DEAR_RAT
ID DEAR_RAT Reviewed; 127 AA.
AC D3ZGZ6; Q6BDA5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Dual endothelin-1/angiotensin II receptor {ECO:0000303|PubMed:9508787};
DE Short=Dear {ECO:0000303|PubMed:9508787};
DE AltName: Full=Dual endothelin-1/VEGFsp receptor {ECO:0000250|UniProtKB:B0L3A2};
DE Short=DEspR protein {ECO:0000250|UniProtKB:B0L3A2};
DE AltName: Full=FBXW7 antisense RNA 1 homolog {ECO:0000250|UniProtKB:B0L3A2};
GN Name=Fbxw7-as1 {ECO:0000250|UniProtKB:B0L3A2};
GN Synonyms=Dear {ECO:0000312|RGD:1303105};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF ARG-64 AND TRP-65, AND FUNCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=9508787; DOI=10.1007/bf03401733;
RA Ruiz-Opazo N., Hirayama K., Akimoto K., Herrera V.L.;
RT "Molecular characterization of a dual endothelin-1/Angiotensin II
RT receptor.";
RL Mol. Med. 4:96-108(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF SER-44 AND MET-74, AND FUNCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=15561758; DOI=10.1152/physiolgenomics.00108.2004;
RA Kaneko Y., Herrera V.L., Didishvili T., Ruiz-Opazo N.;
RT "Sex-specific effects of dual ET-1/ANG II receptor (Dear) variants in Dahl
RT salt-sensitive/resistant hypertension rat model.";
RL Physiol. Genomics 20:157-164(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Dual endothelin-1/angiotensin-2 receptor that is functionally
CC coupled to a calcium-mobilizing transduction system, responding
CC equivalently to both endothelin-1/EDN1 and angiotensin-2 peptides in a
CC highly specific manner (PubMed:15561758, PubMed:9508787). Also binds
CC the signal peptide of VEGFA (By similarity). May play a role in
CC angiogenesis with a significant role in cardiovascular and neural
CC development (By similarity). {ECO:0000250|UniProtKB:B0L3A2,
CC ECO:0000250|UniProtKB:Q2QKR2, ECO:0000269|PubMed:15561758,
CC ECO:0000269|PubMed:9508787}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9508787};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:B0L3A2,
CC ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Prominently expressed in brain and heart tissues.
CC Weakly expressed in aorta, adrenal gland, and lung tissues.
CC {ECO:0000269|PubMed:9508787}.
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DR EMBL; AY664492; AAT76519.1; -; mRNA.
DR EMBL; AABR07012054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001004448.2; NM_001004448.2.
DR AlphaFoldDB; D3ZGZ6; -.
DR PaxDb; D3ZGZ6; -.
DR Ensembl; ENSRNOT00000042146; ENSRNOP00000039897; ENSRNOG00000033147.
DR GeneID; 446170; -.
DR KEGG; rno:446170; -.
DR CTD; 446170; -.
DR RGD; 1303105; Dear.
DR GeneTree; ENSGT00940000177316; -.
DR HOGENOM; CLU_1969856_0_0_1; -.
DR OrthoDB; 1825385at2759; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000033147; Expressed in frontal cortex.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IMP:RGD.
DR GO; GO:0004962; F:endothelin receptor activity; IMP:RGD.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISS:UniProtKB.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..127
FT /note="Dual endothelin-1/angiotensin II receptor"
FT /id="PRO_0000454052"
FT TOPO_DOM 1..69
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:B0L3A2"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:B0L3A2"
FT MUTAGEN 44
FT /note="S->P: In Dahl R mutant. Does not affect expression
FT levels; when associated with T-74. Loss of angiotensin-2
FT peptide binding; when associated with T-74. Does not affect
FT EDN1 binding; when associated with T-74."
FT /evidence="ECO:0000269|PubMed:15561758"
FT MUTAGEN 64
FT /note="R->G: Abolishes binding with EDN1 without affecting
FT angiotensin-2 peptide binding."
FT /evidence="ECO:0000269|PubMed:9508787"
FT MUTAGEN 65
FT /note="W->G: Abolishes binding with EDN1. Affects binding
FT with angiotensin-2 peptide."
FT /evidence="ECO:0000269|PubMed:9508787"
FT MUTAGEN 74
FT /note="M->T: In Dahl R mutant. Does not affect expression
FT levels; when associated with T-44. Loss of angiotensin-2
FT peptide binding; when associated with T-44. Does not affect
FT EDN1 binding; when associated with T-44."
FT /evidence="ECO:0000269|PubMed:15561758"
FT CONFLICT 4
FT /note="F -> L (in Ref. 1; AAT76519)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 13733 MW; C0D549CB6F61EF65 CRC64;
MSTFYVTAVP KSHSSLPKCQ AMMSRTLLTG MAMYLDSSHA GAASMQVSWP PLLTSLGSKE
MKSRWNWGSI TCIMCFTCVG SQLSMSSSKA SNFSGPLQLY QRGIGHITNP YRRPPAPAWP
CSSSGTT
