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Q16853 (AOC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Membrane primary amine oxidase

EC=1.4.3.21
Alternative name(s):
Copper amine oxidase
HPAO
Semicarbazide-sensitive amine oxidase
Short name=SSAO
Vascular adhesion protein 1
Short name=VAP-1
Gene names
Name:AOC3
Synonyms:VAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion. Has semicarbazide-sensitive (SSAO) monoamine oxidase activity. May play a role in adipogenesis. Ref.2 Ref.4 Ref.11 Ref.12

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.

Subunit structure

Homodimer; disulfide-linked. Can heterodimerize with isoform 2 leading to reduced surface expression. Forms a heterodimer with AOC2. Ref.4 Ref.12 Ref.15

Subcellular location

Cell membrane; Single-pass type II membrane protein Ref.2.

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 also in adipose tissue, in bone marrow, colon, heart, kidney, ovary, pancreas, placenta, prostate, skeletal muscle, spleen and testis. Isoform 2 seems to be the predominant transcript in fetal kidneys, fetal cartilage and fetal tonsils. The highest relative expression of isoform 2 occurs in skeletal muscle, heart, pancreas, kidney, and lung. Ref.2 Ref.4 Ref.11

Induction

Up-regulated during in vitro adipocyte differentiation. Ref.11

Post-translational modification

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

N- and O-glycosylated. Ref.14 Ref.15

Sequence similarities

Belongs to the copper/topaquinone oxidase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.94 mM for 2-phenylethylamine Ref.12

KM=0.67 mM for methylamine

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
Copper
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
TPQ
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processamine metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

cation transport

Inferred from direct assay PubMed 19764817. Source: GOC

cell adhesion

Inferred from direct assay Ref.2. Source: UniProtKB

inflammatory response

Traceable author statement Ref.2. Source: UniProtKB

response to antibiotic

Inferred from direct assay PubMed 19764817. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay Ref.4Ref.2. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.4. Source: UniProtKB

integral component of membrane

Inferred from direct assay Ref.2. Source: UniProtKB

microvillus

Inferred from direct assay Ref.4. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionaliphatic-amine oxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

aminoacetone:oxygen oxidoreductase(deaminating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

calcium ion binding

Inferred from direct assay PubMed 19764817. Source: UniProtKB

cation channel activity

Inferred from direct assay PubMed 19764817. Source: UniProtKB

copper ion binding

Inferred from direct assay PubMed 19764817. Source: UniProtKB

phenethylamine:oxygen oxidoreductase (deaminating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

primary amine oxidase activity

Inferred from direct assay PubMed 19764817Ref.4Ref.2. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction Ref.4. Source: UniProtKB

protein homodimerization activity

Traceable author statement Ref.2. Source: UniProtKB

quinone binding

Inferred from direct assay Ref.2. Source: UniProtKB

tryptamine:oxygen oxidoreductase (deaminating) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16853-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q16853-2)

Also known as: VAP-1Delta3;

The sequence of this isoform differs from the canonical sequence as follows:
     630-634: YQLAV → IWWPG
     635-763: Missing.
Note: Devoid of the semicarbazide-sensitive amine oxidase (SSAO) activity.
Isoform 3 (identifier: Q16853-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-543: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 763762Membrane primary amine oxidase
PRO_0000064102

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
Metal binding5221Copper
Metal binding5291Calcium 1
Metal binding5301Calcium 1; via carbonyl oxygen
Metal binding5311Calcium 1
Metal binding5721Calcium 2
Metal binding6381Calcium 2
Metal binding6631Calcium 2; via carbonyl oxygen
Metal binding6651Calcium 2
Metal binding6671Calcium 2
Metal binding6731Calcium 1
Metal binding6741Calcium 1; via carbonyl oxygen
Metal binding6841Copper

Amino acid modifications

Modified residue47112',4',5'-topaquinone
Glycosylation1371N-linked (GlcNAc...) Ref.13 Ref.15
Glycosylation2121O-linked (GalNAc...) Probable
Glycosylation2321N-linked (GlcNAc...) Ref.15
Glycosylation2941N-linked (GlcNAc...) Ref.13 Ref.15
Glycosylation5921N-linked (GlcNAc...) (complex) Ref.10 Ref.13 Ref.14 Ref.15
Glycosylation6181N-linked (GlcNAc...) Ref.10 Ref.13 Ref.15
Glycosylation6661N-linked (GlcNAc...) Ref.10 Ref.13 Ref.15
Disulfide bond198 ↔ 199 Ref.15
Disulfide bond734 ↔ 741 Ref.15
Disulfide bond748Interchain Ref.15

Natural variations

Alternative sequence1 – 543543Missing in isoform 3.
VSP_055201
Alternative sequence630 – 6345YQLAV → IWWPG in isoform 2.
VSP_053751
Alternative sequence635 – 763129Missing in isoform 2.
VSP_053752
Natural variant51T → R. Ref.6
Corresponds to variant rs33954211 [ dbSNP | Ensembl ].
VAR_025035
Natural variant781R → Q.
Corresponds to variant rs402680 [ dbSNP | Ensembl ].
VAR_052603
Natural variant1671H → Y. Ref.6
Corresponds to variant rs2228470 [ dbSNP | Ensembl ].
VAR_025027
Natural variant1711V → M.
Corresponds to variant rs408038 [ dbSNP | Ensembl ].
VAR_052604
Natural variant2031H → R.
Corresponds to variant rs630079 [ dbSNP | Ensembl ].
VAR_052605
Natural variant3171Y → H.
Corresponds to variant rs438287 [ dbSNP | Ensembl ].
VAR_012064
Natural variant3291R → Q.
Corresponds to variant rs2229595 [ dbSNP | Ensembl ].
VAR_024343
Natural variant3711I → T. Ref.6
Corresponds to variant rs35097308 [ dbSNP | Ensembl ].
VAR_025028
Natural variant4081A → S. Ref.6
Corresponds to variant rs35643019 [ dbSNP | Ensembl ].
VAR_025029
Natural variant4261R → H. Ref.6
Corresponds to variant rs33986943 [ dbSNP | Ensembl ].
VAR_025030
Natural variant4411R → W. Ref.6
Corresponds to variant rs2229596 [ dbSNP | Ensembl ].
VAR_025031
Natural variant5821A → T. Ref.6
Corresponds to variant rs34987927 [ dbSNP | Ensembl ].
VAR_025032
Natural variant7001G → S. Ref.6
Corresponds to variant rs477207 [ dbSNP | Ensembl ].
VAR_025033
Natural variant7491A → V. Ref.6
Corresponds to variant rs34012919 [ dbSNP | Ensembl ].
VAR_025034

Experimental info

Mutagenesis2111M → V: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469. Ref.12
Mutagenesis3941Y → N: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469. Ref.12
Mutagenesis4691L → G: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394. Ref.12

Secondary structure

........................................................................................................................................ 763
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 58AD55605EC9D228

FASTA76384,622
        10         20         30         40         50         60 
MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP WTHPGQSQLF 

        70         80         90        100        110        120 
ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE LQLPPKAAAL AHLDRGSPPP 

       130        140        150        160        170        180 
AREALAIVFF GRQPQPNVSE LVVGPLPHPS YMRDVTVERH GGPLPYHRRP VLFQEYLDID 

       190        200        210        220        230        240 
QMIFNRELPQ ASGLLHHCCF YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL 

       250        260        270        280        290        300 
HHVGLELLVN HKALDPARWT 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 MGKYTTPLTR GVDCPYLATY VDWHFLLESQ 

       430        440        450        460        470        480 
APKTIRDAFC VFEQNQGLPL RRHHSDLYSH YFGGLAETVL VVRSMSTLLN YDYVWDTVFH 

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

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

       610        620        630        640        650        660 
RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ NDPWAPTVDF 

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

       730        740        750        760 
DSIYFRGDQD AGACEVNPLA CLPQAAACAP DLPAFSHGGF SHN 

« Hide

Isoform 2 (VAP-1Delta3) [UniParc].

Checksum: 3275AE7C61775C99
Show »

FASTA63470,675
Isoform 3 [UniParc].

Checksum: 37CB1D564AC233E2
Show »

FASTA22024,533

References

« Hide 'large scale' references
[1]"Cloning and sequencing of a copper-containing, topaquinone-containing monoamine oxidase from human placenta."
Zhang X., McIntire W.S.
Gene 179:279-286(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule."
Smith D.J., Salmi M., Bono P., Hellman J., Leu T., Jalkanen S.
J. Exp. Med. 188:17-27(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Lung.
[3]"Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina."
Zhang Q., Mashima Y., Noda S., Imamura Y., Kudoh J., Shimizu N., Nishiyama T., Umeda S., Oguchi Y., Tanaka Y., Iwata T.
Gene 318:45-53(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Functional modulation of vascular adhesion protein-1 by a novel splice variant."
Kaitaniemi S., Gron K., Elovaara H., Salmi M., Jalkanen S., Elima K.
PLoS ONE 8:E54151-E54151(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Tissue: Placenta.
[6]NIEHS SNPs program
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-5; TYR-167; THR-371; SER-408; HIS-426; TRP-441; THR-582; SER-700 AND VAL-749.
[7]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: PNS.
[9]"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 79-90 AND 123-132.
Tissue: Adipocyte.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666.
Tissue: Plasma.
[11]"Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes."
Bour S., Daviaud D., Gres S., Lefort C., Prevot D., Zorzano A., Wabitsch M., Saulnier-Blache J.-S., Valet P., Carpene C.
Biochimie 89:916-925(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[12]"The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase."
Kaitaniemi S., Elovaara H., Groen K., Kidron H., Liukkonen J., Salminen T., Salmi M., Jalkanen S., Elima K.
Cell. Mol. Life Sci. 66:2743-2757(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF MET-211; TYR-394 AND LEU-469.
[13]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592; ASN-618 AND ASN-666.
Tissue: Liver.
[14]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-592.
[15]"Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications."
Airenne T.T., Nymalm Y., Kidron H., Smith D.J., Pihlavisto M., Salmi M., Jalkanen S., Johnson M.S., Salminen T.A.
Protein Sci. 14:1964-1974(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH COPPER AND CALCIUM IONS, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39447 mRNA. Translation: AAC50919.1.
AF067406 mRNA. Translation: AAC25170.1.
AB050502 Genomic DNA. Translation: BAB18866.1.
JX020506 mRNA. Translation: AGB67480.1.
AK025727 mRNA. No translation available.
AK315129 mRNA. Translation: BAG37582.1.
DQ143944 Genomic DNA. Translation: AAZ38716.1.
AC016889 Genomic DNA. No translation available.
BC050549 mRNA. Translation: AAH50549.1.
CCDSCCDS11444.1.
PIRJC5234.
RefSeqNP_001264660.1. NM_001277731.1. [Q16853-2]
NP_001264661.1. NM_001277732.1.
NP_003725.1. NM_003734.3. [Q16853-1]
UniGeneHs.198241.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PU4X-ray3.20A/B1-763[»]
1US1X-ray2.90A/B1-763[»]
2C10X-ray2.50A/B/C/D29-763[»]
2C11X-ray2.90A/B/C/D29-763[»]
2Y73X-ray2.60A/B1-763[»]
2Y74X-ray2.95A/B1-763[»]
3ALAX-ray2.90A/B/C/D/E/F/G33-763[»]
4BTWX-ray2.80A/B27-763[»]
4BTXX-ray2.78A/B27-763[»]
4BTYX-ray3.10A/B27-763[»]
ProteinModelPortalQ16853.
SMRQ16853. Positions 58-761.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114192. 2 interactions.
IntActQ16853. 2 interactions.
STRING9606.ENSP00000312326.

Chemistry

BindingDBQ16853.
ChEMBLCHEMBL3437.
DrugBankDB01275. Hydralazine.
DB00780. Phenelzine.

Polymorphism databases

DMDM2501336.

Proteomic databases

PaxDbQ16853.
PeptideAtlasQ16853.
PRIDEQ16853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308423; ENSP00000312326; ENSG00000131471.
ENST00000591562; ENSP00000468632; ENSG00000131471.
GeneID8639.
KEGGhsa:8639.
UCSCuc002ibv.4. human. [Q16853-1]

Organism-specific databases

CTD8639.
GeneCardsGC17P041003.
HGNCHGNC:550. AOC3.
HPACAB025797.
HPA000980.
MIM603735. gene.
neXtProtNX_Q16853.
PharmGKBPA24840.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3733.
HOGENOMHOG000233919.
HOVERGENHBG004164.
InParanoidQ16853.
KOK00276.
OMASWERYQL.
OrthoDBEOG7353W8.
PhylomeDBQ16853.
TreeFamTF314750.

Enzyme and pathway databases

SABIO-RKQ16853.

Gene expression databases

ArrayExpressQ16853.
BgeeQ16853.
CleanExHS_AOC3.
GenevestigatorQ16853.

Family and domain databases

Gene3D2.70.98.20. 1 hit.
3.10.450.40. 2 hits.
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]
PANTHERPTHR10638. PTHR10638. 1 hit.
PfamPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSPR00766. CUDAOXIDASE.
SUPFAMSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ16853.
GeneWikiAOC3.
GenomeRNAi8639.
NextBio32389.
PROQ16853.
SOURCESearch...

Entry information

Entry nameAOC3_HUMAN
AccessionPrimary (citable) accession number: Q16853
Secondary accession number(s): B2RCI5 expand/collapse secondary AC list , K7ESB3, L0L8N9, Q45F94
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM