Type-1 angiotensin II receptor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P30556 (AGTR1_HUMAN)

Last modified July 22, 2008. Version 85. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Type-1 angiotensin II receptor
Alternative name(s):
    AT1
    AT1AR
    AT1BR

Gene names

Name:	AGTR1
Synonyms:	AGTR1A, AGTR1B, AT2R1, AT2R1B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Liver, lung, adrenal and adrenocortical adenomas.
Post-translational modification	C-terminal Ser or Thr residues may be phosphorylated.
Involvement in disease	Defects in AGTR1 are a cause of renal tubular dysgenesis (RTD) [MIM:267430]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

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Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transmembrane
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	calcium-mediated signaling Ref.3 Inferred from direct assay. Source: UniProtKB elevation of cytosolic calcium ion concentration during G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) Ref.3 Inferred from direct assay. Source: UniProtKB kidney development Ref.11 Inferred from mutant phenotype. Source: UniProtKB oxygen and reactive oxygen species metabolic process Traceable author statement. Source: UniProtKB positive regulation of NAD(P)H oxidase activity Traceable author statement. Source: UniProtKB positive regulation of inflammatory response Traceable author statement. Source: UniProtKB regulation of blood vessel size by renin-angiotensin Inferred by curator. Source: UniProtKB regulation of cell growth Non-traceable author statement. Source: UniProtKB regulation of cell proliferation Non-traceable author statement. Source: UniProtKB regulation of natriuresis Non-traceable author statement. Source: UniProtKB regulation of vasoconstriction Ref.1 Inferred from direct assay. Source: UniProtKB regulation of vasodilation Ref.1 Inferred by curator. Source: UniProtKB renin-angiotensin regulation of aldosterone production Non-traceable author statement. Source: UniProtKB
Cellular component	integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc
Molecular function	angiotensin type I receptor activity Ref.1 Inferred from direct assay. Source: UniProtKB angiotensin type II receptor activity Ref.3 Ref.6 Non-traceable author statement. Source: UniProtKB bradykinin receptor binding Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 359

359

Type-1 angiotensin II receptor

Regions

Topological domain

1 – 27

Extracellular Potential

Transmembrane

28 – 52

1 Potential

Topological domain

53 – 64

Cytoplasmic Potential

Transmembrane

65 – 87

2 Potential

Topological domain

88 – 102

Extracellular Potential

Transmembrane

103 – 124

3 Potential

Topological domain

125 – 142

Cytoplasmic Potential

Transmembrane

143 – 162

4 Potential

Topological domain

163 – 192

Extracellular Potential

Transmembrane

193 – 214

5 Potential

Topological domain

215 – 240

Cytoplasmic Potential

Transmembrane

241 – 262

6 Potential

Topological domain

263 – 275

Extracellular Potential

Transmembrane

276 – 296

7 Potential

Topological domain

297 – 359

Cytoplasmic Potential

Amino acid modifications

Lipidation

355

S-palmitoyl cysteine Potential

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

176

N-linked (GlcNAc...) Potential

Glycosylation

188

N-linked (GlcNAc...) Potential

Disulfide bond

101 ↔ 180

By similarity

Natural variations

Natural variant

L → V: dbSNP rs2011425.

Natural variant

163

A → T: dbSNP rs12721226.

Natural variant

244

A → S: dbSNP rs12721225.

Natural variant

282

T → M in RTD.

Natural variant

289

C → W: dbSNP rs1064533.

Natural variant

336

T → P: dbSNP rs1801021.

Experimental info

Sequence conflict

187

Q → R in BAA02968. Ref.6

Sequence conflict

204 – 205

FL → SC in BAA02968. Ref.6

Sequence conflict

232

K → N in BAA02968. Ref.6

Sequence conflict

240

K → R in BAA02968. Ref.6

Sequence conflict

268

L → Q in BAA02968. Ref.6

Sequence conflict

311 – 313

RYF → KDI in BAA02968. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

P30556-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 35FC856F53E911A6
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FASTA

359

41,061

        10         20         30         40         50         60 
MILNSSTEDG IKRIQDDCPK AGRHNYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK 

        70         80         90        100        110        120 
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYRWPFGNYL CKIASASVSF NLYASVFLLT 

       130        140        150        160        170        180 
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLLAGLAS LPAIIHRNVF FIENTNITVC 

       190        200        210        220        230        240 
AFHYESQNST LPIGLGLTKN ILGFLFPFLI ILTSYTLIWK ALKKAYEIQK NKPRNDDIFK 

       250        260        270        280        290        300 
IIMAIVLFFF FSWIPHQIFT FLDVLIQLGI IRDCRIADIV DTAMPITICI AYFNNCLNPL 

       310        320        330        340        350 
FYGFLGKKFK RYFLQLLKYI PPKAKSHSNL STKMSTLSYR PSDNVSSSTK KPAPCFEVE

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References

[1]	"Cloning, expression, and characterization of a gene encoding the human angiotensin II type 1A receptor." Mauzy C.A., Hwang O., Egloff A.M., Wu L.H., Chung F.-Z. Biochem. Biophys. Res. Commun. 186:277-284(1992) [PubMed: 1378723] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular cloning and sequencing of the gene encoding human angiotensin II type 1 receptor." Furuta H., Guo D.F., Inagami T. Biochem. Biophys. Res. Commun. 183:8-13(1992) [PubMed: 1543512] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lymphocyte.
[3]	"Cloning and characterization of a human angiotensin II type 1 receptor." Bergsma D.J., Ellis C., Kumar C., Nuthalaganti P., Kersten H., Elshourbagy N.A., Griffin E., Stadel J.M., Aiyar N. Biochem. Biophys. Res. Commun. 183:989-995(1992) [PubMed: 1567413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Molecular cloning, sequence analysis and expression of a cDNA encoding human type-1 angiotensin II receptor." Takayanagi R., Ohnaka K., Sakai Y., Nakao R., Yanase T., Haji M., Inagami T., Furuta H., Gou D.F., Nakamuta M., Nawata H. Biochem. Biophys. Res. Commun. 183:910-916(1992) [PubMed: 1550596] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[5]	"Genetic analysis of the human type-1 angiotensin II receptor." Curnow K.M., Pascoe L., White P.C. Mol. Endocrinol. 6:1113-1118(1992) [PubMed: 1508224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Novel subtype of human angiotensin II type 1 receptor: cDNA cloning and expression." Konishi H., Kuroda S., Inada Y., Fujisawa Y. Biochem. Biophys. Res. Commun. 199:467-474(1994) [PubMed: 8135787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT TRP-289. Tissue: Placenta.
[7]	"Type 1 angiotensin II receptors of adrenal tumors." Nawata H., Takayanagi R., Ohnaka K., Sakai Y., Imasaki K., Yanase T., Ikuyama S., Tanaka S., Ohe K. Steroids 60:28-34(1995) [PubMed: 7792812] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[8]	"Cloning and sequencing of a human cDNA encoding the angiotensin II receptor type 1." Ostermann E., Castanon M.J. Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[9]	"Rapid identification of polymorphisms in genomic DNA: a high density SNP map of the type I angiotensin II receptor gene locus on chromosome 3q." Antonellis A., Rogus J.J., Pezzolesi M.G., Makita Y., Nam M., Doria A., Warram J.H., Krolewski A.S. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Kopatz S.A., Aronstam R.S., Sharma S.V. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]	"Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis." Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M., Antignac C., Gubler M.-C. Nat. Genet. 37:964-968(2005) [PubMed: 16116425] [Abstract] Cited for: VARIANT RTD MET-282.
+	Additional computationally mapped references.

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Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Angiotensin receptor entry

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Cross-references

Sequence databases

M91464 Genomic DNA. Translation: AAA35569.1.
Z11162 Genomic DNA. Translation: CAA77513.1.
M87290 mRNA. Translation: AAA35535.1.
S77410 mRNA. Translation: AAB34644.1.
M93394 mRNA. Translation: AAA58370.1.
D13814 mRNA. Translation: BAA02968.1.
X65699 mRNA. Translation: CAA46621.1.
AF245699 Genomic DNA. Translation: AAF70464.1.
AY221090 Genomic DNA. Translation: AAO65968.1.

PIR

I39418.
JC1104.

RefSeq

NP_000676.1.
NP_004826.2.
NP_033611.1.
NP_114038.1.
NP_114438.1.

UniGene

Hs.477887
Hs.705369

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZV0	model	-	B	1-359	[»]

ModBase

Search...

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P30556.

Genome annotation databases

Ensembl

ENSG00000144891. Homo sapiens. [Contig view]

GeneID

185.

KEGG

hsa:185.

Organism-specific databases

H-InvDB

HIX0003757.

HGNC

HGNC:336. AGTR1.

MIM

106165. gene.
267430. phenotype.

Orphanet

3033. Renal tubular dysgenesis.

PharmGKB

PA43.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P30556.

HOVERGEN

P30556.

Gene expression databases

ArrayExpress

P30556.

CleanEx

HS_AGTR1.

GermOnline

ENSG00000144891. Homo sapiens.

Family and domain databases

InterPro

IPR000190. ATII_AT1_rcpt.
IPR000248. ATII_rcpt.
IPR001186. BK_rcpt_B1.
IPR001277. CXC_4_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00241. ANGIOTENSINR.
PR00635. ANGIOTENSN1R.
PR00993. BRADYKINNB1R.
PR00645. CXCCHMKINER4.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProDom

P30556.
[Graphical view] [Entries sharing at least one domain]

BLOCKS

Search...

Other Resources

DrugBank

DB00796. Candesartan.
DB00876. Eprosartan.
DB01342. Forasartan.
DB01029. Irbesartan.
DB00678. Losartan.
DB00275. Olmesartan.
DB01347. Saprisartan.
DB00421. Spironolactone.
DB01349. Tasosartan.
DB00966. Telmisartan.
DB00177. Valsartan.

SOURCE

Search...

ProtoNet

Search...

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Entry information

Entry name

AGTR1_HUMAN

Accession

Primary (citable) accession number: P30556
Secondary accession number(s): Q13725

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	July 22, 2008
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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