AGTR2_MERUN
ID AGTR2_MERUN Reviewed; 363 AA.
AC Q9Z0Z6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Type-2 angiotensin II receptor;
DE AltName: Full=Angiotensin II type-2 receptor;
DE Short=AT2 receptor {ECO:0000303|PubMed:14615403};
GN Name=AGTR2;
OS Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Gerbillinae; Meriones.
OX NCBI_TaxID=10047;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=14615403; DOI=10.1152/ajpregu.00008.2003;
RA Hoe K.-L., Armando I., Baiardi G., Sreenath T., Kulkarni A., Martinez A.,
RA Saavedra J.M.;
RT "Molecular cloning, characterization, and distribution of the gerbil
RT angiotensin II AT2 receptor.";
RL Am. J. Physiol. 285:R1373-R1383(2003).
CC -!- FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide.
CC Signals primarily via a non-canonical G-protein- and beta-arrestin
CC independent pathways. Cooperates with MTUS1 to inhibit ERK2 activation
CC and cell proliferation. {ECO:0000250|UniProtKB:P50052}.
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 -!- 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; AF080066; AAD19339.1; -; mRNA.
DR AlphaFoldDB; Q9Z0Z6; -.
DR SMR; Q9Z0Z6; -.
DR Ensembl; ENSMUGT00000009209; ENSMUGP00000007795; ENSMUGG00000007071.
DR OrthoDB; 685818at2759; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004945; F:angiotensin type II receptor activity; ISS:UniProtKB.
DR GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0002035; P:brain renin-angiotensin system; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR GO; GO:0010459; P:negative regulation of heart rate; IEA:Ensembl.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0072300; P:positive regulation of metanephric glomerulus development; IEA:Ensembl.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0035566; P:regulation of metanephros size; IEA:Ensembl.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..363
FT /note="Type-2 angiotensin II receptor"
FT /id="PRO_0000069168"
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 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 117..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 363 AA; 41435 MW; A0BCA803AD967DBE CRC64;
MKDNFSFAAT SRNITSSLPF VNLNMSGTND LIFNCSHKPS DKHLEAIPVL YYLIFVIGFA
VNIIVVSLFC CQKGPKKVSS IYIFNLAVAD LLLLATLPLW ATYYSYRYDW LFGPVMCKVF
GSFLTLNMFA SIFFITCMSV DRYQSVIYPF LSQRRNPWQA SYVVPLVWCM ACLSSLPTFY
FRDVRTIEYL GVNACVMAFP PEKYAQWSAG IALMKNVLGF IIPLIFIATC YFGIRKHLLK
TNSYGKNRIT RDQVLKMAAA VVLAFIICWL PFHVLTFLDA LSWMGIINSC EVMAVIDLAL
PFAILLGFTN SCVNPFLYCF VGNRFQQKLR SMFRVPITWL QGKRETMSCR KSSSLREMDT
FVS
