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Acts by binding to angiotensin receptors AGTR1 and AGTR2 (PubMed:1567413). Also binds the DEAR/FBXW7-AS1 receptor (By similarity)"}],"commentType":"FUNCTION","molecule":"Angiotensin-2"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1132082"}],"value":"Stimulates aldosterone release"}],"commentType":"FUNCTION","molecule":"Angiotensin-3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P11859"}],"value":"Is a ligand for the G protein-coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects. Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets (By similarity)"}],"commentType":"FUNCTION","molecule":"Angiotensin 1-7"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20927107"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7539791"}],"value":"During pregnancy, exists as a disulfide-linked 2:2 heterotetramer with the proform of PRG2 and as a complex (probably a 2:2:2 heterohexamer) with pro-PRG2 and C3dg"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"Q9UI10","geneName":"EIF2B4","intActId":"EBI-2340132"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"O00746","geneName":"NME4","intActId":"EBI-744871"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"C9J082","geneName":"NPHP1","intActId":"EBI-25830675"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"O14744","geneName":"PRMT5","intActId":"EBI-351098"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"Q8TAS3","geneName":"PRRG2","intActId":"EBI-10272071"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"P00797","geneName":"REN","intActId":"EBI-715794"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"Q8IYM2","geneName":"SLFN12","intActId":"EBI-2822550"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"Q9UMY4","geneName":"SNX12","intActId":"EBI-1752602"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"O43493-5","geneName":"TGOLN2","intActId":"EBI-25830716"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"Q8NFB2","geneName":"TMEM185A","intActId":"EBI-21757569"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"Q8N0U8","geneName":"VKORC1L1","intActId":"EBI-11337915"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"P25095","geneName":"Agtr1","intActId":"EBI-764979"},"numberOfExperiments":10,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P01019","intActId":"EBI-751728"},"interactantTwo":{"uniProtKBAccession":"Q10714","geneName":"Ance","intActId":"EBI-115736"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000032457","intActId":"EBI-25493366"},"interactantTwo":{"uniProtKBAccession":"Q9BYF1","geneName":"ACE2","intActId":"EBI-7730807"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000032458","intActId":"EBI-6622938"},"interactantTwo":{"uniProtKBAccession":"Q9BYF1","geneName":"ACE2","intActId":"EBI-7730807"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000032458","intActId":"EBI-6622938"},"interactantTwo":{"uniProtKBAccession":"P30556","geneName":"AGTR1","intActId":"EBI-6623016"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000032459","intActId":"EBI-2927577"},"interactantTwo":{"uniProtKBAccession":"P50052","geneName":"AGTR2","intActId":"EBI-1748067"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"4300938"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7259779"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7539791"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1692023"}],"value":"Expressed by the liver and secreted in plasma"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17138938"}],"value":"Beta-decarboxylation of Asp-25 in angiotensin-2, by mononuclear leukocytes produces alanine (PubMed:17138938). The resulting peptide form, angiotensin-A, has the same affinity for the AT1 receptor as angiotensin-2, but a higher affinity for the AT2 receptor (PubMed:17138938)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10969042"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11815627"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12045255"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15283675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"4322742"}],"value":"In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1 (PubMed:12045255). Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2 (PubMed:10969042, PubMed:4322742). Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4 (PubMed:10969042, PubMed:11815627). 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 (PubMed:10969042, PubMed:11815627). Angiotensin 1-7 has also been proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin) (PubMed:15283675)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20927107"}],"value":"The disulfide bond is labile. 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