AGTRA_MOUSE
ID AGTRA_MOUSE Reviewed; 359 AA.
AC P29754;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Type-1 angiotensin II receptor A {ECO:0000305};
DE AltName: Full=Angiotensin II type-1 receptor A {ECO:0000303|PubMed:1497638};
DE Short=AT1 receptor A {ECO:0000303|PubMed:1599461};
GN Name=Agtr1a; Synonyms=Agtr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1599461; DOI=10.1016/s0006-291x(05)80983-0;
RA Sasamura H., Hein L., Krieger J.E., Pratt R.E., Kobilka B.K., Dzau V.J.;
RT "Cloning, characterization, and expression of two angiotensin receptor (AT-
RT 1) isoforms from the mouse genome.";
RL Biochem. Biophys. Res. Commun. 185:253-259(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1497638; DOI=10.1016/0006-291x(92)90852-c;
RA Yoshida H., Kakuchi J., Guo D.F., Furuta H., Iwai N.,
RA van der Meer-De Jong R., Inagami T., Ichikawa I.;
RT "Analysis of the evolution of angiotensin II type 1 receptor gene in
RT mammals (mouse, rat, bovine and human).";
RL Biochem. Biophys. Res. Commun. 186:1042-1049(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- INTERACTION:
CC P29754; Q9WVK0: Agtrap; NbExp=5; IntAct=EBI-765178, EBI-645964;
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; S37484; AAB22269.1; -; Genomic_DNA.
DR EMBL; BC036175; AAH36175.1; -; mRNA.
DR CCDS; CCDS26415.1; -.
DR PIR; JH0621; JH0621.
DR RefSeq; NP_796296.1; NM_177322.3.
DR RefSeq; XP_006516597.1; XM_006516534.1.
DR RefSeq; XP_011242566.1; XM_011244264.2.
DR AlphaFoldDB; P29754; -.
DR SMR; P29754; -.
DR BioGRID; 198029; 3.
DR CORUM; P29754; -.
DR IntAct; P29754; 2.
DR MINT; P29754; -.
DR STRING; 10090.ENSMUSP00000070958; -.
DR BindingDB; P29754; -.
DR ChEMBL; CHEMBL5741; -.
DR GlyGen; P29754; 3 sites.
DR iPTMnet; P29754; -.
DR PhosphoSitePlus; P29754; -.
DR PaxDb; P29754; -.
DR PRIDE; P29754; -.
DR DNASU; 11607; -.
DR Ensembl; ENSMUST00000066412; ENSMUSP00000070958; ENSMUSG00000049115.
DR GeneID; 11607; -.
DR KEGG; mmu:11607; -.
DR UCSC; uc007pyu.2; mouse.
DR CTD; 11607; -.
DR MGI; MGI:87964; Agtr1a.
DR VEuPathDB; HostDB:ENSMUSG00000049115; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P29754; -.
DR OMA; QVFHFMQ; -.
DR OrthoDB; 810397at2759; -.
DR PhylomeDB; P29754; -.
DR TreeFam; TF330024; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 11607; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Agtr1a; mouse.
DR PRO; PR:P29754; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P29754; protein.
DR Bgee; ENSMUSG00000049115; Expressed in adrenal gland and 161 other tissues.
DR ExpressionAtlas; P29754; baseline and differential.
DR Genevisible; P29754; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0031968; C:organelle outer membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0001596; F:angiotensin type I receptor activity; IDA:MGI.
DR GO; GO:0004945; F:angiotensin type II receptor activity; ISO:MGI.
DR GO; GO:0031711; F:bradykinin receptor binding; ISO:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0042976; P:activation of Janus kinase activity; ISO:MGI.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISO:MGI.
DR GO; GO:0001568; P:blood vessel development; IGI:MGI.
DR GO; GO:0002035; P:brain renin-angiotensin system; IMP:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISO:MGI.
DR GO; GO:0042756; P:drinking behavior; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0002034; P:maintenance of blood vessel diameter homeostasis by renin-angiotensin; ISS:UniProtKB.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0086097; P:phospholipase C-activating angiotensin-activated signaling pathway; ISO:MGI.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:MGI.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:MGI.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:MGI.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0032430; P:positive regulation of phospholipase A2 activity; ISO:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0006885; P:regulation of pH; ISO:MGI.
DR GO; GO:0002019; P:regulation of renal output by angiotensin; IMP:MGI.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IGI:MGI.
DR GO; GO:1905459; P:regulation of vascular associated smooth muscle cell apoptotic process; IGI:MGI.
DR GO; GO:0019229; P:regulation of vasoconstriction; ISO:MGI.
DR GO; GO:0002001; P:renin secretion into blood stream; IMP:MGI.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IMP:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; ISO:MGI.
DR GO; GO:0009651; P:response to salt stress; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0042310; P:vasoconstriction; ISO:MGI.
DR GO; GO:0046718; P:viral entry into host cell; ISO:MGI.
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 1: Evidence at protein 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..359
FT /note="Type-1 angiotensin II receptor A"
FT /id="PRO_0000069155"
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, ECO:0000305"
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 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..351
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 LIPID 355
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
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 7
FT /note="T -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 20..21
FT /note="RA -> IS (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="I -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="M -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40856 MW; 966958A738D8F53E CRC64;
MALNSSTEDG IKRIQDDCPR AGRHSYIFVM IPTLYSIIFV VGIFGNSLVV IVIYFYMKLK
TVASVFLLNL ALADLCFLLT LPLWAVYTAM EYRWPFGNHL CKIASASVSF NLYASVFLLT
CLSIDRYLAI VHPMKSRLRR TMLVAKVTCI IIWLMAGLAS LPAVIHRNVY FIENTNITVC
AFHYESRNST LPIGLGLTKN ILGFLFPFLI ILTSYTLIWK ALKKAYEIQK NKPRNDDIFR
IIMAIVLFFF FSWVPHQIFT FLDVLIQLGV IHDCKIADIV DTAMPITICI AYFNNCLNPL
FYGFLGKKFK KYFLQLLKYI PPKAKSHSSL STKMSTLSYR PSDNMSSAAK KPASCSEVE
