNAc...). 
CARBOHYD   618   618        N-linked (GlcNAc...). 
CARBOHYD   666   666        N-linked (GlcNAc...). 
DISULFID   198   199         
DISULFID   734   741         
DISULFID   748   748        Interchain. 
VARIANT   5     5  1     T -> R. VAR_025035 
VARIANT   167   167  1     H -> Y. VAR_025027 [3D]
VARIANT   317   317  1     Y -> H (in dbSNP:rs438287 [NCBI]). VAR_012064 [3D]
VARIANT   329   329  1     R -> Q (in dbSNP:rs2229595 [NCBI]). VAR_024343 [3D]
VARIANT   371   371  1     I -> T. VAR_025028 [3D]
VARIANT   408   408  1     A -> S. VAR_025029 [3D]
VARIANT   426   426  1     R -> H. VAR_025030 [3D]
VARIANT   441   441  1     R -> W. VAR_025031 [3D]
VARIANT   582   582  1     A -> T. VAR_025032 [3D]
VARIANT   700   700  1     G -> S. VAR_025033 [3D]
VARIANT   749   749  1     A -> V. VAR_025034 
HELIX   65    78  14      
HELIX   86    88  3      
STRAND   93   102  10      
HELIX   106   115  10      
STRAND   123   130  8      
STRAND   132   135  4      
STRAND   137   148  12      
STRAND   151   154  4      
HELIX   156   160  5      
HELIX   166   168  3      
HELIX   173   184  12      
TURN   185   187  3      
HELIX   188   191  4      
HELIX   192   199  8      
STRAND   207   211  5      
STRAND   217   219  3      
STRAND   224   231  8      
HELIX   238   240  3      
STRAND   242   250  9      
STRAND   253   255  3      
HELIX   256   258  3      
STRAND   260   266  7      
STRAND   269   272  4      
HELIX   274   282  9      
STRAND   297   300  4      
STRAND   314   316  3      
STRAND   322   326  5      
STRAND   329   341  13      
STRAND   343   345  3      
STRAND   347   354  8      
STRAND   357   372  16      
HELIX   377   381  5      
STRAND   383   385  3      
HELIX   386   388  3      
TURN   391   394  4      
TURN   400   402  3      
STRAND   408   421  14      
STRAND   423   445  23      
STRAND   447   449  3      
STRAND   451   468  18      
STRAND   471   479  9      
STRAND   485   493  9      
STRAND   497   499  3      
STRAND   506   512  7      
STRAND   515   518  4      
STRAND   520   530  11      
STRAND   534   550  17      
STRAND   557   569  13      
HELIX   572   575  4      
STRAND   577   581  5      
STRAND   585   594  10      
STRAND   600   608  9      
HELIX   622   629  8      
STRAND   630   636  7      
STRAND   653   655  3      
HELIX   660   663  4      
STRAND   670   684  15      
HELIX   688   690  3      
STRAND   701   713  13      
HELIX   715   718  4      
STRAND   723   726  4      
TURN   734   736  3      
HELIX   738   740  3      
TURN   742   746  5      
Sequence information
Length: 763 AA [This is the length of the unprocessed precursor] Molecular weight: 84622 Da [This is the MW of the unprocessed precursor]