P21451 (EDNRB_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endothelin B receptor
Short name=ET-B
Short name=ET-BR

Alternative name(s):
Endothelin receptor non-selective type

Gene names

Name:

Ednrb

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	442 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Tissue specificity	Widely distributed in cell types of a variety of tissues.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRB sub-subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger Inferred from mutant phenotype. Source: RGD aging Inferred from expression pattern. Source: RGD cGMP-mediated signaling Inferred from mutant phenotype. Source: RGD cellular response to lipopolysaccharide Inferred from expression pattern. Source: RGD elevation of cytosolic calcium ion concentration Inferred from direct assay Ref.2. Source: RGD enteric nervous system development Inferred from genetic interaction. Source: RGD epithelial fluid transport Inferred from mutant phenotype. Source: RGD melanocyte differentiation Inferred from direct assay. Source: RGD negative regulation of apoptotic process Inferred from mutant phenotype. Source: RGD positive regulation of cell proliferation Inferred from mutant phenotype. Source: RGD positive regulation of penile erection Inferred from mutant phenotype. Source: RGD positive regulation of protein phosphorylation Inferred from direct assay. Source: RGD positive regulation of renal sodium excretion Inferred from mutant phenotype. Source: RGD positive regulation of urine volume Inferred from mutant phenotype. Source: RGD regulation of blood pressure Inferred from mutant phenotype. Source: RGD regulation of epithelial cell proliferation Inferred from mutant phenotype. Source: RGD regulation of sensory perception of pain Inferred from mutant phenotype. Source: RGD response to organic cyclic compound Inferred from expression pattern. Source: RGD response to pain Inferred from mutant phenotype. Source: RGD sensory perception of pain Inferred from mutant phenotype. Source: RGD vasoconstriction Inferred from mutant phenotype. Source: RGD vasodilation Inferred from mutant phenotype. Source: RGD
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from direct assay. Source: RGD membrane raft Inferred from direct assay. Source: RGD nuclear membrane Inferred from direct assay. Source: RGD plasma membrane Inferred from direct assay. Source: RGD
Molecular function	endothelin receptor activity Inferred from direct assay Ref.2. Source: RGD type 1 angiotensin receptor binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 26	26	Potential
	Chain	27 – 442	416	Endothelin B receptor		PRO_0000012733
Regions
	Topological domain	27 – 101	75	Extracellular Potential
	Transmembrane	102 – 126	25	Helical; Name=1; Potential
	Topological domain	127 – 137	11	Cytoplasmic Potential
	Transmembrane	138 – 163	26	Helical; Name=2; Potential
	Topological domain	164 – 175	12	Extracellular Potential
	Transmembrane	176 – 197	22	Helical; Name=3; Potential
	Topological domain	198 – 218	21	Cytoplasmic Potential
	Transmembrane	219 – 243	25	Helical; Name=4; Potential
	Topological domain	244 – 271	28	Extracellular Potential
	Transmembrane	272 – 296	25	Helical; Name=5; Potential
	Topological domain	297 – 324	28	Cytoplasmic Potential
	Transmembrane	325 – 350	26	Helical; Name=6; Potential
	Topological domain	351 – 362	12	Extracellular Potential
	Transmembrane	363 – 389	27	Helical; Name=7; Potential
	Topological domain	390 – 442	53	Cytoplasmic Potential
Amino acid modifications
	Lipidation	402	1	S-palmitoyl cysteine Potential
	Lipidation	403	1	S-palmitoyl cysteine Potential
	Lipidation	405	1	S-palmitoyl cysteine Potential
	Glycosylation	60	1	N-linked (GlcNAc...) Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Disulfide bond	174 ↔ 255		By similarity
Experimental info
	Sequence conflict	66 – 69	4	SSAP → FRT in CAA40916. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P21451 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: BDA628D78E8071CB	FASTA	442	49,455
	10 20 30 40 50 60 MQSSASRCGR ALVALLLACG LLGVWGEKRG FPPAQATPSL LGTKEVMTPP TKTSWTRGSN 70 80 90 100 110 120 SSLMRSSAPA EVTKGGRVAG VPPRSFPPPC QRKIEINKTF KYINTIVSCL VFVLGIIGNS 130 140 150 160 170 180 TLLRIIYKNK CMRNGPNILI ASLALGDLLH IIIDIPINAY KLLAGDWPFG AEMCKLVPFI 190 200 210 220 230 240 QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF 250 260 270 280 290 300 DVITSDYKGK PLRVCMLNPF QKTAFMQFYK TAKDWWLFSF YFCLPLAITA IFYTLMTCEM 310 320 330 340 350 360 LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTLY DQSNPQRCEL 370 380 390 400 410 420 LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQTFEE KQSLEEKQSC 430 440 LKFKANDHGY DNFRSSNKYS SS

References

[1]	"Distinct tissue distribution and cellular localization of two messenger ribonucleic acids encoding different subtypes of rat endothelin receptors." Hori S., Komatsu Y., Shigemoto R., Mizuno N., Nakanishi S. Endocrinology 130:1885-1895(1992) [PubMed: 1312429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	"Cloning of a cDNA encoding a non-isopeptide-selective subtype of the endothelin receptor." Sakurai T., Yanagisawa M., Takuwa Y., Miyazaki H., Kimura S., Goto K., Masaki T. Nature 348:732-735(1990) [PubMed: 2175397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[3]	"Alternative transcript of the nonselective-type endothelin receptor from rat brain." Cheng H.F., Su Y.M., Yeh J.R., Chang K.J. Mol. Pharmacol. 44:533-538(1993) [PubMed: 8371713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X57764 mRNA. Translation: CAA40916.1. S65355 mRNA. Translation: AAB28172.1.
IPI	IPI00203268.
PIR	S13425.
RefSeq	NP_059029.1. NM_017333.1.
UniGene	Rn.11412.
3D structure databases
ProteinModelPortal	P21451.
ModBase	Search...
Protein-protein interaction databases
STRING	P21451.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P21451.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	50672.
KEGG	rno:50672.
Organism-specific databases
CTD	1910.
RGD	2536. Ednrb.
Phylogenomic databases
HOVERGEN	HBG051443.
Gene expression databases
Genevestigator	P21451.
Family and domain databases
InterPro	IPR000276. 7TM_GPCR_Rhodpsn. IPR000499. Endthln_rcpt. IPR001112. ETB_rcpt. IPR017452. GPCR_Rhodpsn_supfam. [Graphical view]
KO	K04198.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00571. ENDOTHELINBR. PR00366. ENDOTHELINR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	610502.

Entry information

Entry name

EDNRB_RAT

Accession

Primary (citable) accession number: P21451

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program