AGTRB_RAT
ID AGTRB_RAT Reviewed; 359 AA.
AC P29089;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Type-1 angiotensin II receptor B {ECO:0000303|PubMed:1575725};
DE AltName: Full=AT3;
DE AltName: Full=Angiotensin II type-1 receptor B {ECO:0000303|PubMed:1374402};
DE Short=AT1 receptor B;
GN Name=Agtr1b; Synonyms=Agtr1, At1b;
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].
RC TISSUE=Pituitary anterior lobe;
RX PubMed=1567388; DOI=10.1016/s0006-291x(05)80302-x;
RA Kakar S.S., Sellers J.C., Devor D.C., Musgrove L.C., Neill J.D.;
RT "Angiotensin II type-1 receptor subtype cDNAs: differential tissue
RT expression and hormonal regulation.";
RL Biochem. Biophys. Res. Commun. 183:1090-1096(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1575725; DOI=10.1016/0006-291x(92)90700-u;
RA Elton T.S., Stephan C.C., Taylor G.R., Kimball M.G., Martin M.M.,
RA Durand J.N., Oparil S.;
RT "Isolation of two distinct type I angiotensin II receptor genes.";
RL Biochem. Biophys. Res. Commun. 184:1067-1073(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Adrenal gland;
RX PubMed=1544458; DOI=10.1016/0014-5793(92)80071-n;
RA Iwai N., Inagami T.;
RT "Identification of two subtypes in the rat type I angiotensin II
RT receptor.";
RL FEBS Lett. 298:257-260(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal cortex;
RX PubMed=1374402; DOI=10.1016/s0021-9258(19)50109-0;
RA Sandberg K., Ji H., Clark A.J., Shapira H., Catt K.J.;
RT "Cloning and expression of a novel angiotensin II receptor subtype.";
RL J. Biol. Chem. 267:9455-9458(1992).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 84-259.
RC TISSUE=Kidney;
RX PubMed=1599457; DOI=10.1016/s0006-291x(05)80976-3;
RA Ye M.Q., Healy D.P.;
RT "Characterization of an angiotensin type-1 receptor partial cDNA from rat
RT kidney: evidence for a novel AT1B receptor subtype.";
RL Biochem. Biophys. Res. Commun. 185:204-210(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 -!- TISSUE SPECIFICITY: Is expressed in the liver, kidney, aorta, lung,
CC uterus, ovary, spleen, heart, and vascular smooth muscle cell.
CC Expressed most abundantly in the adrenal gland.
CC {ECO:0000269|PubMed:1544458}.
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; M87003; AAA40739.1; -; mRNA.
DR EMBL; X64052; CAA45410.1; -; mRNA.
DR EMBL; M90065; AAA40704.1; -; mRNA.
DR EMBL; S37461; AAB22267.1; -; mRNA.
DR PIR; A42656; A42656.
DR PIR; JQ1516; JQ1516.
DR RefSeq; NP_112271.2; NM_031009.2.
DR RefSeq; XP_006232249.1; XM_006232187.2.
DR RefSeq; XP_008759101.1; XM_008760879.2.
DR AlphaFoldDB; P29089; -.
DR SMR; P29089; -.
DR STRING; 10116.ENSRNOP00000014175; -.
DR BindingDB; P29089; -.
DR ChEMBL; CHEMBL263; -.
DR DrugCentral; P29089; -.
DR GuidetoPHARMACOLOGY; 34; -.
DR GlyGen; P29089; 3 sites.
DR iPTMnet; P29089; -.
DR PhosphoSitePlus; P29089; -.
DR PaxDb; P29089; -.
DR Ensembl; ENSRNOT00000014178; ENSRNOP00000014175; ENSRNOG00000010640.
DR GeneID; 81638; -.
DR KEGG; rno:81638; -.
DR UCSC; RGD:2071; rat.
DR CTD; 11608; -.
DR RGD; 2071; Agtr1b.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P29089; -.
DR OMA; WVPHQIL; -.
DR OrthoDB; 810397at2759; -.
DR PhylomeDB; P29089; -.
DR TreeFam; TF330024; -.
DR PRO; PR:P29089; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010640; Expressed in kidney and 7 other tissues.
DR Genevisible; P29089; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001596; F:angiotensin type I receptor activity; ISS:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB.
DR GO; GO:0042756; P:drinking behavior; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:UniProtKB.
DR GO; GO:0010259; P:multicellular organism aging; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045777; P:positive regulation of blood pressure; IMP:BHF-UCL.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0002019; P:regulation of renal output by angiotensin; TAS:RGD.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; ISO:RGD.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0001999; P:renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure; TAS:RGD.
DR GO; GO:1990776; P:response to angiotensin; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009651; P:response to salt stress; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Type-1 angiotensin II receptor B"
FT /id="PRO_0000069161"
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 REGION 339..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 2
FT /note="T -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="V -> M (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="L -> Y (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40912 MW; A2CC21E0B3365C5B CRC64;
MTLNSSTEDG IKRIQDDCPK AGRHNYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYRWPFGNHL CKIASASVSF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLMAGLAS LPAVIYRNVY FIENTNITVC
AFHYESQNST LPIGLGLTKN ILGFVFPFLI ILTSYTLIWK ALKKAYKIQK NTPRNDDIFR
IIMAIVLFFF FSWVPHQIFT FLDVLIQLGI IRDCEIADIV DTAMPITICI AYFNNCLNPL
FYGFLGKKFK KYFLQLLKYI PPTAKSHAGL STKMSTLSYR PSDNMSSSAK KSASFFEVE
