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P35374 (AGTR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type-2 angiotensin II receptor
Alternative name(s):
Angiotensin II type-2 receptor
Short name=AT2
Gene names
Name:Agtr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation. Ref.8

Subunit structure

Interacts with MTUS1. Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.8.

Tissue specificity

Expressed at highest levels in adrenal gland and uterus. Ref.8

Post-translational modification

C-terminal Ser or Thr residues may be phosphorylated.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence caution

The sequence AAB49539.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger

Inferred from direct assay PubMed 17000928. Source: BHF-UCL

aldosterone secretion

Inferred from electronic annotation. Source: Ensembl

angiotensin-activated signaling pathway

Inferred from direct assay PubMed 9878677. Source: GOC

brain renin-angiotensin system

Inferred from direct assay PubMed 9878677. Source: MGI

cell growth involved in cardiac muscle cell development

Inferred from electronic annotation. Source: Ensembl

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular sodium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cerebellar cortex development

Inferred from electronic annotation. Source: Ensembl

dopamine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

exploration behavior

Inferred from mutant phenotype PubMed 7477267. Source: BHF-UCL

inflammatory response

Inferred from genetic interaction PubMed 19404405. Source: MGI

intracellular signal transduction

Inferred from direct assay PubMed 17000928. Source: BHF-UCL

negative regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of heart rate

Inferred from mutant phenotype PubMed 9449684. Source: BHF-UCL

negative regulation of icosanoid secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of neurotrophin TRK receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of norepinephrine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of branching involved in ureteric bud morphogenesis

Inferred from mutant phenotype PubMed 18607644. Source: UniProtKB

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of metanephric glomerulus development

Inferred from mutant phenotype PubMed 18607644. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Inferred from direct assay PubMed 17000928. Source: BHF-UCL

positive regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of renal sodium excretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 15153556PubMed 18607644. Source: UniProtKB

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

regulation of metanephros size

Inferred from mutant phenotype PubMed 18607644. Source: UniProtKB

regulation of systemic arterial blood pressure by circulatory renin-angiotensin

Inferred from mutant phenotype PubMed 7477267. Source: BHF-UCL

regulation of transcription factor import into nucleus

Inferred from electronic annotation. Source: Ensembl

renin-angiotensin regulation of aldosterone production

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

vasodilation by angiotensin involved in regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 10425188. Source: MGI

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionangiotensin type II receptor activity

Inferred from direct assay PubMed 9878677. Source: MGI

peptide hormone binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 363363Type-2 angiotensin II receptor
PRO_0000069169

Regions

Topological domain1 – 4545Extracellular Potential
Transmembrane46 – 7126Helical; Name=1; Potential
Topological domain72 – 809Cytoplasmic Potential
Transmembrane81 – 10222Helical; Name=2; Potential
Topological domain103 – 11917Extracellular Potential
Transmembrane120 – 14021Helical; Name=3; Potential
Topological domain141 – 16020Cytoplasmic Potential
Transmembrane161 – 17919Helical; Name=4; Potential
Topological domain180 – 20829Extracellular Potential
Transmembrane209 – 23426Helical; Name=5; Potential
Topological domain235 – 25622Cytoplasmic Potential
Transmembrane257 – 27822Helical; Name=6; Potential
Topological domain279 – 29719Extracellular Potential
Transmembrane298 – 31821Helical; Name=7; Potential
Topological domain319 – 36345Cytoplasmic Potential

Amino acid modifications

Modified residue3541Phosphoserine; by PKC Potential
Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation131N-linked (GlcNAc...) Potential
Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation341N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 290 Ref.7
Disulfide bond117 ↔ 195 Ref.7

Sequences

Sequence LengthMass (Da)Tools
P35374 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 6C7D6E3B026D1E80

FASTA36341,374
        10         20         30         40         50         60 
MKDNFSFAAT SRNITSSRPF DNLNATGTNE SAFNCSHKPS DKHLEAIPVL YYMIFVIGFA 

        70         80         90        100        110        120 
VNIVVVSLFC CQKGPKKVSS IYIFNLALAD LLLLATLPLW ATYYSYRYDW LFGPVMCKVF 

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

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

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

       310        320        330        340        350        360 
PFAILLGFTN SCVNPFLYCF VGNRFQQKLR SVFRVPITWL QGKRETMSCR KGSSLREMDT 


FVS 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of cDNA and analysis of the gene for mouse angiotensin II type 2 receptor."
Nakajima M., Mukoyama M., Pratt R.E., Horiuchi M., Dzau V.J.
Biochem. Biophys. Res. Commun. 197:393-399(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Fetus.
[2]"Cloning of the cDNA and the genomic DNA of the mouse angiotensin II type 2 receptor."
Ichiki T., Herold C.L., Kambayashi Y., Bardhan S., Inagami T.
Biochim. Biophys. Acta 1189:247-250(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[3]"Molecular and functional characterization of angiotensin II AT2 receptor in neuroblastoma N1E-115 cells."
Nahmias C., Cazaubon S.M., Sutren M., Masson M., Lazard D., Villageois P., Elbaz N., Strosberg A.D.
Adv. Exp. Med. Biol. 396:167-173(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"The growth-dependent expression of angiotensin II type 2 receptor is regulated by transcription factors interferon regulatory factor-1 and -2."
Horiuchi M., Koike G., Yamada T., Mukoyama M., Nakajima M., Dzau V.J.
J. Biol. Chem. 270:20225-20230(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Liver.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head.
[6]"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].
Strain: C57BL/6J.
Tissue: Mammary gland.
[7]"Identification and function of disulfide bridges in the extracellular domains of the angiotensin II type 2 receptor."
Heerding J.N., Hines J., Fluharty S.J., Yee D.K.
Biochemistry 40:8369-8377(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[8]"Regulation of transport of the angiotensin AT2 receptor by a novel membrane-associated Golgi protein."
Wruck C.J., Funke-Kaiser H., Pufe T., Kusserow H., Menk M., Schefe J.H., Kruse M.L., Stoll M., Unger T.
Arterioscler. Thromb. Vasc. Biol. 25:57-64(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MTUS1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S67465 mRNA. Translation: AAB29336.1.
U04828 mRNA. Translation: AAC52128.1.
U00766 mRNA. Translation: AAC04933.1.
L32840 mRNA. Translation: AAB49539.1. Different initiation.
U11073 Genomic DNA. Translation: AAA82184.1.
AK086334 mRNA. Translation: BAC39650.1.
BC003811 mRNA. Translation: AAH03811.1.
CCDSCCDS40889.1.
PIRI48261.
RefSeqNP_031455.1. NM_007429.5.
UniGeneMm.2679.

3D structure databases

ProteinModelPortalP35374.
SMRP35374. Positions 46-330.
ModBaseSearch...
MobiDBSearch...

Chemistry

GuidetoPHARMACOLOGY35.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP35374.

Proteomic databases

PRIDEP35374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089188; ENSMUSP00000086592; ENSMUSG00000068122.
GeneID11609.
KEGGmmu:11609.
UCSCuc009suq.2. mouse.

Organism-specific databases

CTD186.
MGIMGI:87966. Agtr2.

Phylogenomic databases

eggNOGNOG311643.
GeneTreeENSGT00720000108671.
HOVERGENHBG104998.
InParanoidP35374.
KOK04167.
OMANCSHKPS.
OrthoDBEOG7TQV1F.
PhylomeDBP35374.
TreeFamTF330024.

Gene expression databases

BgeeP35374.
CleanExMM_AGTR2.
GenevestigatorP35374.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000147. ATII_AT2_rcpt.
IPR000248. ATII_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00241. ANGIOTENSINR.
PR00636. ANGIOTENSN2R.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279152.
PROP35374.
SOURCESearch...

Entry information

Entry nameAGTR2_MOUSE
AccessionPrimary (citable) accession number: P35374
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries