ID   AGTR2_MOUSE             Reviewed;         363 AA.
AC   P35374;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Type-2 angiotensin II receptor;
DE   AltName: Full=Angiotensin II type-2 receptor {ECO:0000303|PubMed:8292631};
DE            Short=AT2 receptor {ECO:0000303|PubMed:8726696};
GN   Name=Agtr2 {ECO:0000312|MGI:MGI:87966};
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 [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Fetus;
RX   PubMed=8267573; DOI=10.1006/bbrc.1993.2492;
RA   Nakajima M., Mukoyama M., Pratt R.E., Horiuchi M., Dzau V.J.;
RT   "Cloning of cDNA and analysis of the gene for mouse angiotensin II type 2
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 197:393-399(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=8292631; DOI=10.1016/0005-2736(94)90072-8;
RA   Ichiki T., Herold C.L., Kambayashi Y., Bardhan S., Inagami T.;
RT   "Cloning of the cDNA and the genomic DNA of the mouse angiotensin II type 2
RT   receptor.";
RL   Biochim. Biophys. Acta 1189:247-250(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=8726696; DOI=10.1007/978-1-4899-1376-0_17;
RA   Nahmias C., Cazaubon S.M., Sutren M., Masson M., Lazard D., Villageois P.,
RA   Elbaz N., Strosberg A.D.;
RT   "Molecular and functional characterization of angiotensin II AT2 receptor
RT   in neuroblastoma N1E-115 cells.";
RL   Adv. Exp. Med. Biol. 396:167-173(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ; TISSUE=Liver;
RX   PubMed=7650042; DOI=10.1074/jbc.270.34.20225;
RA   Horiuchi M., Koike G., Yamada T., Mukoyama M., Nakajima M., Dzau V.J.;
RT   "The growth-dependent expression of angiotensin II type 2 receptor is
RT   regulated by transcription factors interferon regulatory factor-1 and -2.";
RL   J. Biol. Chem. 270:20225-20230(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
RN   [7]
RP   DISULFIDE BONDS.
RX   PubMed=11444984; DOI=10.1021/bi002805p;
RA   Heerding J.N., Hines J., Fluharty S.J., Yee D.K.;
RT   "Identification and function of disulfide bridges in the extracellular
RT   domains of the angiotensin II type 2 receptor.";
RL   Biochemistry 40:8369-8377(2001).
RN   [8]
RP   FUNCTION, INTERACTION WITH MTUS1, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15539617; DOI=10.1161/01.atv.0000150662.51436.14;
RA   Wruck C.J., Funke-Kaiser H., Pufe T., Kusserow H., Menk M., Schefe J.H.,
RA   Kruse M.L., Stoll M., Unger T.;
RT   "Regulation of transport of the angiotensin AT2 receptor by a novel
RT   membrane-associated Golgi protein.";
RL   Arterioscler. Thromb. Vasc. Biol. 25:57-64(2005).
CC   -!- FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide
CC       (PubMed:8726696). Signals primarily via a non-canonical G-protein- and
CC       beta-arrestin independent pathways (By similarity). Cooperates with
CC       MTUS1 to inhibit ERK2 activation and cell proliferation
CC       (PubMed:15539617). {ECO:0000250|UniProtKB:P50052,
CC       ECO:0000269|PubMed:15539617, ECO:0000269|PubMed:8726696}.
CC   -!- SUBUNIT: Interacts with MTUS1. {ECO:0000269|PubMed:15539617}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15539617};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P50052}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in adrenal gland and
CC       uterus. {ECO:0000269|PubMed:15539617}.
CC   -!- DOMAIN: Helix VIII may act as a gatekeeper for either suppression or
CC       activation of the receptor, depending on post-translational
CC       modifications and interactions with various receptor partners. Helix
CC       VIII is found in a non-canonical position, stabilizing the active-like
CC       state, but at the same time preventing the recruitment of G-proteins or
CC       beta-arrestins. Upon switching to a membrane-bound conformation, helix
CC       VIII can support the recruitment of G proteins and beta-arrestins.
CC       {ECO:0000250|UniProtKB:P50052}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB49539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; S67465; AAB29336.1; -; mRNA.
DR   EMBL; U04828; AAC52128.1; -; mRNA.
DR   EMBL; U00766; AAC04933.1; -; mRNA.
DR   EMBL; L32840; AAB49539.1; ALT_INIT; mRNA.
DR   EMBL; U11073; AAA82184.1; -; Genomic_DNA.
DR   EMBL; AK086334; BAC39650.1; -; mRNA.
DR   EMBL; BC003811; AAH03811.1; -; mRNA.
DR   CCDS; CCDS40889.1; -.
DR   PIR; I48261; I48261.
DR   RefSeq; NP_031455.1; NM_007429.5.
DR   AlphaFoldDB; P35374; -.
DR   SMR; P35374; -.
DR   STRING; 10090.ENSMUSP00000086592; -.
DR   ChEMBL; CHEMBL4680025; -.
DR   GlyCosmos; P35374; 5 sites, No reported glycans.
DR   GlyGen; P35374; 5 sites.
DR   iPTMnet; P35374; -.
DR   PhosphoSitePlus; P35374; -.
DR   PaxDb; 10090-ENSMUSP00000086592; -.
DR   ProteomicsDB; 282044; -.
DR   Pumba; P35374; -.
DR   Antibodypedia; 29644; 300 antibodies from 36 providers.
DR   DNASU; 11609; -.
DR   Ensembl; ENSMUST00000089188.9; ENSMUSP00000086592.3; ENSMUSG00000068122.11.
DR   GeneID; 11609; -.
DR   KEGG; mmu:11609; -.
DR   UCSC; uc009suq.3; mouse.
DR   AGR; MGI:87966; -.
DR   CTD; 186; -.
DR   MGI; MGI:87966; Agtr2.
DR   VEuPathDB; HostDB:ENSMUSG00000068122; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244888; -.
DR   HOGENOM; CLU_009579_8_3_1; -.
DR   InParanoid; P35374; -.
DR   OMA; STFNCSH; -.
DR   OrthoDB; 4179713at2759; -.
DR   PhylomeDB; P35374; -.
DR   TreeFam; TF330024; -.
DR   Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 11609; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Agtr2; mouse.
DR   PRO; PR:P35374; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P35374; Protein.
DR   Bgee; ENSMUSG00000068122; Expressed in dermis and 114 other cell types or tissues.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004945; F:angiotensin type II receptor activity; IDA:MGI.
DR   GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0002035; P:brain renin-angiotensin system; IDA:MGI.
DR   GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI.
DR   GO; GO:0021695; P:cerebellar cortex development; ISO:MGI.
DR   GO; GO:0042416; P:dopamine biosynthetic process; ISO:MGI.
DR   GO; GO:0035640; P:exploration behavior; IMP:BHF-UCL.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; IDA:BHF-UCL.
DR   GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:BHF-UCL.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; ISO:MGI.
DR   GO; GO:0060993; P:kidney morphogenesis; ISO:MGI.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0010459; P:negative regulation of heart rate; IMP:BHF-UCL.
DR   GO; GO:0032304; P:negative regulation of icosanoid secretion; ISO:MGI.
DR   GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR   GO; GO:0010700; P:negative regulation of norepinephrine secretion; ISO:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR   GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0072300; P:positive regulation of metanephric glomerulus development; IMP:UniProtKB.
DR   GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
DR   GO; GO:0035566; P:regulation of metanephros size; IMP:UniProtKB.
DR   GO; GO:0042306; P:regulation of protein import into nucleus; ISO:MGI.
DR   GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IMP:BHF-UCL.
DR   GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; ISO:MGI.
DR   GO; GO:0042311; P:vasodilation; ISO:MGI.
DR   CDD; cd15191; 7tmA_AT2R; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000147; ATII_AT2_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; PR00636; ANGIOTENSN2R.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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; P35374; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..363
FT                   /note="Type-2 angiotensin II receptor"
FT                   /id="PRO_0000069169"
FT   TOPO_DOM        1..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TRANSMEM        46..70
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TOPO_DOM        71..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TRANSMEM        81..104
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TOPO_DOM        105..114
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TRANSMEM        115..140
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TOPO_DOM        141..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TRANSMEM        160..181
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TOPO_DOM        182..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TRANSMEM        207..232
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TOPO_DOM        233..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TRANSMEM        258..281
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TOPO_DOM        282..294
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TRANSMEM        295..320
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   TOPO_DOM        321..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   REGION          324..333
FT                   /note="Helix VIII"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   BINDING         103
FT                   /ligand="angiotensin II"
FT                   /ligand_id="ChEBI:CHEBI:58506"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   BINDING         104
FT                   /ligand="angiotensin II"
FT                   /ligand_id="ChEBI:CHEBI:58506"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   BINDING         182
FT                   /ligand="angiotensin II"
FT                   /ligand_id="ChEBI:CHEBI:58506"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   BINDING         204
FT                   /ligand="angiotensin II"
FT                   /ligand_id="ChEBI:CHEBI:58506"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   BINDING         215
FT                   /ligand="angiotensin II"
FT                   /ligand_id="ChEBI:CHEBI:58506"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   BINDING         279
FT                   /ligand="angiotensin II"
FT                   /ligand_id="ChEBI:CHEBI:58506"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   BINDING         297
FT                   /ligand="angiotensin II"
FT                   /ligand_id="ChEBI:CHEBI:58506"
FT                   /evidence="ECO:0000250|UniProtKB:P50052"
FT   MOD_RES         354
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        24
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        29
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..290
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT                   ECO:0000269|PubMed:11444984"
FT   DISULFID        117..195
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT                   ECO:0000269|PubMed:11444984"
SQ   SEQUENCE   363 AA;  41374 MW;  6C7D6E3B026D1E80 CRC64;
     MKDNFSFAAT SRNITSSRPF DNLNATGTNE SAFNCSHKPS DKHLEAIPVL YYMIFVIGFA
     VNIVVVSLFC CQKGPKKVSS IYIFNLALAD LLLLATLPLW ATYYSYRYDW LFGPVMCKVF
     GSFLTLNMFA SIFFITCMSV DRYQSVIYPF LSQRRNPWQA SYVVPLVWCM ACLSSLPTFY
     FRDVRTIEYL GVNACIMAFP PEKYAQWSAG IALMKNILGF IIPLIFIATC YFGIRKHLLK
     TNSYGKNRIT RDQVLKMAAA VVLAFIICWL PFHVLTFLDA LTWMGIINSC EVIAVIDLAL
     PFAILLGFTN SCVNPFLYCF VGNRFQQKLR SVFRVPITWL QGKRETMSCR KGSSLREMDT
     FVS
//