AGTR1_MERUN
ID AGTR1_MERUN Reviewed; 359 AA.
AC O35210;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Type-1 angiotensin II receptor;
DE AltName: Full=Angiotensin II type-1 receptor {ECO:0000303|PubMed:9757050};
DE Short=AT1 receptor;
DE Short=GkAT1 {ECO:0000303|PubMed:9757050};
GN Name=AGTR1;
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], AND FUNCTION.
RX PubMed=9757050; DOI=10.1016/s0169-328x(98)00187-9;
RA Moriuchi R., Shibata S., Himeno A., Johren O., Hoe K.L., Saavedra J.M.;
RT "Molecular cloning and pharmacological characterization of an atypical
RT gerbil angiotensin II type-1 receptor and its mRNA expression in brain and
RT peripheral tissues.";
RL Brain Res. Mol. Brain Res. 60:234-246(1998).
CC -!- FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide,
CC which acts as a key regulator of blood pressure and sodium retention by
CC the kidney (PubMed:9757050). The activated receptor in turn couples to
CC G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates
CC phospholipase C and increases the cytosolic Ca(2+) concentrations,
CC which in turn triggers cellular responses such as stimulation of
CC protein kinase C (By similarity). {ECO:0000250|UniProtKB:P30556,
CC ECO:0000269|PubMed:9757050}.
CC -!- SUBUNIT: Interacts with MAS1 (By similarity). Interacts with ARRB1 (By
CC similarity). Interacts with FLNA (via filamin repeat 21); increases
CC PKA-mediated phosphorylation of FLNA (By similarity).
CC {ECO:0000250|UniProtKB:P25095, ECO:0000250|UniProtKB:P30556}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30556};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
CC -!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
CC {ECO:0000250|UniProtKB:P30556}.
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; AF011903; AAB65429.1; -; mRNA.
DR AlphaFoldDB; O35210; -.
DR SMR; O35210; -.
DR Ensembl; ENSMUGT00000027020; ENSMUGP00000023563; ENSMUGG00000019728.
DR Ensembl; ENSMUGT00000027033; ENSMUGP00000023574; ENSMUGG00000019735.
DR OrthoDB; 810397at2759; -.
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:0001596; F:angiotensin type I receptor activity; IDA:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IEA:InterPro.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:UniProtKB.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR InterPro; IPR000190; ATII_AT1_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; PR00635; ANGIOTENSN1R.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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 Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Type-1 angiotensin II receptor"
FT /id="PRO_0000069154"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 26..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 56..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556, ECO:0000305"
FT TRANSMEM 62..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 90..98
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556, ECO:0000305"
FT TRANSMEM 99..125
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 126..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 142..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 166..190
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 191..216
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 217..239
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 240..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 269..278
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556, ECO:0000305"
FT TRANSMEM 279..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 305..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 15
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 17
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 167
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 182
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 183
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 184
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 199
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT LIPID 355
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 18..274
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT DISULFID 101..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 359 AA; 40780 MW; 84C1E9B9C64736DD CRC64;
MALNSSADDG IKRIQDDCPK AGRHSYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPVWAVYTAM EYRWPFGNHL CKIASAGISF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCV VIWLLAGLAS LPAVIHRNVY FIENTNSTVC
AFHYESQNST LPVGLGLTKN ILGFMFPFLI ILTSYTLIWK ALKKAYEIQK NKPRNDDIFR
IIMAIVLFFF FSWIPHQIFT FLDVLIQLGV IRDCKIADVV DTAMPITICI AYFNNCLNPL
FYGFLGKKFK KYFLQLLKYI PPKAKSHSSL STKMSTLSYR PSDNMNSSAK KPASCFEVE
