ANGT_HORSE
ID ANGT_HORSE Reviewed; 14 AA.
AC P01016;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Angiotensinogen;
DE AltName: Full=Serpin A8;
DE Contains:
DE RecName: Full=Angiotensin-1;
DE AltName: Full=Angiotensin 1-10;
DE AltName: Full=Angiotensin I;
DE Short=Ang I;
DE Contains:
DE RecName: Full=Angiotensin-2;
DE AltName: Full=Angiotensin 1-8;
DE AltName: Full=Angiotensin II;
DE Short=Ang II;
DE Contains:
DE RecName: Full=Angiotensin-3;
DE AltName: Full=Angiotensin 2-8;
DE AltName: Full=Angiotensin III;
DE Short=Ang III;
DE AltName: Full=Des-Asp[1]-angiotensin II;
DE Contains:
DE RecName: Full=Angiotensin-4;
DE AltName: Full=Angiotensin 3-8;
DE AltName: Full=Angiotensin IV;
DE Short=Ang IV;
DE Contains:
DE RecName: Full=Angiotensin 1-9;
DE Contains:
DE RecName: Full=Angiotensin 1-7;
DE Contains:
DE RecName: Full=Angiotensin 1-5;
DE Contains:
DE RecName: Full=Angiotensin 1-4;
DE Flags: Fragment;
GN Name=AGT; Synonyms=SERPINA8;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=13463253; DOI=10.1084/jem.106.3.439;
RA Skeggs L.T. Jr., Kahn J.R., Lentz K., Shumway N.P.;
RT "The preparation, purification, and amino acid sequence of a polypeptide
RT renin substrate.";
RL J. Exp. Med. 106:439-453(1957).
CC -!- FUNCTION: Essential component of the renin-angiotensin system (RAS), a
CC potent regulator of blood pressure, body fluid and electrolyte
CC homeostasis. {ECO:0000250|UniProtKB:P01019}.
CC -!- FUNCTION: [Angiotensin-2]: Acts directly on vascular smooth muscle as a
CC potent vasoconstrictor, affects cardiac contractility and heart rate
CC through its action on the sympathetic nervous system, and alters renal
CC sodium and water absorption through its ability to stimulate the zona
CC glomerulosa cells of the adrenal cortex to synthesize and secrete
CC aldosterone. Acts by binding to angiotensin receptors AGTR1 and AGTR2.
CC Also binds the DEAR/FBXW7-AS1 receptor. {ECO:0000250|UniProtKB:P01015,
CC ECO:0000250|UniProtKB:P01019}.
CC -!- FUNCTION: [Angiotensin-3]: Stimulates aldosterone release.
CC {ECO:0000250|UniProtKB:P01019}.
CC -!- FUNCTION: [Angiotensin 1-7]: Is a ligand for the G-protein coupled
CC receptor MAS1. Has vasodilator and antidiuretic effects. Has an
CC antithrombotic effect that involves MAS1-mediated release of nitric
CC oxide from platelets. {ECO:0000250|UniProtKB:P11859}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:13463253}.
CC -!- PTM: In response to low blood pressure, the enzyme renin/REN cleaves
CC angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate
CC of ACE (angiotensin converting enzyme) that removes a dipeptide to
CC yield the physiologically active peptide angiotensin-2. Angiotensin-1
CC and angiotensin-2 can be further processed to generate angiotensin-3,
CC angiotensin-4. Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2
CC and can be further processed by ACE to produce angiotensin 1-7,
CC angiotensin 1-5 and angiotensin 1-4. Angiotensin 1-7 has also been
CC proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1
CC by MME (neprilysin) (By similarity). {ECO:0000250|UniProtKB:P01019}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR PIR; A92775; A01250.
DR PDB; 1ER8; X-ray; 2.00 A; I=7-13.
DR PDBsum; 1ER8; -.
DR SMR; P01016; -.
DR MEROPS; I04.005; -.
DR EvolutionaryTrace; P01016; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome; Secreted;
KW Vasoactive; Vasoconstrictor.
FT CHAIN 1..>14
FT /note="Angiotensinogen"
FT /id="PRO_0000045869"
FT PEPTIDE 1..10
FT /note="Angiotensin-1"
FT /evidence="ECO:0000269|PubMed:13463253"
FT /id="PRO_0000032453"
FT PEPTIDE 1..9
FT /note="Angiotensin 1-9"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420654"
FT PEPTIDE 1..8
FT /note="Angiotensin-2"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032454"
FT PEPTIDE 1..7
FT /note="Angiotensin 1-7"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420655"
FT PEPTIDE 1..5
FT /note="Angiotensin 1-5"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420656"
FT PEPTIDE 1..4
FT /note="Angiotensin 1-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420657"
FT PEPTIDE 2..8
FT /note="Angiotensin-3"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032455"
FT PEPTIDE 3..8
FT /note="Angiotensin-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420658"
FT NON_TER 14
SQ SEQUENCE 14 AA; 1759 MW; 2E9921F8EEEFBDD7 CRC64;
DRVYIHPFHL LVYS
