P01017 · ANGT_BOVIN
- ProteinAngiotensinogen
- GeneAGT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids476 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.
Angiotensin-2
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. Acts by binding to angiotensin receptors AGTR1 and AGTR2. Also binds the DEAR/FBXW7-AS1 receptor.
Angiotensin-3
Stimulates aldosterone release.
Angiotensin 1-7
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Biological Process | acrosome reaction | |
Biological Process | calcium-ion regulated exocytosis | |
Biological Process | positive regulation of epithelial to mesenchymal transition | |
Biological Process | regulation of apoptotic process | |
Biological Process | regulation of systemic arterial blood pressure by renin-angiotensin | |
Biological Process | vasoconstriction |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAngiotensinogen
- Alternative names
- Cleaved into 8 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP01017
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, peptide, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MAPAGLSLGAAILCLLAWAGLAAG | ||||||
Peptide | PRO_0000420641 | 25-28 | Angiotensin 1-4 | |||
Sequence: DRVY | ||||||
Peptide | PRO_0000420640 | 25-29 | Angiotensin 1-5 | |||
Sequence: DRVYV | ||||||
Peptide | PRO_0000420639 | 25-31 | Angiotensin 1-7 | |||
Sequence: DRVYVHP | ||||||
Peptide | PRO_0000032443 | 25-32 | Angiotensin-2 | |||
Sequence: DRVYVHPF | ||||||
Peptide | PRO_0000420638 | 25-33 | Angiotensin 1-9 | |||
Sequence: DRVYVHPFH | ||||||
Peptide | PRO_0000032442 | 25-34 | Angiotensin-1 | |||
Sequence: DRVYVHPFHL | ||||||
Chain | PRO_0000420642 | 25-476 | Angiotensinogen | |||
Sequence: DRVYVHPFHLLVYSKSNCDQLEKPSVETPPDPTFTPVPIQTKSSAVDEEALWEQLVRATEKLEAEDRLRASEVGLLLNFMGFHMYKTLSETWSVASGAVFSPVALFSTLTSFYVGALDPTASRLQAFLGVPGEGQGCTSRLDGHKVLSSLQTIQGLLVAQGGASSQARLLLSTVVGLFTAPGLHLKQPFVQSLSSFAPITLPRSLDLSTDPNLAAEKINRFMQSVTGWNMGRALTAVSPDSTLLFNAYVHFQGKMKGFSLLPGLKEFWVDNTTSVSVPMLSGTGIFHFWSDSQNNLSVTRVPLSANTYLLLIQPHHTPDLRKVEALTFQHNFLTRMKNLSPRAIHLTMPQLTLKASYDLQDLLAQAKLPTLLGAEANLSKISDANLRVGKVLNSVLFELKADGEQAPESVPQPAGPEALEVTLNSPFLLAVLERSSGALHFLGRVSRPLSAE | ||||||
Peptide | PRO_0000032444 | 26-32 | Angiotensin-3 | |||
Sequence: RVYVHPF | ||||||
Peptide | PRO_0000450600 | 27-32 | Angiotensin-4 | |||
Sequence: VYVHPF | ||||||
Disulfide bond | 42↔161 | |||||
Sequence: CDQLEKPSVETPPDPTFTPVPIQTKSSAVDEEALWEQLVRATEKLEAEDRLRASEVGLLLNFMGFHMYKTLSETWSVASGAVFSPVALFSTLTSFYVGALDPTASRLQAFLGVPGEGQGC | ||||||
Glycosylation | 295 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 319 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 362 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 401 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2. Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4. Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2 and can be further processed by ACE to produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4. Angiotensin 1-7 has also been proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin) (By similarity).
The disulfide bond is labile. Angiotensinogen is present in the circulation in a near 40:60 ratio with the oxidized disulfide-bonded form, which preferentially interacts with receptor-bound renin.
Keywords
- PTM
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length476
- Mass (Da)51,424
- Last updated2020-08-12 v2
- ChecksumD34978061DB96AB4
Keywords
- Technical term