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Reviewed, UniProtKB/Swiss-Prot P50052 (AGTR2_HUMAN)

Last modified July 22, 2008. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Type-2 angiotensin II receptor
Alternative name(s):
    AT2
Gene names
Name: AGTR2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation.

Subunit structure

Interacts with MTUS1.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

In adult, highly expressed in myometrium with lower levels in adrenal gland and fallopian tube. Very highly expressed in fetal kidney and intestine.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords

   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMGlycoprotein

Gene Ontology (GO)

   Biological processG-protein signaling, coupled to cGMP nucleotide second messenger

Inferred from sequence or structural similarity. Source: UniProtKB

behavior

Inferred from mutant phenotype. Source: UniProtKB

blood vessel remodeling

Traceable author statement. Source: UniProtKB

brain development

Non-traceable author statement. Source: UniProtKB

negative regulation of blood vessel endothelial cell migration

Non-traceable author statement. Source: UniProtKB

negative regulation of cell growth

Traceable author statement. Source: UniProtKB

negative regulation of heart rate

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of nerve growth factor receptor signaling pathway

Inferred from mutant phenotype. Source: UniProtKB

nitric oxide mediated signal transduction

Traceable author statement. Source: UniProtKB

positive regulation of apoptosis

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred by curator. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phosphoprotein phosphatase activity

Inferred from direct assay. Source: UniProtKB

positive regulation of vasodilation

Inferred from direct assay. Source: UniProtKB

protein kinase cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of systemic arterial blood pressure by circulatory renin-angiotensin

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentintegral to plasma membrane Ref.3

Traceable author statement. Source: ProtInc

   Molecular functionangiotensin type II receptor activity

Traceable author statement. Source: ProtInc

receptor antagonist activity

Traceable author statement. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TIMP3P356255EBI-1748067,EBI-1748085

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 363363Type-2 angiotensin II receptor

Regions

Topological domain1 – 4545Extracellular Potential
Transmembrane46 – 71261 Potential
Topological domain72 – 809Cytoplasmic Potential
Transmembrane81 – 102222 Potential
Topological domain103 – 11917Extracellular Potential
Transmembrane120 – 140213 Potential
Topological domain141 – 16020Cytoplasmic Potential
Transmembrane161 – 179194 Potential
Topological domain180 – 20829Extracellular Potential
Transmembrane209 – 234265 Potential
Topological domain235 – 25622Cytoplasmic Potential
Transmembrane257 – 278226 Potential
Topological domain279 – 29719Extracellular Potential
Transmembrane298 – 318217 Potential
Topological domain319 – 36345Cytoplasmic Potential

Amino acid modifications

Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation131N-linked (GlcNAc...) Potential
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation341N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 290 By similarity
Disulfide bond117 ↔ 195 By similarity

Natural variations

Natural variant2481R → K: dbSNP rs5191.
Natural variant2681C → W: dbSNP rs1042860.

Experimental info

Sequence conflict2691W → C Ref.5
Sequence conflict2721F → L in AAA50762. Ref.4
Sequence conflict3231N → G in AAA50762. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P50052-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: FDD7D4E6F9B43E60

FASTA36341,184
        10         20         30         40         50         60 
MKGNSTLATT SKNITSGLHF GLVNISGNNE STLNCSQKPS DKHLDAIPIL YYIIFVIGFL 

        70         80         90        100        110        120 
VNIVVVTLFC CQKGPKKVSS IYIFNLAVAD LLLLATLPLW ATYYSYRYDW LFGPVMCKVF 

       130        140        150        160        170        180 
GSFLTLNMFA SIFFITCMSV DRYQSVIYPF LSQRRNPWQA SYIVPLVWCM ACLSSLPTFY 

       190        200        210        220        230        240 
FRDVRTIEYL GVNACIMAFP PEKYAQWSAG IALMKNILGF IIPLIFIATC YFGIRKHLLK 

       250        260        270        280        290        300 
TNSYGKNRIT RDQVLKMAAA VVLAFIICWL PFHVLTFLDA LAWMGVINSC EVIAVIDLAL 

       310        320        330        340        350        360 
PFAILLGFTN SCVNPFLYCF VGNRFQQKLR SVFRVPITWL QGKRESMSCR KSSSLREMET 


FVS 

« Hide

References

« Hide 'large scale' references
[1]"The sequence and genomic organization of the human type 2 angiotensin II receptor."
Martin M.M., Elton T.S.
Biochem. Biophys. Res. Commun. 209:554-562(1995) [PubMed: 7733925] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]"Assignment of the human angiotensin II type 2 receptor gene (AGTR2) to chromosome Xq22-q23 by fluorescence in situ hybridization."
Chassagne C., Beatty B.G., Meloche S.
Genomics 25:601-603(1995) [PubMed: 7790004] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[3]"Human type 2 angiotensin II receptor gene: cloned, mapped to the X chromosome, and its mRNA is expressed in the human lung."
Koike G., Horiuchi M., Yamada T., Szpirer C., Jacob H.J., Dzau V.J.
Biochem. Biophys. Res. Commun. 203:1842-1850(1994) [PubMed: 7945336] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[4]"Molecular cloning and expression of the gene encoding human angiotensin II type 2 receptor."
Tsuzuki S., Ichiki T., Nakakubo H., Kitami Y., Guo D.F., Shirai H., Inagami T.
Biochem. Biophys. Res. Commun. 200:1449-1454(1994) [PubMed: 8185599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[5]"Molecular cloning of the human angiotensin II type 2 receptor cDNA."
Martin M.M., Su B., Elton T.S.
Biochem. Biophys. Res. Commun. 205:645-651(1994) [PubMed: 7999093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[6]"Molecular characterization and chromosome localization of a human angiotensin II AT2 receptor gene highly expressed in fetal tissues."
Lazard D., Briend-Sutren M.M., Villageois P., Mattei M.-G., Strosberg A.D., Nahmias C.
Recept. Channels 2:271-280(1994) [PubMed: 7719706] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[7]"Sequence of the AGTR2 gene in Cantonese."
Zhang M., Ma H., Wang B., Zhao Y.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Isolation of complete coding sequence for angiotensin II receptor, type 2 (AGTR2)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., Toth E.J., Nickerson D.A.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[13]Katsuya T., Dzau V.J.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-22.
Tissue: Blood.
[14]Warnecke C.H., Holzmeister J., Regitz-Zagrosek V., Fleck E.
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-16.
Tissue: Uterus.
[15]"Trans-inactivation of receptor tyrosine kinases by novel angiotensin II AT2 receptor-interacting protein, ATIP."
Nouet S., Amzallag N., Li J.-M., Louis S., Seitz I., Cui T.-X., Alleaume A.-M., Di Benedetto M., Boden C., Masson M., Strosberg A.D., Horiuchi M., Couraud P.-O., Nahmias C.
J. Biol. Chem. 279:28989-28997(2004) [PubMed: 15123706] [Abstract]
Cited for: INTERACTION WITH MTUS1, FUNCTION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

U20860 Genomic DNA. Translation: AAA85851.1.
L34579 Genomic DNA. Translation: AAA98990.1.
U10273 Genomic DNA. Translation: AAA61794.1.
U15592 Genomic DNA. Translation: AAA50762.1.
U16957 mRNA. Translation: AAA67753.1.
U27478 Genomic DNA. Translation: AAA84900.1.
AY536522 Genomic DNA. Translation: AAS45437.1.
AY322542 Genomic DNA. Translation: AAP84355.1.
AY324607 Genomic DNA. Translation: AAP72969.1.
CR541969 mRNA. Translation: CAG46767.1.
AL732602 Genomic DNA. Translation: CAI40984.1.
BC095504 mRNA. Translation: AAH95504.1.
X87723 mRNA. Translation: CAA61022.1.
PIRJC2543.
RefSeqNP_000677.2.
UniGeneHs.405348

3D structure databases

HSSPHSSP built from PDB template 1DDD based on UniProtKB P34996.
ModBaseSearch...

Protein-protein interaction databases

IntActP50052.

Protein family/group databases

GPCRDBSearch...

Genome annotation databases

EnsemblENSG00000180772. Homo sapiens. [Contig view]
GeneID186.
KEGGhsa:186.

Organism-specific databases

HGNCHGNC:338. AGTR2.
MIM300034. gene+phenotype.
PharmGKBPA44.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP50052.
HOVERGENP50052.

Gene expression databases

ArrayExpressP50052.
CleanExHS_AGTR2.
GermOnlineENSG00000180772. Homo sapiens.

Family and domain databases

InterProIPR000147. ATII_AT2_rcpt.
IPR000248. ATII_rcpt.
IPR001186. BK_rcpt_B1.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]
PANTHERPTHR19264:SF268. ATII_AT2_rcpt. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00241. ANGIOTENSINR.
PR00636. ANGIOTENSN2R.
PR00993. BRADYKINNB1R.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
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