AOC3

Functionⁱ

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.4 Publications

Catalytic activityⁱ

RCH₂NH₂ + H₂O + O₂ = RCHO + NH₃ + H₂O₂.1 Publication

Cofactorⁱ

Protein has several cofactor binding sites:

Cu cation
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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 (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM; COPPER AND SUBSTRATE, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
Note: Binds 1 copper ion per subunit.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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 (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM; COPPER AND SUBSTRATE, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
Ca²⁺
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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 (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM; COPPER AND SUBSTRATE, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
Note: Binds 2 calcium ions per subunit.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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 (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM; COPPER AND SUBSTRATE, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
L-topaquinone
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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 (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM; COPPER AND SUBSTRATE, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.
Note: Contains 1 topaquinone per subunit.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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 (2.90 ANGSTROMS) IN COMPLEX WITH CALCIUM; COPPER AND SUBSTRATE, DISULFIDE BONDS, TOPAQUINONE AT TYR-471, GLYCOSYLATION AT ASN-137; THR-212; ASN-232; ASN-294; ASN-592; ASN-618 AND ASN-666.

Kineticsⁱ

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	386	Proton acceptorBy similarity	1
Active siteⁱ	471	Schiff-base intermediate with substrate; via topaquinoneCombined sources	1
Metal bindingⁱ	520	Copper; via tele nitrogenCombined sources1 Publication	1
Metal bindingⁱ	522	Copper; via tele nitrogenCombined sources1 Publication	1
Metal bindingⁱ	529	Calcium 1Combined sources	1
Metal bindingⁱ	530	Calcium 1; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	531	Calcium 1Combined sources	1
Metal bindingⁱ	572	Calcium 2Combined sources	1
Metal bindingⁱ	638	Calcium 2Combined sources	1
Metal bindingⁱ	641	Calcium 2Combined sources	1
Metal bindingⁱ	663	Calcium 2; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	665	Calcium 2Combined sources	1
Metal bindingⁱ	667	Calcium 2Combined sources	1
Metal bindingⁱ	673	Calcium 1Combined sources	1
Metal bindingⁱ	674	Calcium 1; via carbonyl oxygenCombined sources	1
Metal bindingⁱ	684	Copper; via pros nitrogenCombined sources1 Publication	1

GO - Molecular functionⁱ

aliphatic-amine oxidase activity Source: UniProtKB-EC
aminoacetone:oxygen oxidoreductase(deaminating) activity Source: UniProtKB-EC
calcium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19764817
copper ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19764817
phenethylamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC
primary amine oxidase activity
Source: UniProtKB
Inferred from direct assayⁱ
protein heterodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 23349812
protein homodimerization activity
Source: UniProtKB
Traceable author statementⁱ
- 9653080
quinone binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9653080
tryptamine:oxygen oxidoreductase (deaminating) activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

amine metabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 9653080
cell adhesion
Source: UniProtKB
Inferred from direct assayⁱ
- 9653080
inflammatory response
Source: UniProtKB
Traceable author statementⁱ
- 9653080
negative regulation of primary amine oxidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 23349812
response to antibiotic
Source: UniProtKB
Inferred from direct assayⁱ
- 19764817
xenobiotic metabolic process Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Cell adhesion
Ligand	Calcium, Copper, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	1.4.3.21 2681
Reactomeⁱ	R-HSA-211945 Phase I - Functionalization of compounds
SABIO-RKⁱ	Q16853

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Membrane primary amine oxidase (EC:1.4.3.211 Publication) Alternative name(s): Copper amine oxidase HPAO Semicarbazide-sensitive amine oxidase Short name: SSAO Vascular adhesion protein 1 Short name: VAP-1
Gene namesⁱ	Name:AOC3 Synonyms:VAP1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 17

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000131471.6
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:550 AOC3
MIMⁱ	603735 gene
neXtProtⁱ	NX_Q16853

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 5	CytoplasmicSequence analysis	5
Transmembraneⁱ	6 – 26	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	21
Topological domainⁱ	27 – 763	ExtracellularSequence analysisAdd BLAST	737

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	211	M → V: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with N-394 and G-469. 1 Publication	1
Mutagenesisⁱ	394	Y → N: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and G-469. 1 Publication	1
Mutagenesisⁱ	469	L → G: Increased activity towards 2-phenylethylamine, and decreased activity towards methylamine; when associated with V-211 and N-394. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	8639
Open Targets More...OpenTargetsⁱ	ENSG00000131471
PharmGKBⁱ	PA24840

Chemistry databases

ChEMBLⁱ	CHEMBL3437
Drug and drug target database More...DrugBankⁱ	DB04334 6-hydroxydopa quinone DB01275 Hydralazine DB00780 Phenelzine
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2767

Polymorphism and mutation databases

DMDMⁱ	2501336

DMDMⁱ

2501336

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000064102	1 – 763	Membrane primary amine oxidaseAdd BLAST		763

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	137	N-linked (GlcNAc...) asparagineCombined sources2 Publications	1
Disulfide bondⁱ	198 ↔ 199	1 Publication
Glycosylationⁱ	212	O-linked (GalNAc...) threonine1 Publication	1
Glycosylationⁱ	232	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1
Glycosylationⁱ	294	N-linked (GlcNAc...) asparagineCombined sources2 Publications	1
Disulfide bondⁱ	404 ↔ 430	By similarity
Modified residueⁱ	471	2',4',5'-topaquinoneCombined sources	1
Glycosylationⁱ	592	N-linked (GlcNAc...) (complex) asparagineCombined sources4 Publications	1
Glycosylationⁱ	618	N-linked (GlcNAc...) asparagineCombined sources3 Publications	1
Glycosylationⁱ	666	N-linked (GlcNAc...) asparagineCombined sources3 Publications	1
Disulfide bondⁱ	734 ↔ 741	1 Publication
Disulfide bondⁱ	748	Interchain1 Publication

Post-translational modificationⁱ

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.1 Publication

N- and O-glycosylated.4 Publications

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbⁱ	Q16853
PeptideAtlas More...PeptideAtlasⁱ	Q16853
PRIDEⁱ	Q16853
ProteomicsDBⁱ	61105

PTM databases

iPTMnetⁱ	Q16853
PhosphoSitePlusⁱ	Q16853

Expressionⁱ

Tissue specificityⁱ

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.3 Publications

Inductionⁱ

Up-regulated during in vitro adipocyte differentiation.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000131471 Expressed in 206 organ(s), highest expression level in adipose tissue
CleanExⁱ	HS_AOC3
ExpressionAtlasⁱ	Q16853 baseline and differential
Genevisibleⁱ	Q16853 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB025797 HPA000980

HPAⁱ

CAB025797
HPA000980

Interactionⁱ

Subunit structureⁱ

Homodimer; disulfide-linked. Can heterodimerize with isoform 2 leading to reduced surface expression. Forms a heterodimer with AOC2.3 Publications

GO - Molecular functionⁱ

protein heterodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 23349812
protein homodimerization activity
Source: UniProtKB
Traceable author statementⁱ
- 9653080

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	114192, 11 interactors
IntActⁱ	Q16853, 10 interactors
STRINGⁱ	9606.ENSP00000312326

Chemistry databases

BindingDBⁱ

Q16853

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	65 – 78	Combined sources	14
Beta strandⁱ	83 – 85	Combined sources	3
Helixⁱ	86 – 88	Combined sources	3
Beta strandⁱ	93 – 102	Combined sources	10
Helixⁱ	106 – 115	Combined sources	10
Beta strandⁱ	123 – 130	Combined sources	8
Beta strandⁱ	132 – 135	Combined sources	4
Beta strandⁱ	137 – 144	Combined sources	8
Beta strandⁱ	146 – 148	Combined sources	3
Beta strandⁱ	151 – 154	Combined sources	4
Helixⁱ	156 – 160	Combined sources	5
Helixⁱ	166 – 168	Combined sources	3
Helixⁱ	173 – 185	Combined sources	13
Helixⁱ	188 – 191	Combined sources	4
Helixⁱ	192 – 199	Combined sources	8
Turnⁱ	203 – 206	Combined sources	4
Beta strandⁱ	208 – 211	Combined sources	4
Beta strandⁱ	217 – 219	Combined sources	3
Beta strandⁱ	224 – 231	Combined sources	8
Beta strandⁱ	234 – 236	Combined sources	3
Helixⁱ	238 – 240	Combined sources	3
Beta strandⁱ	242 – 250	Combined sources	9
Beta strandⁱ	253 – 255	Combined sources	3
Helixⁱ	256 – 258	Combined sources	3
Beta strandⁱ	260 – 266	Combined sources	7
Beta strandⁱ	269 – 272	Combined sources	4
Helixⁱ	274 – 282	Combined sources	9
Turnⁱ	283 – 285	Combined sources	3
Turnⁱ	298 – 300	Combined sources	3
Beta strandⁱ	314 – 316	Combined sources	3
Beta strandⁱ	318 – 320	Combined sources	3
Beta strandⁱ	322 – 326	Combined sources	5
Beta strandⁱ	329 – 342	Combined sources	14
Turnⁱ	343 – 345	Combined sources	3
Beta strandⁱ	346 – 354	Combined sources	9
Beta strandⁱ	357 – 372	Combined sources	16
Helixⁱ	377 – 380	Combined sources	4
Beta strandⁱ	383 – 385	Combined sources	3
Helixⁱ	386 – 388	Combined sources	3
Turnⁱ	391 – 394	Combined sources	4
Turnⁱ	400 – 402	Combined sources	3
Beta strandⁱ	408 – 421	Combined sources	14
Beta strandⁱ	423 – 445	Combined sources	23
Beta strandⁱ	447 – 449	Combined sources	3
Beta strandⁱ	451 – 468	Combined sources	18
Beta strandⁱ	471 – 479	Combined sources	9
Turnⁱ	481 – 483	Combined sources	3
Beta strandⁱ	485 – 493	Combined sources	9
Beta strandⁱ	497 – 499	Combined sources	3
Beta strandⁱ	506 – 512	Combined sources	7
Beta strandⁱ	515 – 518	Combined sources	4
Beta strandⁱ	520 – 530	Combined sources	11
Beta strandⁱ	534 – 551	Combined sources	18
Beta strandⁱ	554 – 569	Combined sources	16
Helixⁱ	572 – 575	Combined sources	4
Beta strandⁱ	577 – 581	Combined sources	5
Beta strandⁱ	585 – 594	Combined sources	10
Beta strandⁱ	600 – 608	Combined sources	9
Beta strandⁱ	617 – 619	Combined sources	3
Helixⁱ	622 – 629	Combined sources	8
Beta strandⁱ	630 – 636	Combined sources	7
Turnⁱ	647 – 651	Combined sources	5
Beta strandⁱ	653 – 655	Combined sources	3
Helixⁱ	660 – 663	Combined sources	4
Beta strandⁱ	670 – 684	Combined sources	15
Helixⁱ	688 – 690	Combined sources	3
Beta strandⁱ	700 – 713	Combined sources	14
Helixⁱ	715 – 718	Combined sources	4
Beta strandⁱ	723 – 729	Combined sources	7
Turnⁱ	734 – 736	Combined sources	3
Helixⁱ	738 – 741	Combined sources	4
Helixⁱ	742 – 745	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	Q16853
SMRⁱ	Q16853
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q16853

EvolutionaryTraceⁱ

Q16853

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	384 – 394	Substrate bindingCombined sourcesAdd BLAST		11
Regionⁱ	468 – 473	Substrate bindingBy similarity		6

Sequence similaritiesⁱ

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG1186 Eukaryota COG3733 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00510000046461
HOGENOMⁱ	HOG000233919
HOVERGENⁱ	HBG004164
InParanoidⁱ	Q16853
KEGG Orthology (KO) More...KOⁱ	K00276
OMAⁱ	ISWGRYQ
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G02WY
PhylomeDBⁱ	Q16853
TreeFamⁱ	TF314750

Family and domain databases

Gene3Dⁱ	2.70.98.20, 1 hit
InterProⁱ	View protein in InterPro IPR000269 Cu_amine_oxidase IPR015798 Cu_amine_oxidase_C IPR036460 Cu_amine_oxidase_C_sf IPR016182 Cu_amine_oxidase_N-reg IPR015800 Cu_amine_oxidase_N2 IPR015802 Cu_amine_oxidase_N3
PANTHERⁱ	PTHR10638 PTHR10638, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01179 Cu_amine_oxid, 1 hit PF02727 Cu_amine_oxidN2, 1 hit PF02728 Cu_amine_oxidN3, 1 hit
PRINTSⁱ	PR00766 CUDAOXIDASE
SUPFAMⁱ	SSF49998 SSF49998, 1 hit SSF54416 SSF54416, 2 hits
PROSITEⁱ	View protein in PROSITE PS01164 COPPER_AMINE_OXID_1, 1 hit PS01165 COPPER_AMINE_OXID_2, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.ⁱShow all

Isoform 1 (identifier: Q16853-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP 
        60         70         80         90        100
WTHPGQSQLF ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE 
       110        120        130        140        150
LQLPPKAAAL AHLDRGSPPP AREALAIVFF GRQPQPNVSE LVVGPLPHPS 
       160        170        180        190        200
YMRDVTVERH GGPLPYHRRP VLFQEYLDID QMIFNRELPQ ASGLLHHCCF 
       210        220        230        240        250
YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL HHVGLELLVN 
       260        270        280        290        300
HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW 
       310        320        330        340        350
SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF 
       360        370        380        390        400
DVRFQGERLV YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR 
       410        420        430        440        450
GVDCPYLATY VDWHFLLESQ APKTIRDAFC VFEQNQGLPL RRHHSDLYSH 
       460        470        480        490        500
YFGGLAETVL VVRSMSTLLN YDYVWDTVFH PSGAIEIRFY ATGYISSAFL 
       510        520        530        540        550
FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW AEDMVFVPMA 
       560        570        580        590        600
VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP 
       610        620        630        640        650
RGYRIQMLSF AGEPLPQNSS MARGFSWERY QLAVTQRKEE EPSSSSVFNQ 
       660        670        680        690        700
NDPWAPTVDF SDFINNETIA GKDLVAWVTA GFLHIPHAED IPNTVTVGNG 
       710        720        730        740        750
VGFFLRPYNF FDEDPSFYSA DSIYFRGDQD AGACEVNPLA CLPQAAACAP 
       760 
DLPAFSHGGF SHN

Length:763

Mass (Da):84,622

Last modified:January 23, 2007 - v3

Checksum:ⁱ58AD55605EC9D228

GO

Isoform 2 (identifier: Q16853-2) [UniParc]FASTA Add to basket

Also known as: VAP-1Delta3

The sequence of this isoform differs from the canonical sequence as follows:
630-634: YQLAV → IWWPG
635-763: Missing.

« Hide

        10         20         30         40         50
MNQKTILVLL ILAVITIFAL VCVLLVGRGG DGGEPSQLPH CPSVSPSAQP 
        60         70         80         90        100
WTHPGQSQLF ADLSREELTA VMRFLTQRLG PGLVDAAQAR PSDNCVFSVE 
       110        120        130        140        150
LQLPPKAAAL AHLDRGSPPP AREALAIVFF GRQPQPNVSE LVVGPLPHPS 
       160        170        180        190        200
YMRDVTVERH GGPLPYHRRP VLFQEYLDID QMIFNRELPQ ASGLLHHCCF 
       210        220        230        240        250
YKHRGRNLVT MTTAPRGLQS GDRATWFGLY YNISGAGFFL HHVGLELLVN 
       260        270        280        290        300
HKALDPARWT IQKVFYQGRY YDSLAQLEAQ FEAGLVNVVL IPDNGTGGSW 
       310        320        330        340        350
SLKSPVPPGP APPLQFYPQG PRFSVQGSRV ASSLWTFSFG LGAFSGPRIF 
       360        370        380        390        400
DVRFQGERLV YEISLQEALA IYGGNSPAAM TTRYVDGGFG MGKYTTPLTR 
       410        420        430        440        450
GVDCPYLATY VDWHFLLESQ APKTIRDAFC VFEQNQGLPL RRHHSDLYSH 
       460        470        480        490        500
YFGGLAETVL VVRSMSTLLN YDYVWDTVFH PSGAIEIRFY ATGYISSAFL 
       510        520        530        540        550
FGATGKYGNQ VSEHTLGTVH THSAHFKVDL DVAGLENWVW AEDMVFVPMA 
       560        570        580        590        600
VPWSPEHQLQ RLQVTRKLLE MEEQAAFLVG SATPRYLYLA SNHSNKWGHP 
       610        620        630 
RGYRIQMLSF AGEPLPQNSS MARGFSWERI WWPG

Note: Devoid of the semicarbazide-sensitive amine oxidase (SSAO) activity.

Show »

Length:634

Mass (Da):70,675

Checksum:ⁱ3275AE7C61775C99

GO

Isoform 3 (identifier: Q16853-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-543: Missing.

« Hide

        10         20         30         40         50
MVFVPMAVPW SPEHQLQRLQ VTRKLLEMEE QAAFLVGSAT PRYLYLASNH 
        60         70         80         90        100
SNKWGHPRGY RIQMLSFAGE PLPQNSSMAR GFSWERYQLA VTQRKEEEPS 
       110        120        130        140        150
SSSVFNQNDP WAPTVDFSDF INNETIAGKD LVAWVTAGFL HIPHAEDIPN 
       160        170        180        190        200
TVTVGNGVGF FLRPYNFFDE DPSFYSADSI YFRGDQDAGA CEVNPLACLP 
       210        220
QAAACAPDLP AFSHGGFSHN

Note: No experimental confirmation available.

Show »

Length:220

Mass (Da):24,533

Checksum:ⁱ37CB1D564AC233E2

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation
K7EIK5	K7EIK5_HUMAN	Amine oxidase Amine oxidase, EC 1.4.3.-	AOC3	144	Annotation score:
K7EL47	K7EL47_HUMAN	Amine oxidase Amine oxidase, EC 1.4.3.-	AOC3	152	Annotation score:
K7EQZ5	K7EQZ5_HUMAN	Amine oxidase Amine oxidase, EC 1.4.3.-	AOC3	112	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_025035	5	T → R1 PublicationCorresponds to variant dbSNP:rs33954211Ensembl.	1
Natural variantⁱVAR_052603	78	R → Q. Corresponds to variant dbSNP:rs402680Ensembl.	1
Natural variantⁱVAR_025027	167	H → Y1 PublicationCorresponds to variant dbSNP:rs2228470Ensembl.	1
Natural variantⁱVAR_052604	171	V → M. Corresponds to variant dbSNP:rs408038Ensembl.	1
Natural variantⁱVAR_052605	203	H → R. Corresponds to variant dbSNP:rs630079Ensembl.	1
Natural variantⁱVAR_012064	317	Y → H. Corresponds to variant dbSNP:rs438287Ensembl.	1
Natural variantⁱVAR_024343	329	R → Q. Corresponds to variant dbSNP:rs2229595Ensembl.	1
Natural variantⁱVAR_025028	371	I → T1 PublicationCorresponds to variant dbSNP:rs35097308Ensembl.	1
Natural variantⁱVAR_025029	408	A → S1 PublicationCorresponds to variant dbSNP:rs35643019Ensembl.	1
Natural variantⁱVAR_025030	426	R → H1 PublicationCorresponds to variant dbSNP:rs33986943Ensembl.	1
Natural variantⁱVAR_025031	441	R → W1 PublicationCorresponds to variant dbSNP:rs2229596Ensembl.	1
Natural variantⁱVAR_025032	582	A → T1 PublicationCorresponds to variant dbSNP:rs34987927Ensembl.	1
Natural variantⁱVAR_025033	700	G → S1 PublicationCorresponds to variant dbSNP:rs477207Ensembl.	1
Natural variantⁱVAR_025034	749	A → V1 PublicationCorresponds to variant dbSNP:rs34012919Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_055201	1 – 543	Missing in isoform 3. 1 PublicationAdd BLAST	543
Alternative sequenceⁱVSP_053751	630 – 634	YQLAV → IWWPG in isoform 2. 1 Publication	5
Alternative sequenceⁱVSP_053752	635 – 763	Missing in isoform 2. 1 PublicationAdd BLAST	129

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11444.1 [Q16853-1] CCDS62198.1 [Q16853-3] CCDS74071.1 [Q16853-2]
PIRⁱ	JC5234
NCBI Reference Sequences More...RefSeqⁱ	NP_001264660.1, NM_001277731.1 [Q16853-2] NP_001264661.1, NM_001277732.1 [Q16853-3] NP_003725.1, NM_003734.3 [Q16853-1]
UniGeneⁱ	Hs.198241

Genome annotation databases

Ensemblⁱ	ENST00000308423; ENSP00000312326; ENSG00000131471 [Q16853-1] ENST00000591562; ENSP00000468632; ENSG00000131471 [Q16853-3] ENST00000613571; ENSP00000484312; ENSG00000131471 [Q16853-2] ENST00000617500; ENSP00000477686; ENSG00000131471 [Q16853-3]
GeneIDⁱ	8639
KEGGⁱ	hsa:8639
UCSC genome browser More...UCSCⁱ	uc002ibv.6 human [Q16853-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q16853-3	Amine oxidase (Fragment)		HUMAN		152	UniRef100_Q16853-3
Amine oxidase (Fragment)		HUMAN		64
Amine oxidase (Fragment)		HUMAN		112
UPI0005CFFF81		HUMAN		794

Protein	Similar proteins		Species	Score	Length	Source
Q16853	Amine oxidase		PANTR		781	UniRef90_Q16853
Amine oxidase		SAIBB		763
Amine oxidase		CALJA		763
Amine oxidase		PONAB		763
Amine oxidase		PANPA		763
+29
Q16853-3	Amine oxidase (Fragment)		HUMAN		152	UniRef90_Q16853-3
Amine oxidase (Fragment)		HUMAN		64
Amine oxidase (Fragment)		HUMAN		112
UPI0005CFFF81		HUMAN		794
UPI0005D00B09		HUMAN		665

Protein	Similar proteins		Species	Score	Length	Source
Q16853	Membrane primary amine oxidase		BOVIN		763	UniRef50_Q16853
Retina-specific copper amine oxidase		MOUSE		757
Membrane primary amine oxidase		PONAB		763
Retina-specific copper amine oxidase		HUMAN		756
Amine oxidase		PANTR		781
+483

Cross-referencesⁱ

Web resourcesⁱ

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
CCDSⁱ	CCDS11444.1 [Q16853-1] CCDS62198.1 [Q16853-3] CCDS74071.1 [Q16853-2]
PIRⁱ	JC5234
RefSeqⁱ	NP_001264660.1, NM_001277731.1 [Q16853-2] NP_001264661.1, NM_001277732.1 [Q16853-3] NP_003725.1, NM_003734.3 [Q16853-1]
UniGeneⁱ	Hs.198241

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	4BTW	X-ray	2.80	A/B	27-763	[»]
	4BTX	X-ray	2.78	A/B	27-763	[»]
	4BTY	X-ray	3.10	A/B	27-763	[»]
ProteinModelPortalⁱ	Q16853
SMRⁱ	Q16853
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114192, 11 interactors
IntActⁱ	Q16853, 10 interactors
STRINGⁱ	9606.ENSP00000312326

Chemistry databases

BindingDBⁱ	Q16853
ChEMBLⁱ	CHEMBL3437
DrugBankⁱ	DB04334 6-hydroxydopa quinone DB01275 Hydralazine DB00780 Phenelzine
GuidetoPHARMACOLOGYⁱ	2767

PTM databases

iPTMnetⁱ	Q16853
PhosphoSitePlusⁱ	Q16853

Polymorphism and mutation databases

DMDMⁱ	2501336

DMDMⁱ

2501336

Proteomic databases

PaxDbⁱ	Q16853
PeptideAtlasⁱ	Q16853
PRIDEⁱ	Q16853
ProteomicsDBⁱ	61105

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000308423; ENSP00000312326; ENSG00000131471 [Q16853-1] ENST00000591562; ENSP00000468632; ENSG00000131471 [Q16853-3] ENST00000613571; ENSP00000484312; ENSG00000131471 [Q16853-2] ENST00000617500; ENSP00000477686; ENSG00000131471 [Q16853-3]
GeneIDⁱ	8639
KEGGⁱ	hsa:8639
UCSCⁱ	uc002ibv.6 human [Q16853-1]

Organism-specific databases

CTDⁱ	8639
DisGeNETⁱ	8639
EuPathDBⁱ	HostDB:ENSG00000131471.6
GeneCardsⁱ	AOC3
HGNCⁱ	HGNC:550 AOC3
HPAⁱ	CAB025797 HPA000980
MIMⁱ	603735 gene
neXtProtⁱ	NX_Q16853
OpenTargetsⁱ	ENSG00000131471
PharmGKBⁱ	PA24840
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1186 Eukaryota COG3733 LUCA
GeneTreeⁱ	ENSGT00510000046461
HOGENOMⁱ	HOG000233919
HOVERGENⁱ	HBG004164
InParanoidⁱ	Q16853
KOⁱ	K00276
OMAⁱ	ISWGRYQ
OrthoDBⁱ	EOG091G02WY
PhylomeDBⁱ	Q16853
TreeFamⁱ	TF314750

Enzyme and pathway databases

BRENDAⁱ	1.4.3.21 2681
Reactomeⁱ	R-HSA-211945 Phase I - Functionalization of compounds
SABIO-RKⁱ	Q16853

Miscellaneous databases

ChiTaRSⁱ	AOC3 human
EvolutionaryTraceⁱ	Q16853
GeneWikiⁱ	AOC3
GenomeRNAiⁱ	8639
Protein Ontology More...PROⁱ	PR:Q16853
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000131471 Expressed in 206 organ(s), highest expression level in adipose tissue
CleanExⁱ	HS_AOC3
ExpressionAtlasⁱ	Q16853 baseline and differential
Genevisibleⁱ	Q16853 HS

Family and domain databases

Gene3Dⁱ	2.70.98.20, 1 hit
InterProⁱ	View protein in InterPro IPR000269 Cu_amine_oxidase IPR015798 Cu_amine_oxidase_C IPR036460 Cu_amine_oxidase_C_sf IPR016182 Cu_amine_oxidase_N-reg IPR015800 Cu_amine_oxidase_N2 IPR015802 Cu_amine_oxidase_N3
PANTHERⁱ	PTHR10638 PTHR10638, 1 hit
Pfamⁱ	View protein in Pfam PF01179 Cu_amine_oxid, 1 hit PF02727 Cu_amine_oxidN2, 1 hit PF02728 Cu_amine_oxidN3, 1 hit
PRINTSⁱ	PR00766 CUDAOXIDASE
SUPFAMⁱ	SSF49998 SSF49998, 1 hit SSF54416 SSF54416, 2 hits
PROSITEⁱ	View protein in PROSITE PS01164 COPPER_AMINE_OXID_1, 1 hit PS01165 COPPER_AMINE_OXID_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	AOC3_HUMAN
Accessionⁱ	Q16853Primary (citable) accession number: Q16853 Secondary accession number(s): B2RCI5 , K7ESB3, L0L8N9, Q45F94
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	January 23, 2007
	Last modified:	September 12, 2018
	This is version 182 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

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Supporting data

UniProtKB - Q16853 (AOC3_HUMAN)

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Membrane primary amine oxidase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Endoplasmic reticulum

Endosome

Golgi apparatus

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Functionⁱ

Kineticsⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Computationally mapped potential isoform sequencesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ