AGTRA_XENLA
ID AGTRA_XENLA Reviewed; 362 AA.
AC P32303; Q6PAZ1; Q91383;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Type-1 angiotensin II receptor A;
DE Short=xAT;
DE AltName: Full=Angiotensin 2 receptor, type 1-A;
DE AltName: Full=Angiotensin II receptor, type 1-A;
GN Name=agtr1-a;
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=Myocardium;
RX PubMed=7688227; DOI=10.1006/bbrc.1993.1886;
RA Ji H., Sandberg K., Zhang Y., Catt K.J.;
RT "Molecular cloning, sequencing and functional expression of an amphibian
RT angiotensin II receptor.";
RL Biochem. Biophys. Res. Commun. 194:756-762(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=7519446; DOI=10.1016/0167-4781(94)90193-7;
RA Nishimatsu S., Koyasu N., Sugaya T., Ohnishi J., Yamagishi T., Murakami K.,
RA Miyazaki H.;
RT "Isolation and characterization of two alternatively spliced complementary
RT DNAs encoding a Xenopus laevis angiotensin II receptor.";
RL Biochim. Biophys. Acta 1218:401-407(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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:7519446, PubMed:7688227). The activated receptor in
CC turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and
CC thus activates phospholipase C and increases the cytosolic Ca(2+)
CC concentrations, which in turn triggers cellular responses such as
CC stimulation of protein kinase C (By similarity).
CC {ECO:0000250|UniProtKB:P30556, ECO:0000269|PubMed:7519446,
CC ECO:0000269|PubMed:7688227}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30556};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, liver, kidney, and spleen, with
CC highest expression in the heart. {ECO:0000269|PubMed:7519446,
CC ECO:0000269|PubMed:7688227}.
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; L16463; AAA49647.1; -; mRNA.
DR EMBL; S73388; AAD14966.2; -; mRNA.
DR EMBL; S73274; AAC60749.1; -; mRNA.
DR EMBL; BC059993; AAH59993.1; -; mRNA.
DR PIR; JN0694; JN0694.
DR RefSeq; NP_001083132.1; NM_001089663.1.
DR RefSeq; XP_018117240.1; XM_018261751.1.
DR AlphaFoldDB; P32303; -.
DR SMR; P32303; -.
DR DNASU; 398763; -.
DR GeneID; 398763; -.
DR KEGG; xla:398763; -.
DR CTD; 398763; -.
DR Xenbase; XB-GENE-865228; agtr1.L.
DR OMA; WVPHQIL; -.
DR OrthoDB; 810397at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 398763; Expressed in spleen and 12 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..362
FT /note="Type-1 angiotensin II receptor A"
FT /id="PRO_0000069165"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 27..56
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 57..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 63..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 91..99
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 100..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 127..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 143..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 167..191
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 192..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 218..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 239..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 268..277
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TRANSMEM 278..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT TOPO_DOM 304..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 168
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 185
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT BINDING 200
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT LIPID 361
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 19..273
FT /evidence="ECO:0000250|UniProtKB:P30556"
FT DISULFID 102..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 104
FT /note="V -> I (in Ref. 3; AAH59993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41293 MW; 7E0CA09B185E7D57 CRC64;
MSNASTVETS DVERIAVNCS KSGMHNYIFI AIPIIYSTIF VVGVFGNSMV VIVIYSYMKM
KTVASIFLMN LALSDLCFVI TLPLWAAYTA MHYHWPFGNF LCKVASTAIT LNLYTTVFLL
TCLSIDRYSA IVHPMKSRIW RTAMVARLTC VGIWLVAFLA SMPSIIYRQI YLFHDTNQTV
CAIVYDSGHI YFMVGMSLAK NIVGFLIPFL IILTSYTLIG KTLKEVYRAQ RARNDDIFKM
IVAVVLLFFF CWIPYQVFTF LDVLIQMDVI QNCKMYDIVD TGMPITICIA YFNSCLNPFL
YGFFGKNFRK HFLQLIKYIP PKMRTHASVN TKSSLVSSSL SDTKRASKKI ALQMTDNEEH
CK
