Q16853 (AOC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	763 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. Ref.2 Ref.9 Ref.10
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. Forms heterodimer with AOC2. Ref.10 Ref.12
Subcellular location	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. Ref.2 Ref.9
Induction	Up-regulated during in vitro adipocyte differentiation. Ref.9
Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. N- and O-glycosylated. Ref.8 Ref.11 Ref.12
Sequence similarities	Belongs to the copper/topaquinone oxidase family.
Biophysicochemical properties	Kinetic parameters: KM=1.94 mM for 2-phenylethylamine Ref.10 KM=0.67 mM for methylamine

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein TPQ
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	amine metabolic process Inferred from direct assay Ref.2. Source: UniProtKB 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. Source: UniProtKB
Cellular component	cell surface Inferred from direct assay Ref.2. Source: UniProtKB integral to membrane Inferred from direct assay Ref.2. Source: UniProtKB plasma membrane Inferred from direct assay Ref.2. Source: UniProtKB
Molecular function	aliphatic-amine oxidase activity Inferred from electronic annotation. Source: EC aminoacetone:oxygen oxidoreductase(deaminating) activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from direct assay. Source: UniProtKB cation channel activity Inferred from direct assay. Source: UniProtKB copper ion binding Inferred from direct assay. Source: UniProtKB phenethylamine:oxygen oxidoreductase (deaminating) activity Inferred from electronic annotation. Source: EC primary amine oxidase activity Inferred from direct assay Ref.2. 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: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 763

762

Membrane primary amine oxidase

PRO_0000064102

Regions

Topological domain

2 – 5

4

Cytoplasmic Potential

Transmembrane

6 – 26

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

27 – 763

737

Extracellular Potential

Sites

Active site

386

1

Proton acceptor By similarity

Active site

471

1

Schiff-base intermediate with substrate; via topaquinone By similarity

Metal binding

520

1

Copper

Metal binding

522

1

Copper

Metal binding

529

1

Calcium 1

Metal binding

530

1

Calcium 1; via carbonyl oxygen

Metal binding

531

1

Calcium 1

Metal binding

572

1

Calcium 2

Metal binding

638

1

Calcium 2

Metal binding

663

1

Calcium 2; via carbonyl oxygen

Metal binding

665

1

Calcium 2

Metal binding

667

1

Calcium 2

Metal binding

673

1

Calcium 1

Metal binding

674

1

Calcium 1; via carbonyl oxygen

Metal binding

684

1

Copper

Amino acid modifications

Modified residue

471

1

2',4',5'-topaquinone

Glycosylation

137

1

N-linked (GlcNAc...) Ref.11 Ref.12

Glycosylation

212

1

O-linked (GalNAc...) Probable

Glycosylation

232

1

N-linked (GlcNAc...) Ref.12

Glycosylation

294

1

N-linked (GlcNAc...) Ref.11 Ref.12

Glycosylation

592

1

N-linked (GlcNAc...) Ref.8 Ref.11 Ref.12

Glycosylation

618

1

N-linked (GlcNAc...) Ref.8 Ref.11 Ref.12

Glycosylation

666

1

N-linked (GlcNAc...) Ref.8 Ref.11 Ref.12

Disulfide bond

198 ↔ 199

Ref.12

Disulfide bond

734 ↔ 741

Ref.12

Disulfide bond

748

Interchain Ref.12

Natural variations

Natural variant

5

1

T → R. Ref.5
Corresponds to variant rs33954211 [ dbSNP | Ensembl ].

VAR_025035

Natural variant

78

1

R → Q.
Corresponds to variant rs402680 [ dbSNP | Ensembl ].

VAR_052603

Natural variant

167

1

H → Y. Ref.5
Corresponds to variant rs2228470 [ dbSNP | Ensembl ].

VAR_025027

Natural variant

171

1

V → M.
Corresponds to variant rs408038 [ dbSNP | Ensembl ].

VAR_052604

Natural variant

203

1

H → R.
Corresponds to variant rs630079 [ dbSNP | Ensembl ].

VAR_052605

Natural variant

317

1

Y → H.
Corresponds to variant rs438287 [ dbSNP | Ensembl ].

VAR_012064

Natural variant

329

1

R → Q.
Corresponds to variant rs2229595 [ dbSNP | Ensembl ].

VAR_024343

Natural variant

371

1

I → T. Ref.5
Corresponds to variant rs35097308 [ dbSNP | Ensembl ].

VAR_025028

Natural variant

408

1

A → S. Ref.5
Corresponds to variant rs35643019 [ dbSNP | Ensembl ].

VAR_025029

Natural variant

426

1

R → H. Ref.5
Corresponds to variant rs33986943 [ dbSNP | Ensembl ].

VAR_025030

Natural variant

441

1

R → W. Ref.5
Corresponds to variant rs2229596 [ dbSNP | Ensembl ].

VAR_025031

Natural variant

582

1

A → T. Ref.5
Corresponds to variant rs34987927 [ dbSNP | Ensembl ].

VAR_025032

Natural variant

700

1

G → S. Ref.5
Corresponds to variant rs477207 [ dbSNP | Ensembl ].

VAR_025033

Natural variant

749

1

A → V. Ref.5
Corresponds to variant rs34012919 [ dbSNP | Ensembl ].

VAR_025034

Experimental info

Mutagenesis

211

1

M → V: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469. Ref.10

Mutagenesis

394

1

Y → N: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469. Ref.10

Mutagenesis

469

1

L → G: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394. Ref.10

Secondary structure

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763

Helix Strand Turn

Details...

Helix

65 – 78

14

Helix

86 – 88

3

Beta strand

93 – 102

10

Helix

106 – 115

10

Beta strand

123 – 130

8

Beta strand

132 – 135

4

Beta strand

137 – 148

12

Beta 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

Beta strand

207 – 211

5

Beta strand

217 – 219

3

Beta strand

224 – 231

8

Helix

238 – 240

3

Beta strand

242 – 250

9

Beta strand

253 – 255

3

Helix

256 – 258

3

Beta strand

260 – 266

7

Beta strand

269 – 272

4

Helix

274 – 282

9

Beta strand

297 – 300

4

Beta strand

314 – 316

3

Beta strand

322 – 326

5

Beta strand

329 – 341

13

Beta strand

343 – 345

3

Beta strand

347 – 354

8

Beta strand

357 – 372

16

Helix

377 – 381

5

Beta strand

383 – 385

3

Helix

386 – 388

3

Turn

391 – 394

4

Turn

400 – 402

3

Beta strand

408 – 421

14

Beta strand

423 – 445

23

Beta strand

447 – 449

3

Beta strand

451 – 468

18

Beta strand

471 – 479

9

Beta strand

485 – 493

9

Beta strand

497 – 499

3

Beta strand

506 – 512

7

Beta strand

515 – 518

4

Beta strand

520 – 530

11

Beta strand

534 – 550

17

Beta strand

557 – 569

13

Helix

572 – 575

4

Beta strand

577 – 581

5

Beta strand

585 – 594

10

Beta strand

600 – 608

9

Helix

622 – 629

8

Beta strand

630 – 636

7

Beta strand

653 – 655

3

Helix

660 – 663

4

Beta strand

670 – 684

15

Helix

688 – 690

3

Beta strand

701 – 713

13

Helix

715 – 718

4

Beta strand

723 – 726

4

Turn

734 – 736

3

Helix

738 – 740

3

Turn

742 – 746

5

Sequences

	Sequence		Length	Mass (Da)
	Q16853 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 58AD55605EC9D228	FASTA	763	84,622
	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

References

	« Hide 'large scale' referencesShow '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: 8972912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 9653080] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 14585497] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	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.
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: PNS.
[7]	"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: 15242332] [Abstract] Cited for: PROTEIN SEQUENCE OF 79-90 AND 123-132. Tissue: Adipocyte.
[8]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-592; ASN-618 AND ASN-666, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"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: 17400359] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[10]	"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: 19588076] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF MET-211; TYR-394 AND LEU-469.
[11]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-137; ASN-294; ASN-592; ASN-618 AND ASN-666, MASS SPECTROMETRY. Tissue: Liver.
[12]	"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: 16046623] [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

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U39447 mRNA. Translation: AAC50919.1.
AF067406 mRNA. Translation: AAC25170.1.
AB050502 Genomic DNA. Translation: BAB18866.1.
AK315129 mRNA. Translation: BAG37582.1.
DQ143944 Genomic DNA. Translation: AAZ38716.1.
BC050549 mRNA. Translation: AAH50549.1.

IPI

IPI00004457.

PIR

JC5234.

RefSeq

NP_003725.1. NM_003734.2.

UniGene

Hs.198241.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PU4	X-ray	3.20	A/B	1-763	[»]
1US1	X-ray	2.90	A/B	1-763	[»]
2C10	X-ray	2.50	A/B/C/D	29-763	[»]
2C11	X-ray	2.90	A/B/C/D	29-763	[»]
2Y73	X-ray	2.60	A/B	1-763	[»]
2Y74	X-ray	2.95	A/B	1-763	[»]
3ALA	X-ray	2.90	A/B/C/D/E/F/G	33-763	[»]

ProteinModelPortal

Q16853.

SMR

Q16853. Positions 58-761.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q16853. 1 interaction.

STRING

Q16853.

Polymorphism databases

DMDM

2501336.

Proteomic databases

PeptideAtlas

Q16853.

PRIDE

Q16853.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000308423; ENSP00000312326; ENSG00000131471.

GeneID

8639.

KEGG

hsa:8639.

NMPDR

fig|9606.3.peg.13801.

UCSC

uc002ibv.1. human.

Organism-specific databases

CTD

8639.

GeneCards

GC17P041003.

H-InvDB

HIX0013857.

HGNC

HGNC:550. AOC3.

HPA

CAB025797.
HPA000980.

MIM

603735. gene.

neXtProt

NX_Q16853.

PharmGKB

PA24840.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG04445.

HOGENOM

HBG356524.

HOVERGEN

HBG004164.

InParanoid

Q16853.

OMA

IEVKVHA.

OrthoDB

EOG4DZ1TS.

PhylomeDB

Q16853.

Gene expression databases

ArrayExpress

Q16853.

Bgee

Q16853.

CleanEx

HS_AOC3.

Genevestigator

Q16853.

GermOnline

ENSG00000131471. Homo sapiens.

Family and domain databases

InterPro

IPR000269. 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]

Gene3D

G3DSA:3.10.450.40. CuNH_oxidase. 2 hits.
G3DSA:2.70.98.20. Lyase_8_central. 1 hit.

KO

K00276.

PANTHER

PTHR10638. CuNH_oxidase. 1 hit.

Pfam

PF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]

PRINTS

PR00766. CUDAOXIDASE.

SUPFAM

SSF54416. Cu_amine_oxidase_N-reg. 2 hits.
SSF49998. CuNH_oxidase. 1 hit.

PROSITE

PS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB01275. Hydralazine.
DB00780. Phenelzine.

NextBio

32389.

SOURCE

Search...

Entry information

Entry name

AOC3_HUMAN

Accession

Primary (citable) accession number: Q16853
Secondary accession number(s): B2RCI5, Q45F94

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.