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Protein

Angiotensinogen

Gene

Agt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis.By similarity
Angiotensin-2: acts directly on vascular smooth muscle as a potent vasoconstrictor, affects cardiac contractility and heart rate through its action on the sympathetic nervous system, and alters renal sodium and water absorption through its ability to stimulate the zona glomerulosa cells of the adrenal cortex to synthesize and secrete aldosterone.By similarity
Angiotensin-3: stimulates aldosterone release.By similarity
Angiotensin 1-7: is a ligand for the G-protein coupled receptor MAS1 (By similarity). Has vasodilator and antidiuretic effects (By similarity). Has an antithrombotic effect that involves MAS1-mediated release of nitric oxide from platelets.By similarity1 Publication

GO - Molecular functioni

  • angiotensin receptor binding Source: RGD
  • hormone activity Source: BHF-UCL
  • serine-type endopeptidase inhibitor activity Source: GO_Central
  • sodium channel regulator activity Source: Ensembl
  • type 1 angiotensin receptor binding Source: RGD
  • type 2 angiotensin receptor binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Vasoactive, Vasoconstrictor

Enzyme and pathway databases

ReactomeiREACT_306851. Peptide ligand-binding receptors.
REACT_309654. Metabolism of Angiotensinogen to Angiotensins.
REACT_339234. G alpha (i) signalling events.
REACT_353304. G alpha (q) signalling events.

Protein family/group databases

MEROPSiI04.953.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensinogen
Alternative name(s):
Serpin A8
Cleaved into the following 8 chains:
Alternative name(s):
Angiotensin 1-10
Angiotensin I
Short name:
Ang I
Alternative name(s):
Angiotensin 1-8
Angiotensin II
Short name:
Ang II
Alternative name(s):
Angiotensin 2-8
Angiotensin III
Short name:
Ang III
Des-Asp[1]-angiotensin II
Alternative name(s):
Angiotensin 3-8
Angiotensin IV
Short name:
Ang IV
Gene namesi
Name:Agt
Synonyms:Serpina8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi2069. Agt.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: Ensembl
  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 24241 PublicationAdd
BLAST
Chaini25 – 477453AngiotensinogenPRO_0000032468Add
BLAST
Peptidei25 – 3410Angiotensin-1PRO_0000032469
Peptidei25 – 339Angiotensin 1-9PRO_0000420674
Peptidei25 – 328Angiotensin-2PRO_0000032470
Peptidei25 – 317Angiotensin 1-7PRO_0000420675
Peptidei25 – 295Angiotensin 1-5PRO_0000420676
Peptidei25 – 284Angiotensin 1-4PRO_0000420677
Peptidei26 – 327Angiotensin-3PRO_0000032471
Peptidei27 – 326Angiotensin-4PRO_0000420678

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 1611 Publication
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

In response to low blood pressure, the enzyme renin/REN cleaves angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate of ACE (angiotensin converting enzyme) that removes a dipeptide to yield the physiologically active peptide angiotensin-2. Angiotensin-1 and angiotensin-2 can be further processed to generate angiotensin-3, angiotensin-4 (By similarity). Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2 and can be further processed by ACE to produce angiotensin 1-7, angiotensin 1-5 and angiotensin 1-4. Angiotensin 1-7 has also been proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1 by MME (neprilysin) (By similarity).By similarity
The disulfide bond is labile. Angiotensinogen is present in the circulation in a near 40:60 ratio with the oxidized disulfide-bonded form, which preferentially interacts with receptor-bound renin.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP01015.
PRIDEiP01015.

PTM databases

PhosphoSiteiP01015.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

GenevisibleiP01015. RN.

Interactioni

Protein-protein interaction databases

MINTiMINT-1522474.
STRINGi10116.ENSRNOP00000024917.

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni33 – 353Combined sources
Helixi39 – 435Combined sources
Helixi72 – 8413Combined sources
Helixi88 – 11528Combined sources
Beta strandi120 – 1245Combined sources
Helixi126 – 13813Combined sources
Helixi142 – 15110Combined sources
Helixi167 – 18115Combined sources
Beta strandi193 – 20311Combined sources
Helixi211 – 2166Combined sources
Turni217 – 2204Combined sources
Beta strandi224 – 2285Combined sources
Beta strandi231 – 2333Combined sources
Helixi235 – 25016Combined sources
Beta strandi267 – 27913Combined sources
Beta strandi282 – 2843Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi303 – 31513Combined sources
Turni316 – 3194Combined sources
Beta strandi320 – 34021Combined sources
Helixi341 – 3433Combined sources
Helixi344 – 3518Combined sources
Beta strandi353 – 3553Combined sources
Beta strandi366 – 3738Combined sources
Beta strandi375 – 3828Combined sources
Helixi383 – 3897Combined sources
Turni393 – 3964Combined sources
Helixi403 – 4053Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi416 – 42510Combined sources
Beta strandi452 – 4587Combined sources
Turni459 – 4624Combined sources
Beta strandi463 – 4719Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SMRX-ray2.00B/D/F/H30-33[»]
2WXZX-ray2.80A/C25-477[»]
2WY1X-ray3.15A/B25-477[»]
ProteinModelPortaliP01015.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01015.

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00750000117773.
HOGENOMiHOG000033941.
HOVERGENiHBG004233.
InParanoidiP01015.
KOiK09821.
OMAiRFMQAVT.
OrthoDBiEOG7QK0BN.
PhylomeDBiP01015.
TreeFamiTF343201.

Family and domain databases

InterProiIPR000227. Angiotensinogen.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
PRINTSiPR00654. ANGIOTENSNGN.
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01015-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPTGAGLKA TIFCILTWVS LTAGDRVYIH PFHLLYYSKS TCAQLENPSV
60 70 80 90 100
ETLPEPTFEP VPIQAKTSPV DEKTLRDKLV LATEKLEAED RQRAAQVAMI
110 120 130 140 150
ANFMGFRMYK MLSEARGVAS GAVLSPPALF GTLVSFYLGS LDPTASQLQV
160 170 180 190 200
LLGVPVKEGD CTSRLDGHKV LTALQAVQGL LVTQGGSSSQ TPLLQSTVVG
210 220 230 240 250
LFTAPGLRLK QPFVESLGPF TPAIFPRSLD LSTDPVLAAQ KINRFVQAVT
260 270 280 290 300
GWKMNLPLEG VSTDSTLFFN TYVHFQGKMR GFSQLTGLHE FWVDNSTSVS
310 320 330 340 350
VPMLSGTGNF QHWSDAQNNF SVTRVPLGES VTLLLIQPQC ASDLDRVEVL
360 370 380 390 400
VFQHDFLTWI KNPPPRAIRL TLPQLEIRGS YNLQDLLAQA KLSTLLGAEA
410 420 430 440 450
NLGKMGDTNP RVGEVLNSIL LELQAGEEEQ PTESAQQPGS PEVLDVTLSS
460 470
PFLFAIYERD SGALHFLGRV DNPQNVV
Length:477
Mass (Da):51,982
Last modified:July 21, 1986 - v1
Checksum:i689051A5788D693D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00094
, L00091, L00092, L00093 Genomic DNA. Translation: AAA98779.1.
BC078741 mRNA. Translation: AAH78741.1.
BC087679 mRNA. Translation: AAH87679.1.
PIRiA93945. ANRT.
RefSeqiNP_602308.1. NM_134432.2.
XP_008770819.1. XM_008772597.1.
UniGeneiRn.6319.

Genome annotation databases

EnsembliENSRNOT00000024917; ENSRNOP00000024917; ENSRNOG00000018445.
GeneIDi24179.
KEGGirno:24179.
UCSCiRGD:2069. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L00094
, L00091, L00092, L00093 Genomic DNA. Translation: AAA98779.1.
BC078741 mRNA. Translation: AAH78741.1.
BC087679 mRNA. Translation: AAH87679.1.
PIRiA93945. ANRT.
RefSeqiNP_602308.1. NM_134432.2.
XP_008770819.1. XM_008772597.1.
UniGeneiRn.6319.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SMRX-ray2.00B/D/F/H30-33[»]
2WXZX-ray2.80A/C25-477[»]
2WY1X-ray3.15A/B25-477[»]
ProteinModelPortaliP01015.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1522474.
STRINGi10116.ENSRNOP00000024917.

Chemistry

BindingDBiP01015.

Protein family/group databases

MEROPSiI04.953.

PTM databases

PhosphoSiteiP01015.

Proteomic databases

PaxDbiP01015.
PRIDEiP01015.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024917; ENSRNOP00000024917; ENSRNOG00000018445.
GeneIDi24179.
KEGGirno:24179.
UCSCiRGD:2069. rat.

Organism-specific databases

CTDi183.
RGDi2069. Agt.

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00750000117773.
HOGENOMiHOG000033941.
HOVERGENiHBG004233.
InParanoidiP01015.
KOiK09821.
OMAiRFMQAVT.
OrthoDBiEOG7QK0BN.
PhylomeDBiP01015.
TreeFamiTF343201.

Enzyme and pathway databases

ReactomeiREACT_306851. Peptide ligand-binding receptors.
REACT_309654. Metabolism of Angiotensinogen to Angiotensins.
REACT_339234. G alpha (i) signalling events.
REACT_353304. G alpha (q) signalling events.

Miscellaneous databases

EvolutionaryTraceiP01015.
NextBioi602521.
PROiP01015.

Gene expression databases

GenevisibleiP01015. RN.

Family and domain databases

InterProiIPR000227. Angiotensinogen.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
PRINTSiPR00654. ANGIOTENSNGN.
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
  2. "Common structural organization of the angiotensinogen and the alpha 1-antitrypsin genes."
    Tanaka T., Ohkubo H., Nakanishi S.
    J. Biol. Chem. 259:8063-8065(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Kidney.
  4. "Comparative studies on angiotensins. II. Structure of rat angiotensin and its identification by DNS-method."
    Nakayama T., Nakajima T., Sokabe H.
    Chem. Pharm. Bull. 20:1579-1581(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 25-34.
  5. "The antithrombotic effect of angiotensin-(1-7) involves mas-mediated NO release from platelets."
    Fraga-Silva R.A., Pinheiro S.V.B., Goncalves A.C., Alenina N., Bader M., Santos R.A.S.
    Mol. Med. 14:28-35(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF ANGIOTENSIN 1-7.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-477, DISULFIDE BOND.

Entry informationi

Entry nameiANGT_RAT
AccessioniPrimary (citable) accession number: P01015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.