ID   ANGT_COTJA              Reviewed;          10 AA.
AC   P67886; P01018;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Angiotensinogen;
DE   AltName: Full=Serpin A8;
DE   Contains:
DE     RecName: Full=Angiotensin-1;
DE     AltName: Full=Angiotensin I;
DE              Short=Ang I;
DE   Contains:
DE     RecName: Full=Angiotensin-2;
DE     AltName: Full=Angiotensin II;
DE              Short=Ang II;
DE   Contains:
DE     RecName: Full=Angiotensin-3;
DE     AltName: Full=Angiotensin III;
DE              Short=Ang III;
DE     AltName: Full=Des-Asp[1]-angiotensin II;
DE   Flags: Fragment;
GN   Name=AGT; Synonyms=SERPINA8;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2191893; DOI=10.1016/0016-6480(90)90083-x;
RA   Takei Y., Hasegawa Y.;
RT   "Vasopressor and depressor effects of native angiotensins and inhibition of
RT   these effects in the Japanese quail.";
RL   Gen. Comp. Endocrinol. 79:12-22(1990).
CC   -!- FUNCTION: In response to lowered blood pressure, the enzyme renin
CC       cleaves angiotensin-1, from angiotensinogen. ACE (angiotensin
CC       converting enzyme) then removes a dipeptide to yield the
CC       physiologically active peptide angiotensin-2, the most potent pressor
CC       substance known, which helps regulate volume and mineral balance of
CC       body fluids. {ECO:0000250|UniProtKB:P01019}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:2191893}.
CC   -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR   PIR; A60624; A60624.
DR   Proteomes; UP000694412; 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   Direct protein sequencing; Reference proteome; Secreted; Vasoactive;
KW   Vasoconstrictor.
FT   PEPTIDE         1..10
FT                   /note="Angiotensin-1"
FT                   /evidence="ECO:0000269|PubMed:2191893"
FT                   /id="PRO_0000032479"
FT   PEPTIDE         1..8
FT                   /note="Angiotensin-2"
FT                   /evidence="ECO:0000250|UniProtKB:P01019"
FT                   /id="PRO_0000032480"
FT   PEPTIDE         2..8
FT                   /note="Angiotensin-3"
FT                   /evidence="ECO:0000250|UniProtKB:P01019"
FT                   /id="PRO_0000032481"
FT   NON_TER         10
SQ   SEQUENCE   10 AA;  1232 MW;  CEFBEDD761F2DB42 CRC64;
     DRVYVHPFSL