Reviewed, UniProtKB/Swiss-Prot Q16853 (AOC3_HUMAN)

Names and origin

Protein names

Recommended 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
    HPAO

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.
Catalytic activity	RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2).
Cofactor	Binds 1 copper ion per subunit. Binds 2 calcium ions per subunit. Contains 1 topaquinone per subunit.
Subunit structure	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.
Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. N- and O-glycosylated.
Sequence similarities	Belongs to the copper/topaquinone oxidase family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	Calcium Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein TPQ
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell adhesion Ref.2 Inferred from direct assay. Source: UniProtKB cellular amine metabolic process Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB inflammatory response Ref.2 Traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA cell surface Ref.2 Inferred from direct assay. Source: UniProtKB integral to membrane Ref.2 Inferred from direct assay. Source: UniProtKB plasma membrane Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	amine oxidase activity Ref.2 Inferred from direct assay. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion binding Ref.1 Traceable author statement. Source: UniProtKB protein homodimerization activity Ref.2 Traceable author statement. Source: UniProtKB quinone binding Ref.2 Inferred from direct assay. Source: UniProtKB
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

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...)

Glycosylation

212

1

O-linked (GalNAc...) Probable

Glycosylation

232

1

N-linked (GlcNAc...)

Glycosylation

294

1

N-linked (GlcNAc...)

Glycosylation

592

1

N-linked (GlcNAc...)

Glycosylation

618

1

N-linked (GlcNAc...)

Glycosylation

666

1

N-linked (GlcNAc...)

Disulfide bond

198 ↔ 199

Disulfide bond

734 ↔ 741

Disulfide bond

748

Interchain

Natural variations

Natural variant

5

1

T → R

VAR_025035

Natural variant

167

1

H → Y

VAR_025027

Natural variant

317

1

Y → H: dbSNP rs438287.

VAR_012064

Natural variant

329

1

R → Q: dbSNP rs2229595.

VAR_024343

Natural variant

371

1

I → T

VAR_025028

Natural variant

408

1

A → S

VAR_025029

Natural variant

426

1

R → H

VAR_025030

Natural variant

441

1

R → W

VAR_025031

Natural variant

582

1

A → T

VAR_025032

Natural variant

700

1

G → S

VAR_025033

Natural variant

749

1

A → V

VAR_025034

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