ANGT_SHEEP
ID ANGT_SHEEP Reviewed; 476 AA.
AC P20757;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 91.
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: Precursor;
GN Name=AGT; Synonyms=SERPINA8;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7765514; DOI=10.1271/bbb.58.1884;
RA Nagase M., Suzuki F., Fukamizu A., Takeda N., Takeuchi K., Murakami K.,
RA Nakamura Y.;
RT "Sequencing and expression of sheep angiotensinogen cDNA.";
RL Biosci. Biotechnol. Biochem. 58:1884-1885(1994).
RN [2]
RP PROTEIN SEQUENCE OF 25-39.
RX PubMed=3081342; DOI=10.1111/j.1432-1033.1986.tb09440.x;
RA Fernley R.T., John M., Niall H.D., Coghlan J.P.;
RT "Purification and characterization of ovine angiotensinogen.";
RL Eur. J. Biochem. 154:597-601(1986).
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:3081342}.
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 -!- PTM: The disulfide bond is labile. Angiotensinogen is present in the
CC circulation in a near 40:60 ratio with the oxidized disulfide-bonded
CC form, which preferentially interacts with receptor-bound renin (By
CC similarity). {ECO:0000250|UniProtKB:P01019}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; D17520; BAA04470.1; -; mRNA.
DR PIR; JC2318; JC2318.
DR AlphaFoldDB; P20757; -.
DR SMR; P20757; -.
DR STRING; 9940.ENSOARP00000003247; -.
DR MEROPS; I04.953; -.
DR PRIDE; P20757; -.
DR eggNOG; KOG2392; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR000227; Angiotensinogen.
DR InterPro; IPR023795; Serpin_CS.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF13; PTHR11461:SF13; 1.
DR Pfam; PF00079; Serpin; 1.
DR PRINTS; PR00654; ANGIOTENSNGN.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
DR PROSITE; PS00284; SERPIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Vasoactive; Vasoconstrictor.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3081342"
FT CHAIN 25..476
FT /note="Angiotensinogen"
FT /id="PRO_0000032472"
FT PEPTIDE 25..34
FT /note="Angiotensin-1"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032473"
FT PEPTIDE 25..33
FT /note="Angiotensin 1-9"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420679"
FT PEPTIDE 25..32
FT /note="Angiotensin-2"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032474"
FT PEPTIDE 25..31
FT /note="Angiotensin 1-7"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420680"
FT PEPTIDE 25..29
FT /note="Angiotensin 1-5"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420681"
FT PEPTIDE 25..28
FT /note="Angiotensin 1-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420682"
FT PEPTIDE 26..32
FT /note="Angiotensin-3"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032475"
FT PEPTIDE 27..32
FT /note="Angiotensin-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420683"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..161
FT /evidence="ECO:0000250"
SQ SEQUENCE 476 AA; 51304 MW; C8A517CD9FA029F7 CRC64;
MAPAGLSLGA TILCLLAWAG LAAGDRVYIH PFHLLVHSKS NCDQLEKPSV ETPADPTLTP
VPIQTKSSPV DEEALWEQLV RATEKLEAED RLRASEVGLL LNFMGFHVYK TLSETWSVAS
GLVFSPVALF STLTSFYTGA LDPTASRLQA FLGVPGEGQG CTSRLDGRKV LSSLQTIQGL
LVAPGGASSQ ARLLLSTVVG LFTAPGLHLK QPFVQGLSSF APITLPRSLD LSTDPNLAAE
KINRFMHSAT GWNMGRPLAA ASPDSTLLFN AYVHFQGKMK GFSLLPGLTE FWVDNTTSVP
VPMLSGSGTF HYWSDNQNHL SMTRVPLSAN GYLLLIQPHH TLDLRKVEAL IFQHNFLTRM
KNLSPRAIHL TVPQLTLKAS YDLQDLLAQA KLPTLLGAEA NLGKISDANL RVGKVLNSVL
FELKADGEQA PESVPQPAGP EALEVTLNSP FLLAVLERSS GALHFLGRVS RPLSAE
