Aoc3 amine oxidase, copper containing 3 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Aoc3provided by RGD
Official Full Name: amine oxidase, copper containing 3provided by RGD
Primary source: RGD:62058
See related: AllianceGenome:RGD:62058
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: SSAO
Summary: Enables identical protein binding activity and primary methylamine oxidase activity. Involved in several processes, including eating behavior; leukocyte migration involved in inflammatory response; and positive regulation of D-glucose transmembrane transport. Located in extracellular space. Used to study aortic aneurysm; obesity; type 2 diabetes mellitus; and uveitis. Biomarker of intracranial aneurysm. Orthologous to human AOC3 (amine oxidase copper containing 3). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Lung (RPKM 470.0), Heart (RPKM 277.5) and 7 other tissues See more
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Genomic context

Location:: 10q31

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	10	NC_086028.1 (86773018..86780961)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	10	NC_051345.1 (86272757..86280702)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	10	NC_005109.4 (89251370..89259313)

Chromosome 10 - NC_086028.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The Biological Implication of Semicarbazide-Sensitive Amine Oxidase (SSAO) Upregulation in Rat Systemic Inflammatory Response under Simulated Aerospace Environment.
Title: The Biological Implication of Semicarbazide-Sensitive Amine Oxidase (SSAO) Upregulation in Rat Systemic Inflammatory Response under Simulated Aerospace Environment.
Comparison of Inhibitor and Substrate Selectivity between Rodent and Human Vascular Adhesion Protein-1.
Title: Comparison of Inhibitor and Substrate Selectivity between Rodent and Human Vascular Adhesion Protein-1.
In acute mesenteric ischemia, Vap-1 levels are significantly increased and correlated with ischemic changes.
Title: Comparison of the diagnostic values of vascular adhesion protein-1 and intestinal fatty acid-binding protein in the diagnosis of acute mesenteric ischemia.
Data show that 35 potential amine oxidase copper containing 3 (SSAO)-interacting proteins were found to be altered in type 2 Diabetes (T2D).
Title: Alteration of SSAO interactome reveals weakened cell adhesion and motor function of adipocytes in T2D.
VAP-1 plays a critical role in the pathophysiology of renal ischemia/reperfusion injury by enhancement of neutrophil infiltration generating a local hydrogen peroxide gradient.
Title: Vascular adhesion protein-1 enhances neutrophil infiltration by generation of hydrogen peroxide in renal ischemia/reperfusion injury.
The changes of K(M) and k(c)/K(M) values of copper amine oxidase appear due to the presence of positively charged groups in the substrate molecules.
Title: Preliminary kinetic characterization of a copper amine oxidase from rat liver mitochondria matrix.
Provide evidence for a role for VAP-1 in the inflammatory outcome of diabetic retinopathy. Specifically, VAP-1 plays a central role in regulating leukocyte transmigration rate during chronic low-grade inflammation.
Title: Vascular adhesion protein-1 regulates leukocyte transmigration rate in the retina during diabetes.
evidence for an important role of VAP-1 in the recruitment of macrophages to choroidal neovascularization lesions, establishing a novel link between VAP-1 and angiogenesis
Title: Vascular adhesion protein-1 blockade suppresses choroidal neovascularization.
It was concluded that hydroxylamine exerts hypotension partly through conversion to nitric oxide and partly by a "hydralazine-like" mechanism involving SSAO inhibition
Title: Hypotensive effect of hydroxylamine, an endogenous nitric oxide donor and SSAO inhibitor.
BZA + V treatment did not reduce HbA(1C) levels,but it reduced the elevated serum SSAO activity, decreased advanced-glycation end products and increased nitric oxide in diabetic animals.
Title: Studies on the insulinomimetic effects of benzylamine, exogenous substrate of semicarbazide-sensitive amine oxidase enzyme in streptozotocin induced diabetic rats.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Potential readthrough

Included genes: G6pc1, Psme3, Aoc2-ps1

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables aliphatic amine oxidase activity	IEA Inferred from Electronic Annotation more info
enables calcium ion binding	ISO Inferred from Sequence Orthology more info
enables copper ion binding	IBA Inferred from Biological aspect of Ancestor more info
enables copper ion binding	ISO Inferred from Sequence Orthology more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables primary methylamine oxidase activity	IDA Inferred from Direct Assay more info	PubMed
NOT enables primary methylamine oxidase activity	ISO Inferred from Sequence Orthology more info
enables primary methylamine oxidase activity	ISO Inferred from Sequence Orthology more info
enables primary methylamine oxidase activity	ISS Inferred from Sequence or Structural Similarity more info	PubMed
enables protein heterodimerization activity	ISO Inferred from Sequence Orthology more info
enables quinone binding	ISO Inferred from Sequence Orthology more info
enables quinone binding	ISS Inferred from Sequence or Structural Similarity more info	PubMed

Process	Evidence Code	Pubs
involved_in amine metabolic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in amine metabolic process	ISO Inferred from Sequence Orthology more info
involved_in amine metabolic process	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in cell adhesion	ISO Inferred from Sequence Orthology more info
involved_in cell adhesion	ISS Inferred from Sequence or Structural Similarity more info	PubMed
involved_in eating behavior	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in leukocyte migration involved in inflammatory response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of D-glucose transmembrane transport	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of acute inflammatory response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of leukocyte migration	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of blood pressure	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to immobilization stress	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in Golgi apparatus	IBA Inferred from Biological aspect of Ancestor more info
located_in Golgi apparatus	ISO Inferred from Sequence Orthology more info
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in cell surface	ISS Inferred from Sequence or Structural Similarity more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
is_active_in early endosome	IBA Inferred from Biological aspect of Ancestor more info
located_in early endosome	ISO Inferred from Sequence Orthology more info
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	ISO Inferred from Sequence Orthology more info
located_in membrane	ISS Inferred from Sequence or Structural Similarity more info	PubMed
located_in microvillus	ISO Inferred from Sequence Orthology more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISS Inferred from Sequence or Structural Similarity more info	PubMed

General protein information

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Preferred Names: amine oxidase [copper-containing] 3

Names: VAP-1; VP97; copper amine oxidase; membrane primary amine oxidase; semicarbazide-sensitive amine oxidase; vascular adhesion protein 1

NP_113770.2

EC 1.4.3.21

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_031582.3 → NP_113770.2 amine oxidase [copper-containing] 3

See identical proteins and their annotated locations for NP_113770.2

Status: PROVISIONAL

Source sequence(s)

JAXUCZ010000010

UniProtKB/Swiss-Prot

O08590, Q497D2, Q5R1T5

UniProtKB/TrEMBL

A6HJB0

Conserved Domains (4) summary

COG3733
Location:40 → 722

TynA; Cu2+-containing amine oxidase [Secondary metabolites biosynthesis, transport and catabolism]

pfam01179
Location:315 → 721

Cu_amine_oxid; Copper amine oxidase, enzyme domain

pfam02727
Location:66 → 152

Cu_amine_oxidN2; Copper amine oxidase, N2 domain

pfam02728
Location:169 → 269

Cu_amine_oxidN3; Copper amine oxidase, N3 domain