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Type-2 angiotensin II receptor (Angiotensin II type-2 receptor) (AT2)

 AGTR2_MOUSE             Reviewed;         363 AA.
P35374;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
07-NOV-2018, entry version 149.
RecName: Full=Type-2 angiotensin II receptor;
AltName: Full=Angiotensin II type-2 receptor;
Short=AT2;
Name=Agtr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Fetus;
PubMed=8267573; DOI=10.1006/bbrc.1993.2492;
Nakajima M., Mukoyama M., Pratt R.E., Horiuchi M., Dzau V.J.;
"Cloning of cDNA and analysis of the gene for mouse angiotensin II
type 2 receptor.";
Biochem. Biophys. Res. Commun. 197:393-399(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=8292631; DOI=10.1016/0005-2736(94)90072-8;
Ichiki T., Herold C.L., Kambayashi Y., Bardhan S., Inagami T.;
"Cloning of the cDNA and the genomic DNA of the mouse angiotensin II
type 2 receptor.";
Biochim. Biophys. Acta 1189:247-250(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8726696;
Nahmias C., Cazaubon S.M., Sutren M., Masson M., Lazard D.,
Villageois P., Elbaz N., Strosberg A.D.;
"Molecular and functional characterization of angiotensin II AT2
receptor in neuroblastoma N1E-115 cells.";
Adv. Exp. Med. Biol. 396:167-173(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=7650042; DOI=10.1074/jbc.270.34.20225;
Horiuchi M., Koike G., Yamada T., Mukoyama M., Nakajima M., Dzau V.J.;
"The growth-dependent expression of angiotensin II type 2 receptor is
regulated by transcription factors interferon regulatory factor-1 and
-2.";
J. Biol. Chem. 270:20225-20230(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
DISULFIDE BONDS.
PubMed=11444984; DOI=10.1021/bi002805p;
Heerding J.N., Hines J., Fluharty S.J., Yee D.K.;
"Identification and function of disulfide bridges in the extracellular
domains of the angiotensin II type 2 receptor.";
Biochemistry 40:8369-8377(2001).
[8]
FUNCTION, INTERACTION WITH MTUS1, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
PubMed=15539617; DOI=10.1161/01.ATV.0000150662.51436.14;
Wruck C.J., Funke-Kaiser H., Pufe T., Kusserow H., Menk M.,
Schefe J.H., Kruse M.L., Stoll M., Unger T.;
"Regulation of transport of the angiotensin AT2 receptor by a novel
membrane-associated Golgi protein.";
Arterioscler. Thromb. Vasc. Biol. 25:57-64(2005).
-!- FUNCTION: Receptor for angiotensin II. Cooperates with MTUS1 to
inhibit ERK2 activation and cell proliferation.
{ECO:0000269|PubMed:15539617}.
-!- SUBUNIT: Interacts with MTUS1. {ECO:0000269|PubMed:15539617}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15539617};
Multi-pass membrane protein {ECO:0000269|PubMed:15539617}.
-!- TISSUE SPECIFICITY: Expressed at highest levels in adrenal gland
and uterus. {ECO:0000269|PubMed:15539617}.
-!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=AAB49539.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; S67465; AAB29336.1; -; mRNA.
EMBL; U04828; AAC52128.1; -; mRNA.
EMBL; U00766; AAC04933.1; -; mRNA.
EMBL; L32840; AAB49539.1; ALT_INIT; mRNA.
EMBL; U11073; AAA82184.1; -; Genomic_DNA.
EMBL; AK086334; BAC39650.1; -; mRNA.
EMBL; BC003811; AAH03811.1; -; mRNA.
CCDS; CCDS40889.1; -.
PIR; I48261; I48261.
RefSeq; NP_031455.1; NM_007429.5.
UniGene; Mm.2679; -.
ProteinModelPortal; P35374; -.
SMR; P35374; -.
STRING; 10090.ENSMUSP00000086592; -.
iPTMnet; P35374; -.
PhosphoSitePlus; P35374; -.
PaxDb; P35374; -.
PRIDE; P35374; -.
Ensembl; ENSMUST00000089188; ENSMUSP00000086592; ENSMUSG00000068122.
GeneID; 11609; -.
KEGG; mmu:11609; -.
UCSC; uc009suq.3; mouse.
CTD; 186; -.
MGI; MGI:87966; Agtr2.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000119055; -.
HOVERGEN; HBG104998; -.
InParanoid; P35374; -.
KO; K04167; -.
OMA; HKPSDKH; -.
OrthoDB; EOG091G0HEN; -.
PhylomeDB; P35374; -.
TreeFam; TF330024; -.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
Reactome; R-MMU-418594; G alpha (i) signalling events.
PRO; PR:P35374; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000068122; Expressed in 138 organ(s), highest expression level in efferent duct.
CleanEx; MM_AGTR2; -.
Genevisible; P35374; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0004945; F:angiotensin type II receptor activity; IDA:MGI.
GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0035932; P:aldosterone secretion; ISO:MGI.
GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; IMP:MGI.
GO; GO:0002035; P:brain renin-angiotensin system; IDA:MGI.
GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISO:MGI.
GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:MGI.
GO; GO:0021695; P:cerebellar cortex development; ISO:MGI.
GO; GO:0042416; P:dopamine biosynthetic process; ISO:MGI.
GO; GO:0035640; P:exploration behavior; IMP:BHF-UCL.
GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IGI:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:BHF-UCL.
GO; GO:0060993; P:kidney morphogenesis; ISO:MGI.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
GO; GO:0010459; P:negative regulation of heart rate; IMP:BHF-UCL.
GO; GO:0032304; P:negative regulation of icosanoid secretion; ISO:MGI.
GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
GO; GO:0010700; P:negative regulation of norepinephrine secretion; ISO:MGI.
GO; GO:0097755; P:positive regulation of blood vessel diameter; ISO:MGI.
GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0050715; P:positive regulation of cytokine secretion; ISO:MGI.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0072300; P:positive regulation of metanephric glomerulus development; IMP:UniProtKB.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:0035815; P:positive regulation of renal sodium excretion; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0035566; P:regulation of metanephros size; IMP:UniProtKB.
GO; GO:0042306; P:regulation of protein import into nucleus; ISO:MGI.
GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IMP:BHF-UCL.
GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; ISO:MGI.
GO; GO:0042311; P:vasodilation; ISO:MGI.
CDD; cd15191; 7tmA_AT2R; 1.
InterPro; IPR000147; ATII_AT2_rcpt.
InterPro; IPR000248; ATII_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00241; ANGIOTENSINR.
PRINTS; PR00636; ANGIOTENSN2R.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 363 Type-2 angiotensin II receptor.
/FTId=PRO_0000069169.
TOPO_DOM 1 45 Extracellular. {ECO:0000255}.
TRANSMEM 46 71 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 72 80 Cytoplasmic. {ECO:0000255}.
TRANSMEM 81 102 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 103 119 Extracellular. {ECO:0000255}.
TRANSMEM 120 140 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 141 160 Cytoplasmic. {ECO:0000255}.
TRANSMEM 161 179 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 180 208 Extracellular. {ECO:0000255}.
TRANSMEM 209 234 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 235 256 Cytoplasmic. {ECO:0000255}.
TRANSMEM 257 278 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 279 297 Extracellular. {ECO:0000255}.
TRANSMEM 298 318 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 319 363 Cytoplasmic. {ECO:0000255}.
MOD_RES 354 354 Phosphoserine; by PKC. {ECO:0000255}.
CARBOHYD 4 4 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 13 13 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 24 24 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 29 29 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 290 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:11444984}.
DISULFID 117 195 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:11444984}.
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


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