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   27-MAR-2024, entry version 198.
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; 3.
DR   MINT; P29754; -.
DR   STRING; 10090.ENSMUSP00000070958; -.
DR   BindingDB; P29754; -.
DR   ChEMBL; CHEMBL5741; -.
DR   GlyCosmos; P29754; 3 sites, No reported glycans.
DR   GlyGen; P29754; 3 sites.
DR   iPTMnet; P29754; -.
DR   PhosphoSitePlus; P29754; -.
DR   PaxDb; 10090-ENSMUSP00000070958; -.
DR   DNASU; 11607; -.
DR   Ensembl; ENSMUST00000066412.8; ENSMUSP00000070958.8; ENSMUSG00000049115.16.
DR   GeneID; 11607; -.
DR   KEGG; mmu:11607; -.
DR   UCSC; uc007pyu.2; mouse.
DR   AGR; MGI:87964; -.
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; 4179713at2759; -.
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 77 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 163 other cell types or tissues.
DR   ExpressionAtlas; P29754; baseline and differential.
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:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; 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:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; 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: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: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:0010744; P:positive regulation of macrophage derived foam cell differentiation; 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   CDD; cd15192; 7tmA_AT1R; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000190; ATII_AT1_rcpt.
DR   InterPro; IPR000248; ATII_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF951; APELIN RECEPTOR; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P29754; MM.
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
//