ANGT_CALJA
ID ANGT_CALJA Reviewed; 477 AA.
AC Q9TSZ0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 89.
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=ANGT, SERPINA8;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10598135; DOI=10.1097/00005344-199912000-00018;
RA Valdenaire O., Breu V., Giller T., Bur D., Fischli W.;
RT "Cloning and characterization of marmoset renin: comparison with human
RT renin.";
RL J. Cardiovasc. Pharmacol. 34:893-897(1999).
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:0000250|UniProtKB:P01019}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB64880.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ132343; CAB64880.1; ALT_INIT; mRNA.
DR RefSeq; NP_001171966.1; NM_001185037.1.
DR AlphaFoldDB; Q9TSZ0; -.
DR STRING; 9483.ENSCJAP00000022002; -.
DR GeneID; 100389395; -.
DR KEGG; cjc:100389395; -.
DR CTD; 183; -.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; Q9TSZ0; -.
DR OrthoDB; 450590at2759; -.
DR Proteomes; UP000008225; 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 CDD; cd02054; serpinA8_AGT; 1.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR000227; Angiotensinogen.
DR InterPro; IPR033834; Angiotensinogen_serpin_dom.
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:SF331; PTHR11461:SF331; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
KW Vasoactive; Vasoconstrictor.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..477
FT /note="Angiotensinogen"
FT /id="PRO_0000032445"
FT PEPTIDE 25..34
FT /note="Angiotensin-1"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032446"
FT PEPTIDE 25..33
FT /note="Angiotensin 1-9"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420644"
FT PEPTIDE 25..32
FT /note="Angiotensin-2"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032447"
FT PEPTIDE 25..31
FT /note="Angiotensin 1-7"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420645"
FT PEPTIDE 25..29
FT /note="Angiotensin 1-5"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420646"
FT PEPTIDE 25..28
FT /note="Angiotensin 1-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420647"
FT PEPTIDE 26..32
FT /note="Angiotensin-3"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032448"
FT PEPTIDE 27..32
FT /note="Angiotensin-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420648"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..162
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 52290 MW; E24D52022176BED6 CRC64;
MPPASMSLRV TILCLLAWAG LAAGDRVYIH PFHLVIHNES TCEELAKANA GKPEDPTFTP
ALIQAKSLPV DEKALQDQLV LVAAKLNAED KLRAATVGML ANFLSFHIYS MHSELWGMVQ
GATILSPMAV FGTLASLYLG ASNHTAYRLQ AILGVPWKDE NCTSRLDAHK VLSALQAVQG
LLVAQDRAEG QTQLLLSTVV GLFTAPGLHL KQPFVQGLAL YAPAVLPRSL DFSTDLDVAA
EKIDRFMQAV TGWKVSSPLT GASADSNLVF NTYVHFQGKM KGFSLLAEPQ EFWVDNSTSV
SVPMLSGMGT FQHWSDAQDK FSVTQVPFTE SACLLLIQPH YASDLDKVEG LTFQQNSLNW
MNKLSPRAIH LTMPRLVLRG SYDLQDLLAQ AELPTILGTE LNLQKMSNNN LRVGKVLNSI
FFELEADEKE PTESTQQPKG PEVLELNLNH PFLFAVYDQD ATALYFLGRV ANPLTTV
