AGTR2_MOUSE
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 03-AUG-2022, entry version 171.
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 GlyGen; P35374; 5 sites.
DR iPTMnet; P35374; -.
DR PhosphoSitePlus; P35374; -.
DR PaxDb; P35374; -.
DR PRIDE; P35374; -.
DR ProteomicsDB; 282044; -.
DR Antibodypedia; 29644; 266 antibodies from 36 providers.
DR DNASU; 11609; -.
DR Ensembl; ENSMUST00000089188; ENSMUSP00000086592; ENSMUSG00000068122.
DR GeneID; 11609; -.
DR KEGG; mmu:11609; -.
DR UCSC; uc009suq.3; mouse.
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; 685818at2759; -.
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 73 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 tissues.
DR Genevisible; P35374; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IDA:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0035932; P:aldosterone secretion; ISO: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:0006883; P:cellular sodium ion homeostasis; 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: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: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:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
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 InterPro; IPR000147; ATII_AT2_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; PR00636; ANGIOTENSN2R.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 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
