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Database: UniProt
Entry: A0A2K6RJQ0_RHIRO
LinkDB: A0A2K6RJQ0_RHIRO
Original site: A0A2K6RJQ0_RHIRO 
ID   A0A2K6RJQ0_RHIRO        Unreviewed;       485 AA.
AC   A0A2K6RJQ0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Angiotensinogen {ECO:0000256|ARBA:ARBA00015105};
DE   AltName: Full=Serpin A8 {ECO:0000256|ARBA:ARBA00033182};
GN   Name=AGT {ECO:0000313|Ensembl:ENSRROP00000041259.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000041259.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000041259.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Essential component of the renin-angiotensin system (RAS), a
CC       potent regulator of blood pressure, body fluid and electrolyte
CC       homeostasis. {ECO:0000256|ARBA:ARBA00002747}.
CC   -!- FUNCTION: Stimulates aldosterone release.
CC       {ECO:0000256|ARBA:ARBA00029380}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|ARBA:ARBA00009500, ECO:0000256|RuleBase:RU000411}.
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DR   AlphaFoldDB; A0A2K6RJQ0; -.
DR   STRING; 61622.ENSRROP00000041259; -.
DR   Ensembl; ENSRROT00000065756.1; ENSRROP00000041259.1; ENSRROG00000043839.1.
DR   GeneTree; ENSGT00890000139531; -.
DR   OMA; GWKTGCS; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005179; F:hormone activity; 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:0038166; P:angiotensin-activated signaling pathway; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; IEA:Ensembl.
DR   GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; 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:1901203; P:positive regulation of extracellular matrix assembly; 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:1902895; P:positive regulation of miRNA transcription; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:Ensembl.
DR   GO; GO:1903779; P:regulation of cardiac conduction; IEA:Ensembl.
DR   GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR   CDD; cd02054; serpinA8_AGT; 1.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 1.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 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:SF13; ANGIOTENSINOGEN; 1.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   PRINTS; PR00654; ANGIOTENSNGN.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Vasoactive {ECO:0000256|ARBA:ARBA00022858};
KW   Vasoconstrictor {ECO:0000256|ARBA:ARBA00023322}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..485
FT                   /note="Angiotensinogen"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014331387"
FT   DOMAIN          115..481
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
SQ   SEQUENCE   485 AA;  53076 MW;  48A578F6DF6B9744 CRC64;
     TQKRAPQSEM APASVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG
     KPKDPTFTPV PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM
     HSELWGVVHG ATILSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDEN CTSRLDAHKV
     LSALQAVQGL LVAQGRADGQ GQLLLSMVVG LFTAPDLHLK QPFVQGLALY APVVLPRSLD
     FTDLEVAAEK IDRFMQAVTG WKISSPLTGA SADSTVVFNT YVHFQGKMKD FSLLAEPQEF
     WVDNSTSVSV PMLSGVGTFQ HWSDSQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT
     FQQNSLNWMK KLSPRAIRLT MPRLVLRGSY DLQDLLAQAE LPAILGTELN LQKLSTDNLR
     VGKVLNSIFF ELEAAEREPT ESTRQLNRPE VLEVTLDHPF LFAVYDQSAT ALHFLGRVAN
     PLSPA
//
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