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   27-MAR-2024, entry version 173.
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   GlyCosmos; P29755; 3 sites, No reported glycans.
DR   GlyGen; P29755; 3 sites.
DR   iPTMnet; P29755; -.
DR   PhosphoSitePlus; P29755; -.
DR   PaxDb; 10090-ENSMUSP00000068298; -.
DR   ProteomicsDB; 296003; -.
DR   DNASU; 11608; -.
DR   Ensembl; ENSMUST00000068316.8; ENSMUSP00000068298.8; ENSMUSG00000054988.10.
DR   Ensembl; ENSMUST00000163776.3; ENSMUSP00000128724.3; ENSMUSG00000054988.10.
DR   GeneID; 11608; -.
DR   KEGG; mmu:11608; -.
DR   UCSC; uc008osr.1; mouse.
DR   AGR; MGI:87965; -.
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; ITICMAY; -.
DR   OrthoDB; 4179713at2759; -.
DR   PhylomeDB; P29755; -.
DR   TreeFam; TF330024; -.
DR   BioGRID-ORCS; 11608; 1 hit in 76 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 26 other cell types or tissues.
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: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:0051402; P:neuron apoptotic process; IMP:MGI.
DR   GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; ISO:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor 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:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR   GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; 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   CDD; cd15192; 7tmA_AT1R; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000190; ATII_AT1_rcpt.
DR   InterPro; IPR000248; ATII_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF951; APELIN RECEPTOR; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
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   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.
DR   Genevisible; P29755; MM.
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
//