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   02-SEP-2026, entry version 176.
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). Primarily signals via a non-canonical G protein- and
CC       beta-arrestin independent pathway. 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}.
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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_012494.4.
DR   RefSeq; XP_063135845.1; XM_063279775.1.
DR   AlphaFoldDB; P35351; -.
DR   SMR; P35351; -.
DR   BioGRID; 246372; 1.
DR   CORUM; P35351; -.
DR   FunCoup; P35351; 249.
DR   STRING; 10116.ENSRNOP00000064709; -.
DR   BindingDB; P35351; -.
DR   ChEMBL; CHEMBL257; -.
DR   DrugCentral; P35351; -.
DR   GuidetoPHARMACOLOGY; 35; -.
DR   GlyCosmos; P35351; 5 sites, No reported glycans.
DR   GlyGen; P35351; 5 sites.
DR   iPTMnet; P35351; -.
DR   PhosphoSitePlus; P35351; -.
DR   PaxDb; 10116-ENSRNOP00000064709; -.
DR   Ensembl; ENSRNOT00000074269.3; ENSRNOP00000064709.1; ENSRNOG00000050006.3.
DR   Ensembl; ENSRNOT00000127414.1; ENSRNOP00000109539.1; ENSRNOG00000050006.3.
DR   Ensembl; ENSRNOT00000157598.1; ENSRNOP00000106067.1; ENSRNOG00000050006.3.
DR   Ensembl; ENSRNOT00000166735.1; ENSRNOP00000103004.1; ENSRNOG00000050006.3.
DR   Ensembl; ENSRNOT00055043674; ENSRNOP00055035664; ENSRNOG00055025331.
DR   Ensembl; ENSRNOT00055043683; ENSRNOP00055035673; ENSRNOG00055025331.
DR   Ensembl; ENSRNOT00060033601; ENSRNOP00060027505; ENSRNOG00060019463.
DR   Ensembl; ENSRNOT00060033620; ENSRNOP00060027521; ENSRNOG00060019463.
DR   Ensembl; ENSRNOT00065015889; ENSRNOP00065012008; ENSRNOG00065009886.
DR   Ensembl; ENSRNOT00065015895; ENSRNOP00065012010; ENSRNOG00065009886.
DR   GeneID; 24182; -.
DR   KEGG; rno:24182; -.
DR   AGR; RGD:2072; -.
DR   CTD; 186; -.
DR   RGD; 2072; Agtr2.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01130000278303; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; P35351; -.
DR   OMA; TFNCSHK; -.
DR   OrthoDB; 8804420at2759; -.
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 cell types or tissues.
DR   ExpressionAtlas; P35351; baseline and differential.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004945; F:angiotensin type II receptor activity; IDA:UniProtKB.
DR   GO; GO:0001965; F:G-protein alpha-subunit binding; TAS:RGD.
DR   GO; GO:0038166; P:angiotensin-activated signaling pathway; ISO: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: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; ISO:RGD.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; IMP: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:0030182; P:neuron differentiation; TAS:RGD.
DR   GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling; ISO: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:0045893; P:positive regulation of DNA-templated transcription; ISO: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: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:0042311; P:vasodilation; IMP:RGD.
DR   CDD; cd15191; 7tmA_AT2R; 1.
DR   FunFam; 1.20.1070.10:FF:000161; type-2 angiotensin II receptor; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000147; ATII_AT2_rcpt.
DR   InterPro; IPR000248; ATII_rcpt.
DR   InterPro; IPR050119; CCR1-9-like.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR   PANTHER; PTHR10489:SF952; TYPE-2 ANGIOTENSIN II RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00241; ANGIOTENSINR.
DR   PRINTS; PR00636; ANGIOTENSN2R.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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
//