AGTR2_RAT
ID AGTR2_RAT Reviewed; 363 AA.
AC P35351;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Type-2 angiotensin II receptor {ECO:0000303|PubMed:8227010};
DE AltName: Full=Angiotensin II type-2 receptor {ECO:0000303|PubMed:7599191};
DE Short=AT2 receptor {ECO:0000303|PubMed:8227011};
GN Name=Agtr2 {ECO:0000312|RGD:2072};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=8227011; DOI=10.1016/s0021-9258(19)74499-8;
RA Kambayashi Y., Bardhan S., Takahashi K., Tsuzuki S., Inui H., Hamakubo T.,
RA Inagami T.;
RT "Molecular cloning of a novel angiotensin II receptor isoform involved in
RT phosphotyrosine phosphatase inhibition.";
RL J. Biol. Chem. 268:24543-24546(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Fetus;
RX PubMed=8227010; DOI=10.1016/s0021-9258(19)74498-6;
RA Mukoyama M., Nakajima M., Horiuchi M., Sasamura H., Pratt R.E., Dzau V.J.;
RT "Expression cloning of type 2 angiotensin II receptor reveals a unique
RT class of seven-transmembrane receptors.";
RL J. Biol. Chem. 268:24539-24542(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer; TISSUE=Liver;
RX PubMed=7490161; DOI=10.1161/01.hyp.26.6.998;
RA Koike G., Winer E.S., Horiuchi M., Brown D.M., Szpirer C., Dzau V.J.,
RA Jacob H.J.;
RT "Cloning, characterization, and genetic mapping of the rat type 2
RT angiotensin II receptor gene.";
RL Hypertension 26:998-1002(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7713098; DOI=10.1093/eurheartj/15.suppl_d.104;
RA Inagami T., Iwai N., Sasaki K., Yamano Y., Bardhan S., Chaki S., Guo D.F.,
RA Furuta H., Ohyama K., Kambayashi Y., Takahashi K., Ichiki T.;
RT "Cloning, expression and regulation of angiotensin II receptors.";
RL Eur. Heart J. 15:104-107(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-143.
RC STRAIN=Sprague-Dawley;
RX PubMed=7599191; DOI=10.1016/0167-4781(95)00076-s;
RA Kobayashi S., Ohnishi J., Nibu Y., Nishimatsu S., Umemura S., Ishii M.,
RA Murakami K., Miyazaki H.;
RT "Cloning of the rat angiotensin II type 2 receptor gene and identification
RT of its functional promoter region.";
RL Biochim. Biophys. Acta 1262:155-158(1995).
RN [6]
RP DISULFIDE BONDS.
RX PubMed=11068047; DOI=10.1016/s0014-5793(00)02141-4;
RA Feng Y.H., Saad Y., Karnik S.S.;
RT "Reversible inactivation of AT(2) angiotensin II receptor from cysteine-
RT disulfide bond exchange.";
RL FEBS Lett. 484:133-138(2000).
CC -!- FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide
CC (PubMed:8227011). Signals primarily via a non-canonical G-protein- and
CC beta-arrestin independent pathways. Cooperates with MTUS1 to inhibit
CC ERK2 activation and cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:P50052, ECO:0000269|PubMed:8227011}.
CC -!- SUBUNIT: Interacts with MTUS1. {ECO:0000250|UniProtKB:P50052}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35374};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P50052}.
CC -!- TISSUE SPECIFICITY: Abundant expression in fetal tissues, immature
CC brain, skin wound and atretic ovarian follicles.
CC {ECO:0000269|PubMed:8227010, ECO:0000269|PubMed:8227011}.
CC -!- DEVELOPMENTAL STAGE: Abundant in whole fetus but decreases rapidly
CC after birth. In adults is highly expressed in the adrenal, present in
CC the brain and uterus but undetectable in the heart.
CC {ECO:0000269|PubMed:8227010, ECO:0000269|PubMed:8227011}.
CC -!- DOMAIN: Helix VIII may act as a gatekeeper for either suppression or
CC activation of the receptor, depending on post-translational
CC modifications and interactions with various receptor partners. Helix
CC VIII is found in a non-canonical position, stabilizing the active-like
CC state, but at the same time preventing the recruitment of G-proteins or
CC beta-arrestins. Upon switching to a membrane-bound conformation, helix
CC VIII can support the recruitment of G proteins and beta-arrestins.
CC {ECO:0000250|UniProtKB:P50052}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D16840; BAA04116.1; -; mRNA.
DR EMBL; U01908; AAC52126.1; -; Genomic_DNA.
DR EMBL; U22663; AAA86509.1; -; Genomic_DNA.
DR EMBL; D43778; BAA07833.1; -; Genomic_DNA.
DR PIR; A49092; A49092.
DR RefSeq; NP_036626.1; NM_012494.3.
DR RefSeq; XP_006257494.1; XM_006257432.3.
DR AlphaFoldDB; P35351; -.
DR SMR; P35351; -.
DR BioGRID; 246372; 1.
DR STRING; 10116.ENSRNOP00000064709; -.
DR BindingDB; P35351; -.
DR ChEMBL; CHEMBL257; -.
DR DrugCentral; P35351; -.
DR GuidetoPHARMACOLOGY; 35; -.
DR GlyGen; P35351; 5 sites.
DR iPTMnet; P35351; -.
DR PhosphoSitePlus; P35351; -.
DR PaxDb; P35351; -.
DR Ensembl; ENSRNOT00000074269; ENSRNOP00000064709; ENSRNOG00000050006.
DR GeneID; 24182; -.
DR KEGG; rno:24182; -.
DR CTD; 186; -.
DR RGD; 2072; Agtr2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P35351; -.
DR OMA; STFNCSH; -.
DR OrthoDB; 685818at2759; -.
DR PhylomeDB; P35351; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P35351; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000050006; Expressed in esophagus and 5 other tissues.
DR ExpressionAtlas; P35351; baseline and differential.
DR Genevisible; P35351; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; TAS:RGD.
DR GO; GO:0035932; P:aldosterone secretion; IMP:RGD.
DR GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0002035; P:brain renin-angiotensin system; ISO:RGD.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IMP:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:RGD.
DR GO; GO:0021695; P:cerebellar cortex development; IMP:RGD.
DR GO; GO:0042416; P:dopamine biosynthetic process; IMP:RGD.
DR GO; GO:0035640; P:exploration behavior; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IDA:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0060993; P:kidney morphogenesis; IMP:RGD.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:RGD.
DR GO; GO:0010459; P:negative regulation of heart rate; ISO:RGD.
DR GO; GO:0032304; P:negative regulation of icosanoid secretion; IMP:RGD.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:RGD.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; IDA:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; TAS:RGD.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:RGD.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0072300; P:positive regulation of metanephric glomerulus development; ISO:RGD.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0035566; P:regulation of metanephros size; ISO:RGD.
DR GO; GO:0042306; P:regulation of protein import into nucleus; IDA:RGD.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; ISO:RGD.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IMP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0042311; P:vasodilation; IMP:RGD.
DR InterPro; IPR000147; ATII_AT2_rcpt.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00636; ANGIOTENSN2R.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="Type-2 angiotensin II receptor"
FT /id="PRO_0000069170"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 46..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 71..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 81..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 105..114
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 115..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 141..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 160..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 182..206
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 207..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 233..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 258..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 282..294
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 295..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 321..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT REGION 324..333
FT /note="Helix VIII"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 103
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 104
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 182
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 204
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 215
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 279
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 297
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT MOD_RES 354
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:11068047"
FT DISULFID 117..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:11068047"
SQ SEQUENCE 363 AA; 41331 MW; 4FE4551A41336650 CRC64;
MKDNFSFAAT SRNITSSLPF DNLNATGTNE SAFNCSHKPA DKHLEAIPVL YYMIFVIGFA
VNIVVVSLFC CQKGPKKVSS IYIFNLAVAD LLLLATLPLW ATYYSYRYDW LFGPVMCKVF
GSFLTLNMFA SIFFITCMSV DRYQSVIYPF LSQRRNPWQA SYVVPLVWCM ACLSSLPTFY
FRDVRTIEYL GVNACIMAFP PEKYAQWSAG IALMKNILGF IIPLIFIATC YFGIRKHLLK
TNSYGKNRIT RDQVLKMAAA VVLAFIICWL PFHVLTFLDA LTWMGIINSC EVIAVIDLAL
PFAILLGFTN SCVNPFLYCF VGNRFQQKLR SVFRVPITWL QGKRETMSCR KSSSLREMDT
FVS
