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DEAR_HUMAN
ID   DEAR_HUMAN              Reviewed;          85 AA.
AC   B0L3A2;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Dual endothelin-1/angiotensin II receptor {ECO:0000250|UniProtKB:D3ZGZ6};
DE            Short=Dear {ECO:0000303|PubMed:17446437};
DE   AltName: Full=Dual endothelin-1/VEGFsp receptor {ECO:0000303|PubMed:27301377};
DE            Short=DEspR protein {ECO:0000303|PubMed:27301377};
DE   AltName: Full=FBXW7 antisense RNA 1;
GN   Name=FBXW7-AS1 {ECO:0000312|HGNC:HGNC:52397};
GN   Synonyms=DEAR {ECO:0000303|PubMed:17446437},
GN   DEspR {ECO:0000303|PubMed:27301377};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17446437; DOI=10.1161/01.res.0000267716.96196.60;
RA   Glorioso N., Herrera V.L., Bagamasbad P., Filigheddu F., Troffa C.,
RA   Argiolas G., Bulla E., Decano J.L., Ruiz-Opazo N.;
RT   "Association of ATP1A1 and dear single-nucleotide polymorphism haplotypes
RT   with essential hypertension: sex-specific and haplotype-specific effects.";
RL   Circ. Res. 100:1522-1529(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=24465725; DOI=10.1371/journal.pone.0085821;
RA   Herrera V.L., Decano J.L., Tan G.A., Moran A.M., Pasion K.A., Matsubara Y.,
RA   Ruiz-Opazo N.;
RT   "DEspR roles in tumor vasculo-angiogenesis, invasiveness, CSC-survival and
RT   anoikis resistance: a 'common receptor coordinator' paradigm.";
RL   PLoS ONE 9:e85821-e85821(2014).
RN   [4]
RP   ERRATUM OF PUBMED:24465725.
RA   Herrera V.L., Decano J.L., Tan G.A., Moran A.M., Pasion K.A., Matsubara Y.,
RA   Ruiz-Opazo N.;
RL   PLoS ONE 9:e112335-e112335(2014).
RN   [5]
RP   SUBCELLULAR LOCATION, GLYCOSYLATION, AND TOPOLOGY.
RX   PubMed=27301377; DOI=10.1186/s12867-016-0066-8;
RA   Herrera V.L., Steffen M., Moran A.M., Tan G.A., Pasion K.A., Rivera K.,
RA   Pappin D.J., Ruiz-Opazo N.;
RT   "Confirmation of translatability and functionality certifies the dual
RT   endothelin1/VEGFsp receptor (DEspR) protein.";
RL   BMC Mol. Biol. 17:15-15(2016).
RN   [6]
RP   SUBCELLULAR LOCATION, AND RNA EDITING.
RX   PubMed=33853558; DOI=10.1186/s12885-021-08107-w;
RA   Gromisch C.M., Tan G.L.A., Pasion K.A., Moran A.M., Gromisch M.S.,
RA   Grinstaff M.W., Carr F.J., Herrera V.L.M., Ruiz-Opazo N.;
RT   "Humanized anti-DEspR IgG4S228P antibody increases overall survival in a
RT   pancreatic cancer stem cell-xenograft peritoneal carcinomatosis ratnu/nu
RT   model.";
RL   BMC Cancer 21:407-407(2021).
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:17446437, PubMed:24465725). Also binds
CC       the signal peptide of VEGFA (PubMed:17446437, PubMed:24465725). May
CC       play a role in angiogenesis with a significant role in cardiovascular
CC       and neural development (By similarity). {ECO:0000250|UniProtKB:Q2QKR2,
CC       ECO:0000269|PubMed:17446437, ECO:0000269|PubMed:24465725}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24465725,
CC       ECO:0000269|PubMed:27301377, ECO:0000269|PubMed:33853558}; Single-pass
CC       membrane protein {ECO:0000305|PubMed:27301377}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney (PubMed:17446437). Expressed in
CC       endothelial cells (PubMed:24465725). {ECO:0000269|PubMed:17446437,
CC       ECO:0000269|PubMed:24465725}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:27301377}.
CC   -!- RNA EDITING: Modified_positions=14 {ECO:0000269|PubMed:33853558};
CC       Note=The nonsense codon (UGA) at position 14 is modified to a sense
CC       codon (UGI), which is the equivalent of UGG. ADAR is responsible of
CC       FBXW7-AS1 expression and RNA-editing. {ECO:0000269|PubMed:33853558};
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DR   EMBL; EF212178; ABP04239.1; -; mRNA.
DR   EMBL; AC080078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; B0L3A2; -.
DR   PeptideAtlas; B0L3A2; -.
DR   PRIDE; B0L3A2; -.
DR   HGNC; HGNC:52397; FBXW7-AS1.
DR   neXtProt; NX_B0L3A2; -.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004962; F:endothelin receptor activity; IDA:UniProtKB.
DR   GO; GO:0038085; F:vascular endothelial growth factor binding; IDA:UniProtKB.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Receptor; Reference proteome; RNA editing;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..85
FT                   /note="Dual endothelin-1/angiotensin II receptor"
FT                   /id="PRO_0000452831"
FT   TOPO_DOM        1..18
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:27301377"
FT   TRANSMEM        19..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:27301377"
SQ   SEQUENCE   85 AA;  9677 MW;  FE2D2AA722F8EE1B CRC64;
     MTMFKGSNEM KSRWNWGSIT CIICFTCVGS QLSMSSSKAS NFSGPLQLYQ RELEIFIVLT
     DVPNYRLIKE NSHLHTTIVD QGRTV
 
 
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