Target has curated data in GtoImmuPdb
Contents:
- Gene and Protein Information
- Previous and Unofficial Names
- Database Links
- Selected 3D Structures
- Natural/Endogenous Ligands
- Agonists
- Antagonists
- Immunopharmacology Comments
- Immuno Process Associations
- Transduction Mechanisms
- Tissue Distribution
- Expression Datasets
- Functional Assays
- Physiological Functions
- Physiological Consequences of Altering Gene Expression
- Phenotypes, Alleles and Disease Models
- Clinically-Relevant Mutations and Pathophysiology
- Biologically Significant Variants
- General Comments
- References
- Contributors
- How to cite this page
Gene and Protein Information  |
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| class A G protein-coupled receptor | ||||||
| Species | TM | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
| Human | 7 | 363 | Xq23 | AGTR2 | angiotensin II receptor type 2 | 50,91 |
| Mouse | 7 | 363 | X 16.71 cM | Agtr2 | angiotensin II receptor, type 2 | 36 |
| Rat | 7 | 363 | Xq34 | Agtr2 | angiotensin II receptor, type 2 | 91 |
| Previous and Unofficial Names |
| MRX88 | angiotensin receptor 2 | angiotensin II type 2 receptor | AT2R | AT2-R | AT2 receptor | Agtr2 | angiotensin II receptor, type 2 | angiotensin II receptor |
| Database Links |
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| Specialist databases | |
| GPCRdb | agtr2_human (Hs), agtr2_mouse (Mm), agtr2_rat (Rn) |
| Other databases | |
| Alphafold | P50052 (Hs), P35374 (Mm), P35351 (Rn) |
| ChEMBL Target | CHEMBL4607 (Hs), CHEMBL4680025 (Mm), CHEMBL257 (Rn) |
| Ensembl Gene | ENSG00000180772 (Hs), ENSMUSG00000068122 (Mm), ENSRNOG00000050006 (Rn) |
| Entrez Gene | 186 (Hs), 11609 (Mm), 24182 (Rn) |
| Human Protein Atlas | ENSG00000180772 (Hs) |
| KEGG Gene | hsa:186 (Hs), mmu:11609 (Mm), rno:24182 (Rn) |
| OMIM | 300034 (Hs) |
| Orphanet | ORPHA159921 (Hs) |
| Pharos | P50052 (Hs) |
| RefSeq Nucleotide | NM_000686 (Hs), NM_007429 (Mm), NM_012494 (Rn) |
| RefSeq Protein | NP_000677 (Hs), NP_031455 (Mm), NP_036626 (Rn) |
| UniProtKB | P50052 (Hs), P35374 (Mm), P35351 (Rn) |
| Wikipedia | AGTR2 (Hs) |
| Selected 3D Structures |
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| Natural/Endogenous Ligands |
| angiotensin-(1-7) {Sp: Human, Mouse, Rat} |
| angiotensin II {Sp: Human, Mouse, Rat} |
| angiotensin III {Sp: Human, Mouse, Rat} |
Download all structure-activity data for this target as a CSV file 
| Agonists | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| View species-specific agonist tables | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Agonist Comments | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| The natural ligands Ang II and Ang III do not distinguish between the AT1 and AT2 receptors. CGP42112 behaves like an AT1 antagonist at high concentration (Ki 1.7 µM) [12,19]. It was previously thought that Ang I was a natural ligand for AT2R, but this is incorrect. The binding of tissue expressing exclusively the AT2 receptor is not affected by GTP or its analogues [11]. In contrast, an AT2 receptor sensitive to GTPgS and pertussis toxin has been identified in rat brain [92]. β-Amino acid substitution of Ang III congeners for AT2R are reported: β-Arg2Ang III (IC50 2060 nM), β-Val3Ang III (IC50 2350 nM), β-Tyr4Ang III (IC50 1.82 nM), β-Pro7Ang III (IC50 0.47 nM) and β-Phe8Ang III (IC50 20.3 nM); IC50 values derived using HEK293 cells expressing hAT2R. These are specific AT2R agonists [52]. NP-6A4, a selective peptide agonist for AT2R (activity not reported) was shown to reduce aortic stiffness [79]. |
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| Antagonists | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| View species-specific antagonist tables | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Antagonist Comments | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Saralasin is a non specific antagonist, which does not distinguish the AT1 and AT2 receptors [18]. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Immunopharmacology Comments |
| AT2 receptors have been have been identified on human immunocompetent cells, and selective AT2 receptor activation stimulates an anti-inflammatory effect (reduces production of pro-inflammatory cytokines TNFα, IL-6, and IL-10 after LPS challenge) in human monocytes [60]. Experimental work indicates that AT1 and AT2 receptors can modulate the inflammatory NFκB pathway [26-27], and AT2 receptors play a role in the recruitment of inflammatory cells. Accumulating evidence suggests that regulation of the mutually antagonistic angiotensin receptors AT1 and AT2 is an essential process in the control of inflammation and that an imbalance between these two receptors has pathophysiological potential [83]. Existing anti-hypertensive drugs could be used to investigate the effect of manipulating the angiotensin system on a variety of diseases. |
| Immuno Process Associations | ||
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| Primary Transduction Mechanisms
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| Transducer | Effector/Response |
| Gi/Go family |
Phospholipase A2 stimulation Other - See Comments |
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Comments:
The AT2 receptor appear to bind to Gia2 or Gia3 [116]. Depending on the tissues, activation of the AT2 receptor 1) stimulates Tyr and Ser/Thr phosphatases (MKP-1, PP2A, SHP-1) and protein dephosphorylation, 2) regulates the nitric-oxide-cGMP system 3) stimulates phospholipase A2, release arachidonic acid and activates the Na+/HCO3 symporter [20,40,69] 4) inhibits autophagy [73] 5) modulates sympatho-excitation in hypertrophy-heart failure model [32]. Ligand-independent AT2 action results in the induction of apoptosis. Constitutive signal transduction of AT2 [64]: 1) increased bradykinin and iNOS protein expression in VSMCs [46] 2) stimulation of apoptosis in prostate cancer cells [56] 3) increased bradykinin release in mouse coronary artery endothelial cells [119]. G-protein independent signalling: AT2 does not require phosphorylation or heterotrimeric Gαβγ protein to be active [28]. |
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| References: 34,57,116 | |
| Secondary Transduction Mechanisms |
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| Transducer | Effector/Response |
| Gi/Go family | Other - See Comments |
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Comments:
Activation of the AT2 receptor leads to MAP kinase inactivation, opening of delayed-rectifier K channel and closing of T-type Ca channels [14,120] Intracellular storage of AT2R [64]. While antagonism of AT1 mediated signal and function were generally observed, there are several exceptions and conflicting findings (cardiac hypertrophy, etc). Potential mechanisms of the interference include interaction and/or binding between AT2 and AT1 or competing AngII binding. |
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| Tissue Distribution
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| Expression Datasets |
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| Functional Assays
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| Physiological Functions
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| Physiological Consequences of Altering Gene Expression
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| Phenotypes, Alleles and Disease Models
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Mouse data from MGI | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Clinically-Relevant Mutations and Pathophysiology
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| Biologically Significant Variants
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| Biologically Significant Variant Comments | ||||||||||
| For other AGTR2 SNPs, please see the entry for this gene on dbSNP. |
| General Comments |
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The ATGR2 appears to be re-expressed or up-regulated after vascular injury, myocardial infarction, cardiac failure or wound healing, possibly reflecting re-activation of a foetal genetic programme [20-21,38,59] Preclinical in vitro and in vivo studies indicated that the AT2 receptor counterbalances the effect of the AT1 receptor [20,59,63,65-66]. The most relevant transcription factor binding sites in the AGTR2 gene promoter: Most relevant TFs: AP-1, ATF-2, IRF-1, CREB, PPAR-γ1, δCREB, PPAR-γ2, c-Jun. MiRNAs Predicted to Target AGTR2 3’-UTR: Predicted miRNAs. Both conserved and poorly conserved sites are shown [30,55]. |
References
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2. Akishita M, Iwai M, Wu L, Zhang L, Ouchi Y, Dzau VJ, Horiuchi M. (2000) Inhibitory effect of angiotensin II type 2 receptor on coronary arterial remodeling after aortic banding in mice. Circulation, 102 (14): 1684-9. [PMID:11015348]
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