ANGT_BOVIN
ID ANGT_BOVIN Reviewed; 476 AA.
AC P01017; A0A3Q1LGY9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 25-34.
RX PubMed=13403900; DOI=10.1042/bj0650246;
RA Elliott D.F., Peart W.S.;
RT "The amino acid sequence in a hypertensin.";
RL Biochem. J. 65:246-254(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:13403900}.
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.
CC {ECO:0000250|UniProtKB:P01019}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR PIR; A90345; A90345.
DR PDB; 1GVU; X-ray; 0.94 A; I=30-37.
DR PDB; 3ER5; X-ray; 1.80 A; I=6-9.
DR PDBsum; 1GVU; -.
DR PDBsum; 3ER5; -.
DR AlphaFoldDB; P01017; -.
DR SMR; P01017; -.
DR IntAct; P01017; 2.
DR MEROPS; I04.953; -.
DR Ensembl; ENSBTAT00000072571; ENSBTAP00000057860; ENSBTAG00000012393.
DR VEuPathDB; HostDB:ENSBTAG00000012393; -.
DR VGNC; VGNC:103718; AGT.
DR GeneTree; ENSGT00890000139531; -.
DR OMA; FMGFRMY; -.
DR EvolutionaryTrace; P01017; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000012393; Expressed in prefrontal cortex and 83 other tissues.
DR ExpressionAtlas; P01017; baseline.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl.
DR GO; GO:0031703; F:type 2 angiotensin receptor binding; IEA:Ensembl.
DR GO; GO:0007340; P:acrosome reaction; IMP:UniProtKB.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IEA:Ensembl.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:1903779; P:regulation of cardiac conduction; IEA:Ensembl.
DR GO; GO:1901201; P:regulation of extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IEA:InterPro.
DR GO; GO:0003014; P:renal system process; IEA:Ensembl.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Vasoactive; Vasoconstrictor.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..476
FT /note="Angiotensinogen"
FT /evidence="ECO:0000255"
FT /id="PRO_0000420642"
FT PEPTIDE 25..34
FT /note="Angiotensin-1"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032442"
FT PEPTIDE 25..33
FT /note="Angiotensin 1-9"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420638"
FT PEPTIDE 25..32
FT /note="Angiotensin-2"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032443"
FT PEPTIDE 25..31
FT /note="Angiotensin 1-7"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420639"
FT PEPTIDE 25..29
FT /note="Angiotensin 1-5"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420640"
FT PEPTIDE 25..28
FT /note="Angiotensin 1-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420641"
FT PEPTIDE 26..32
FT /note="Angiotensin-3"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032444"
FT PEPTIDE 27..32
FT /note="Angiotensin-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000450600"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..161
FT /evidence="ECO:0000250|UniProtKB:P01019"
SQ SEQUENCE 476 AA; 51424 MW; D34978061DB96AB4 CRC64;
MAPAGLSLGA AILCLLAWAG LAAGDRVYVH PFHLLVYSKS NCDQLEKPSV ETPPDPTFTP
VPIQTKSSAV DEEALWEQLV RATEKLEAED RLRASEVGLL LNFMGFHMYK TLSETWSVAS
GAVFSPVALF STLTSFYVGA LDPTASRLQA FLGVPGEGQG CTSRLDGHKV LSSLQTIQGL
LVAQGGASSQ ARLLLSTVVG LFTAPGLHLK QPFVQSLSSF APITLPRSLD LSTDPNLAAE
KINRFMQSVT GWNMGRALTA VSPDSTLLFN AYVHFQGKMK GFSLLPGLKE FWVDNTTSVS
VPMLSGTGIF HFWSDSQNNL SVTRVPLSAN TYLLLIQPHH TPDLRKVEAL TFQHNFLTRM
KNLSPRAIHL TMPQLTLKAS YDLQDLLAQA KLPTLLGAEA NLSKISDANL RVGKVLNSVL
FELKADGEQA PESVPQPAGP EALEVTLNSP FLLAVLERSS GALHFLGRVS RPLSAE
