Angiotensinogen (AGT)
The protein contains 485 amino acids for an estimated molecular weight of 53154 Da.
Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.', 'acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone.', 'stimulates aldosterone release.', 'is a ligand for the G-protein coupled receptor MAS1. Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets. (updated: Dec. 11, 2019)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is predicted to be membranous by TOPCONS.
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No binding partner found
Biological Process
Activation of MAPK activity
Activation of phospholipase C activity
Aging
Angiotensin-activated signaling pathway
Angiotensin-mediated drinking behavior
Artery smooth muscle contraction
Associative learning
Blood vessel remodeling
Cell growth involved in cardiac muscle cell development
Cell surface receptor signaling pathway
Cell-cell signaling
Cellular response to angiotensin
Cellular response to mechanical stimulus
Cellular sodium ion homeostasis
Cytokine secretion
ERK1 and ERK2 cascade
Female pregnancy
Fibroblast proliferation
G protein-coupled receptor signaling pathway
G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger
Kidney development
Low-density lipoprotein particle remodeling
Maintenance of blood vessel diameter homeostasis by renin-angiotensin
Negative regulation of angiogenesis
Negative regulation of cell growth
Negative regulation of endopeptidase activity
Negative regulation of gene expression
Negative regulation of MAP kinase activity
Negative regulation of neurotrophin TRK receptor signaling pathway
Negative regulation of sodium ion transmembrane transporter activity
Negative regulation of tissue remodeling
Nitric oxide mediated signal transduction
Operant conditioning
Phospholipase C-activating G protein-coupled receptor signaling pathway
Positive regulation of activation of Janus kinase activity
Positive regulation of blood pressure
Positive regulation of branching involved in ureteric bud morphogenesis
Positive regulation of cardiac muscle cell apoptotic process
Positive regulation of cardiac muscle hypertrophy
Positive regulation of cellular protein metabolic process
Positive regulation of cholesterol esterification
Positive regulation of cytokine production
Positive regulation of cytosolic calcium ion concentration
Positive regulation of endothelial cell migration
Positive regulation of epidermal growth factor receptor signaling pathway
Positive regulation of extracellular matrix constituent secretion
Positive regulation of extrinsic apoptotic signaling pathway
Positive regulation of fibroblast proliferation
Positive regulation of gap junction assembly
Positive regulation of inflammatory response
Positive regulation of insulin receptor signaling pathway
Positive regulation of L-arginine import across plasma membrane
Positive regulation of L-lysine import across plasma membrane
Positive regulation of macrophage derived foam cell differentiation
Positive regulation of membrane hyperpolarization
Positive regulation of NAD(P)H oxidase activity
Positive regulation of neuron projection development
Positive regulation of NF-kappaB transcription factor activity
Positive regulation of nitric oxide biosynthetic process
Positive regulation of peptidyl-tyrosine phosphorylation
Positive regulation of phosphatidylinositol 3-kinase signaling
Positive regulation of protein tyrosine kinase activity
Positive regulation of reactive oxygen species metabolic process
Positive regulation of renal sodium excretion
Positive regulation of superoxide anion generation
Positive regulation of transcription, DNA-templated
Positive regulation of vascular associated smooth muscle cell migration
Positive regulation of vascular associated smooth muscle cell proliferation
Protein import into nucleus
Regulation of blood pressure
Regulation of blood volume by renin-angiotensin
Regulation of calcium ion transport
Regulation of cardiac conduction
Regulation of cell growth
Regulation of cell population proliferation
Regulation of extracellular matrix assembly
Regulation of heart rate
Regulation of lipid metabolic process
Regulation of long-term neuronal synaptic plasticity
Regulation of metabolic process
Regulation of norepinephrine secretion
Regulation of renal output by angiotensin
Regulation of renal sodium excretion
Regulation of transmission of nerve impulse
Regulation of vasoconstriction
Renal system process
Renin-angiotensin regulation of aldosterone production
Response to estradiol
Response to muscle activity involved in regulation of muscle adaptation
Smooth muscle cell proliferation
Stress-activated MAPK cascade
Uterine smooth muscle contraction
Vasoconstriction
Vasodilation
The reference OMIM entry for this protein is 106150
Angiotensinogen; agt
Serpina8 iga nephropathy, progression to renal failure in, susceptibility to, included
Angiotensin i, included
Angiotensin ii, included
DESCRIPTION
Angiotensin is formed from a precursor, angiotensinogen, which is produced by the liver and found in the alpha-globulin fraction of plasma. The lowering of blood pressure is a stimulus to secretion of renin (179820) by the kidney into the blood. Renin cleaves from angiotensinogen a terminal decapeptide, angiotensin I. This is further altered by the enzymatic removal of a dipeptide to form angiotensin II.CLONING
Ohkubo et al. (1983) determined the sequence of the cloned rat angiotensinogen gene. The human angiotensinogen molecule has a molecular mass of about 50 kD. The angiotensin I decapeptide is located in its N-terminal part. Kageyama et al. (1984) reported the complete nucleotide sequence of human angiotensinogen mRNA. Similarly, Kunapuli et al. (1987) isolated cDNA clones for human angiotensinogen from a human liver library. The determined nucleotide sequence corroborated the sequence published by Kageyama et al. (1984), with the exception of a single nucleotide change which may represent a simple genetic polymorphism. Kunapuli et al. (1987) constructed a full-length angiotensinogen cDNA which enabled the in vitro synthesis of human angiotensinogen in E. coli. Gaillard et al. (1989) observed that the primary amino acid sequence shows similarities to that of alpha-1-antitrypsin (AAT; 107400) and antithrombin III (AT3; 107300).GENE STRUCTURE
Gaillard et al. (1989) found that the human angiotensinogen gene contains 5 exons. The angiotensinogen gene shows organization identical to that of the AAT gene, but different from that of the AT3 gene.MAPPING
By in situ hybridization, Gaillard-Sanchez et al. (1990) assigned the angiotensinogen gene to 1q4 in the same region as the renin gene. Isa et al. (1989, 1990) used a human angiotensinogen cDNA plasmid probe to localize the gene by nonisotopic in situ hybridization; the location was determined to be 1q42-q43. By screening a panel of human-mouse somatic cell hybrids, Abonia et al. (1993) confirmed the assignment of the AGT locus to chromosome 1. They showed, furthermore, that the homologous gene in the mouse is on the distal end of chromosome 8; a short region of conserved linkage homology between mouse chromosome 8 and human chromosome 1 was indicated by the mapping also of the skeletal alpha-actin locus (102610) to mouse chromosome 8 and human chromosome 1.GENE FUNCTION
Karlsson et al. (1998) analyzed the expression of angiotensinogen and enzymes required for its conversion to angiotensin II in human adipose tissue. Northern blot analysis demonstrated angiotensinogen expression in adipose tissue from 9 obese subjects. Western blot analysis showed a distinct band of expected size of the angiotensinogen protein (61 kD) in isolated adipocytes. RT-PCR and Southern blot analysis demonstrated renin expression in human adipose tissue. Angiotensin-converting enzyme mRNA was detected by RT-PCR, and the identity of the PCR products was verified by restriction enzyme cleavage. Transcripts for cathepsin D (116840) and cathepsin G (116830), components of the nonrenin-angiotensin systems, were detected by RT-PCR and verified by restriction enzyme cleavage. The authors concluded that human adipose tissue expresses angiotensinogen and enzymes of renin- and nonrenin-angiotensin systems. Hypertrophy is a fundamental adaptive process occurring in postmitotic cardiac and skeletal muscle in response to mechanical load. Using an in vitro mod ... More on the omim web site
June 29, 2020: Protein entry updated
Automatic update: OMIM entry 106150 was added.
Jan. 22, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).