AGTR1_MELGA
ID AGTR1_MELGA Reviewed; 359 AA.
AC P33396; Q92158;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Type-1 angiotensin II receptor;
DE AltName: Full=Angiotensin II type-1 receptor;
DE Short=AT1 receptor;
GN Name=AGTR1;
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Adrenal gland;
RX PubMed=8341266;
RA Murphy T.J., Nakamura Y., Takeuchi K., Alexander R.W.;
RT "A cloned angiotensin receptor isoform from the turkey adrenal gland is
RT pharmacologically distinct from mammalian angiotensin receptors.";
RL Mol. Pharmacol. 44:1-7(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-291.
RX PubMed=7916599; DOI=10.1006/bbrc.1993.1326;
RA Carsia R.V., McIlroy P.J., Kowalski K.I., Tilly J.L.;
RT "Isolation of turkey adrenocortical cell angiotensin II (AII) receptor
RT partial cDNA: evidence for a single-copy gene expressed predominantly in
RT the adrenal gland.";
RL Biochem. Biophys. Res. Commun. 191:1073-1080(1993).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30556};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P30556}.
CC -!- TISSUE SPECIFICITY: Adrenal medulla. {ECO:0000269|PubMed:8341266}.
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; L23203; AAA03560.1; -; mRNA.
DR EMBL; S58041; AAB26041.1; -; mRNA.
DR PIR; I51372; I51372.
DR RefSeq; NP_001290120.1; NM_001303191.1.
DR AlphaFoldDB; P33396; -.
DR SMR; P33396; -.
DR Ensembl; ENSMGAT00000017943; ENSMGAP00000016969; ENSMGAG00000016025.
DR GeneID; 100303701; -.
DR KEGG; mgp:100303701; -.
DR CTD; 185; -.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P33396; -.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 810397at2759; -.
DR TreeFam; TF330024; -.
DR Proteomes; UP000001645; Chromosome 11.
DR Bgee; ENSMGAG00000016025; Expressed in ovary and 11 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS: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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..359
FT /note="Type-1 angiotensin II receptor"
FT /id="PRO_0000069164"
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 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 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 187
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 92
FT /note="Y -> C (in Ref. 2; AAB26041)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..170
FT /note="VIIHRNIF -> SSFIVIY (in Ref. 2; AAB26041)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 41250 MW; 94E2B1AF9CE4CB4F CRC64;
MVPNYSTEET VKRIHVDCPV SGRHSYIYIM VPTVYSIIFI IGIFGNSLVV IVIYCYMKLK
TVASIFLLNL ALADLCFLIT LPLWAAYTAM EYQWPFGNCL CKLASAGISF NLYASVFLLT
CLSIDRYLAI VHPVKSRIRR TMFVARVTCI VIWLLAGVAS LPVIIHRNIF FAENLNMTVC
GFRYDNNNTT LRVGLGLSKN LLGFLIPFLI ILTSYTLIWK TLKKAYQIQR NKTRNDDIFK
MIVAIVFFFF FSWIPHQVFT FLDVLIQLHV ITDCKITDIV DTAMPFTICI AYFNNCLNPF
FYVFFGKNFK KYFLQLIKYI PPNVSTHPSL TTKMSSLSYR PPENIRLPTK KTAGSFDTE
