AGTRB_XENLA
ID AGTRB_XENLA Reviewed; 363 AA.
AC P35373; B7ZQ36;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Type-1 angiotensin II receptor B;
DE AltName: Full=Angiotensin 2 receptor, type 1-B;
DE AltName: Full=Angiotensin II receptor, type 1-B;
DE AltName: Full=Angiotensin type 1 receptor;
DE Short=AT1 receptor 1;
DE Short=XAT-1;
GN Name=agtr1-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=8355665;
RA Bergsma D.J., Ellis C., Nuthulaganti P.R., Nambi P., Scaife K., Kumar C.,
RA Aiyar N.;
RT "Isolation and expression of a novel angiotensin II receptor from Xenopus
RT laevis heart.";
RL Mol. Pharmacol. 44:277-284(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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:8355665). 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:8355665}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30556};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
CC -!- TISSUE SPECIFICITY: Heart membranes, follicular oocytes.
CC {ECO:0000269|PubMed:8355665}.
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; U01155; AAC59635.1; -; mRNA.
DR EMBL; BC169667; AAI69667.1; -; mRNA.
DR RefSeq; NP_001079250.1; NM_001085781.1.
DR AlphaFoldDB; P35373; -.
DR SMR; P35373; -.
DR GeneID; 378523; -.
DR CTD; 378523; -.
DR Xenbase; XB-GENE-5969923; agtr1.S.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 685818at2759; -.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 378523; Expressed in muscle tissue and 5 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001595; F:angiotensin receptor activity; IDA:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IDA: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;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="Type-1 angiotensin II receptor B"
FT /id="PRO_0000069166"
FT TOPO_DOM 1..27
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 28..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 58..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 64..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 92..100
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 101..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 128..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 144..167
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 168..192
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 193..218
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 219..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..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 169
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 186
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 201
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT LIPID 346
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 362
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 20..274
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT DISULFID 103..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 363 AA; 41541 MW; 087D7F4A03E6D0CF CRC64;
MLSNISAGEN SEVEKIVVKC SKSGMHNYIF ITIPIIYSTI FVVGVFGNSL VVIVIYSYMK
MKTMASVFLM NLALSDLCFV ITLPLWAVYT AMHYHWPFGD LLCKIASTAI TLNLYTTVFL
LTCLSIDRYS AIVHPMKSRI RRTVMVARLT CVGIWLVAFL ASLPSVIYRQ IFIFPDTNQT
VCALVYHSGH IYFMVGMSLV KNIVGFFIPF VIILTSYTLI GKTLKEVYRA QRARNDDIFK
MIVAVVLLFF FCWIPHQVFT FLDVLIQMDV IQNCKMYDIV DTGMPITICI AYFNSCLNPF
LYGFFGKKFR KHFLQLIKYI PPKMRTHASV NTKSSTVSQR LSDTKCASNK IALWIFDIEE
HCK
