AGTRB_MOUSE
ID AGTRB_MOUSE Reviewed; 359 AA.
AC P29755;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Type-1 angiotensin II receptor B {ECO:0000305};
DE AltName: Full=AT3;
DE AltName: Full=Angiotensin II type-1 receptor B {ECO:0000303|PubMed:1599461};
DE Short=AT1 receptor B {ECO:0000303|PubMed:1599461};
GN Name=Agtr1b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1599461; DOI=10.1016/s0006-291x(05)80983-0;
RA Sasamura H., Hein L., Krieger J.E., Pratt R.E., Kobilka B.K., Dzau V.J.;
RT "Cloning, characterization, and expression of two angiotensin receptor (AT-
RT 1) isoforms from the mouse genome.";
RL Biochem. Biophys. Res. Commun. 185:253-259(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1497638; DOI=10.1016/0006-291x(92)90852-c;
RA Yoshida H., Kakuchi J., Guo D.F., Furuta H., Iwai N.,
RA van der Meer-De Jong R., Inagami T., Ichikawa I.;
RT "Analysis of the evolution of angiotensin II type 1 receptor gene in
RT mammals (mouse, rat, bovine and human).";
RL Biochem. Biophys. Res. Commun. 186:1042-1049(1992).
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. The activated receptor in turn couples to G-alpha proteins
CC G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C
CC and increases the cytosolic Ca(2+) concentrations, which in turn
CC triggers cellular responses such as stimulation of protein kinase C.
CC {ECO:0000250|UniProtKB:P30556}.
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}.
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DR EMBL; S37491; AAB22270.1; -; Genomic_DNA.
DR CCDS; CCDS17264.1; -.
DR PIR; JC1194; JC1194.
DR RefSeq; NP_780295.2; NM_175086.3.
DR AlphaFoldDB; P29755; -.
DR SMR; P29755; -.
DR STRING; 10090.ENSMUSP00000068298; -.
DR GlyGen; P29755; 3 sites.
DR iPTMnet; P29755; -.
DR PhosphoSitePlus; P29755; -.
DR PaxDb; P29755; -.
DR PRIDE; P29755; -.
DR ProteomicsDB; 296003; -.
DR DNASU; 11608; -.
DR Ensembl; ENSMUST00000068316; ENSMUSP00000068298; ENSMUSG00000054988.
DR Ensembl; ENSMUST00000163776; ENSMUSP00000128724; ENSMUSG00000054988.
DR GeneID; 11608; -.
DR KEGG; mmu:11608; -.
DR UCSC; uc008osr.1; mouse.
DR CTD; 11608; -.
DR MGI; MGI:87965; Agtr1b.
DR VEuPathDB; HostDB:ENSMUSG00000054988; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P29755; -.
DR OMA; WVPHQIL; -.
DR OrthoDB; 810397at2759; -.
DR PhylomeDB; P29755; -.
DR TreeFam; TF330024; -.
DR BioGRID-ORCS; 11608; 1 hit in 71 CRISPR screens.
DR PRO; PR:P29755; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P29755; protein.
DR Bgee; ENSMUSG00000054988; Expressed in lumbar dorsal root ganglion and 24 other tissues.
DR Genevisible; P29755; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001596; F:angiotensin type I receptor activity; ISS:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; ISO:MGI.
DR GO; GO:0031711; F:bradykinin receptor binding; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISO:MGI.
DR GO; GO:0001568; P:blood vessel development; IGI:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI.
DR GO; GO:0042756; P:drinking behavior; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0001822; P:kidney development; IGI:MGI.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:UniProtKB.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; ISO:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:MGI.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:MGI.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0032430; P:positive regulation of phospholipase A2 activity; ISO:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IGI:MGI.
DR GO; GO:0019229; P:regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Type-1 angiotensin II receptor B"
FT /id="PRO_0000069156"
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"
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"
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"
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"
FT CONFLICT 7
FT /note="I -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="H -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="E -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="V -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="T -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="F -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40950 MW; 95730F97058EAA4B CRC64;
MILNSSIEDG IKRIQDDCPK AGRHNYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYQWPFGNHL CKIASASVSF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLMAGLAS LPAVIHRNVY FIENTNITVC
AFHYESQNST LPIGLGLTKN ILGFVFPFVI ILTSYTLIWK ALKKAYKIQK NTPRNDDIFR
IIMAIVLFFF FSWVPHQIFS FLDVLIQLGV IHDCEIADVV DTAMPITICI AYFNNCLNPL
FYGFLGKKFK RYFLQLLKYI PPKARSHAGL STKMSTLSYR PSDNMSSSAR KSAYCFEVE
