AGTR1_CHICK
ID AGTR1_CHICK Reviewed; 359 AA.
AC P79785;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Type-1 angiotensin II receptor;
DE AltName: Full=Angiotensin II type-1 receptor;
DE Short=AT1 receptor;
GN Name=AGTR1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8985144; DOI=10.1016/s0014-5793(96)01264-1;
RA Kempf H., le Moullec J.-M., Corvol P., Gasc J.-M.;
RT "Molecular cloning, expression and tissue distribution of a chicken
RT angiotensin II receptor.";
RL FEBS Lett. 399:198-202(1996).
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 -!- 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; U76704; AAB41201.1; -; mRNA.
DR RefSeq; NP_990488.1; NM_205157.3.
DR RefSeq; XP_015146861.1; XM_015291375.1.
DR RefSeq; XP_015146862.1; XM_015291376.1.
DR RefSeq; XP_015146863.1; XM_015291377.1.
DR RefSeq; XP_015146864.1; XM_015291378.1.
DR RefSeq; XP_015146865.1; XM_015291379.1.
DR RefSeq; XP_015146866.1; XM_015291380.1.
DR RefSeq; XP_015146867.1; XM_015291381.1.
DR AlphaFoldDB; P79785; -.
DR SMR; P79785; -.
DR STRING; 9031.ENSGALP00000039673; -.
DR PaxDb; P79785; -.
DR Ensembl; ENSGALT00000048034; ENSGALP00000057556; ENSGALG00000038512.
DR GeneID; 396065; -.
DR KEGG; gga:396065; -.
DR CTD; 185; -.
DR VEuPathDB; HostDB:geneid_396065; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P79785; -.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 810397at2759; -.
DR PhylomeDB; P79785; -.
DR TreeFam; TF330024; -.
DR Reactome; R-GGA-375276; Peptide ligand-binding receptors.
DR Reactome; R-GGA-416476; G alpha (q) signalling events.
DR PRO; PR:P79785; -.
DR Proteomes; UP000000539; Chromosome 9.
DR Bgee; ENSGALG00000038512; Expressed in muscle tissue and 8 other tissues.
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:Ensembl.
DR GO; GO:0031711; F:bradykinin receptor binding; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:UniProtKB.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0032430; P:positive regulation of phospholipase A2 activity; IEA:Ensembl.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; IEA:Ensembl.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0046718; P:viral entry into host cell; IEA:Ensembl.
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_0000069163"
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"
SQ SEQUENCE 359 AA; 41220 MW; 94FEC1AF9CE4CB4F 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 KTAGSFDAE
