Endothelin B receptor precursor - Bos taurus (Bovine)

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P28088 (EDNRB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
Post-translational modification	It is not sure whether phosphorylation is on Ser-434 or Ser-435.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRB sub-subfamily.
Caution	N-terminal sequencing (Ref.5) indicates the presence of a signal peptide but an unprocessed form where the signal sequence is not cleaved has also been detected (Ref.4). It is unclear if this exists in vivo.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: InterPro enteric nervous system development Inferred from electronic annotation. Source: Compara enteric smooth muscle cell differentiation Inferred from electronic annotation. Source: Compara macrophage chemotaxis Inferred from electronic annotation. Source: Compara melanocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of cellular protein metabolic process Inferred from electronic annotation. Source: Compara negative regulation of neuron maturation Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara neural crest cell migration Inferred from electronic annotation. Source: Compara peripheral nervous system development Inferred from electronic annotation. Source: Compara posterior midgut development Inferred from electronic annotation. Source: Compara regulation of blood pressure Inferred from electronic annotation. Source: Compara regulation of pH Inferred from electronic annotation. Source: Compara vein smooth muscle contraction Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	endothelin receptor activity Inferred from electronic annotation. Source: Compara peptide hormone binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

Ref.1 Ref.5

Chain

27 – 441

415

Endothelin B receptor

PRO_0000012726

Regions

Topological domain

27 – 100

Extracellular Potential

Transmembrane

101 – 125

Helical; Name=1; Potential

Topological domain

126 – 136

Cytoplasmic Potential

Transmembrane

137 – 162

Helical; Name=2; Potential

Topological domain

163 – 174

Extracellular Potential

Transmembrane

175 – 196

Helical; Name=3; Potential

Topological domain

197 – 217

Cytoplasmic Potential

Transmembrane

218 – 242

Helical; Name=4; Potential

Topological domain

243 – 270

Extracellular Potential

Transmembrane

271 – 295

Helical; Name=5; Potential

Topological domain

296 – 323

Cytoplasmic Potential

Transmembrane

324 – 349

Helical; Name=6; Potential

Topological domain

350 – 361

Extracellular Potential

Transmembrane

362 – 388

Helical; Name=7; Potential

Topological domain

389 – 441

Cytoplasmic Potential

Amino acid modifications

Modified residue

304

Phosphoserine

Modified residue

418

Phosphoserine

Modified residue

434

Phosphoserine Probable

Modified residue

435

Phosphoserine Probable

Modified residue

438

Phosphotyrosine

Modified residue

439

Phosphoserine

Modified residue

440

Phosphoserine

Modified residue

441

Phosphoserine

Lipidation

402

S-palmitoyl cysteine

Lipidation

404

S-palmitoyl cysteine

Disulfide bond

173 ↔ 254

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P28088 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: F634462C544DB0D2
Show »

FASTA

441

49,371

        10         20         30         40         50         60 
MQPLPSLCGR ALVALILACG VAGIQAEERE FPPAGATQPL PGTGEMMETP TETSWPGRSN 

        70         80         90        100        110        120 
ASDPRSSATP QIPRGGRMAG IPPRTPPPCD GPIEIKETFK YINTVVSCLV FVLGIIGNST 

       130        140        150        160        170        180 
LLRIIYKNKC MRNGPNILIA SLALGDLLHI IIDIPINTYK LLAKDWPFGV EMCKLVPFIQ 

       190        200        210        220        230        240 
KASVGITVLS LCALSIDRYR AVASWSRIKG IGVPKWTAVE IVLIWVVSVV LAVPEAVGFD 

       250        260        270        280        290        300 
IITSDHIGNK LRICLLHPTQ KTAFMQFYKT AKDWWLFSFY FCLPLAITAL FYTLMTCEML 

       310        320        330        340        350        360 
RKKSGMQIAL NDHLKQRREV AKTVFCLVLV FALCWLPLHL SRILKLTLYD QHDPRRCEFL 

       370        380        390        400        410        420 
SFLLVLDYIG INMASLNSCI NPIALYLVSK RFKNCFKSCL CCWCQSFEEK QSLEEKQSCL 

       430        440 
KFKANDHGYD NFRSSNKYSS S

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of bovine endothelin ETB receptor and identification of signal peptidase and metal proteinase cleavage sites." Saito Y., Mizuno T., Itakura M., Suzuki Y., Ito T., Hagiwara H., Hirose S. J. Biol. Chem. 266:23433-23437(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thymus.
[3]	"Purification and characterization of bovine lung endothelin receptor." Kozuka M., Ito T., Hirose S., Lodhi K.M., Hagiwara H. J. Biol. Chem. 266:16892-16896(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 124-127; 262-269; 304-315; 417-421 AND 424-432. Tissue: Lung.
[4]	"Isolation of the endothelin B receptor from bovine lung. Structure, signal sequence, and binding site." Hick S., Heidemann I., Soskic V., Muller-Esterl W., Godovac-Zimmermann J. Eur. J. Biochem. 234:251-257(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Lung.
[5]	"Post-translational modifications of endothelin receptor B from bovine lungs analyzed by mass spectrometry." Roos M., Soskic V., Poznanovic S., Godovac-Zimmermann J. J. Biol. Chem. 273:924-931(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-32, POST-TRANSLATIONAL MODIFICATIONS. Tissue: Lung.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D10994 Genomic DNA. Translation: BAA01762.1. D90456 mRNA. Translation: BAA14422.1. BC120256 mRNA. Translation: AAI20257.1.
IPI	IPI00689046.
PIR	A41591.
RefSeq	NP_776734.1. NM_174309.2.
UniGene	Bt.487.
3D structure databases
ProteinModelPortal	P28088.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000043840.
Protein family/group databases
GPCRDB	Search...
Proteomic databases
PRIDE	P28088.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000006979; ENSBTAP00000006979; ENSBTAG00000005299.
GeneID	281750.
KEGG	bta:281750.
Organism-specific databases
CTD	1910.
Phylogenomic databases
eggNOG	NOG278704.
GeneTree	ENSGT00690000101856.
HOGENOM	HOG000272623.
HOVERGEN	HBG051443.
InParanoid	P28088.
KO	K04198.
OMA	LHIVIDI.
OrthoDB	EOG45HRX3.
Gene expression databases
ArrayExpress	P28088.
Family and domain databases
InterPro	IPR000499. Endthln_rcpt. IPR001112. ETB_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
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
BindingDB	P28088.
ChEMBL	CHEMBL4401.
NextBio	20805669.

Entry information

Entry name

EDNRB_BOVIN

Accession

Primary (citable) accession number: P28088
Secondary accession number(s): Q0VCB3, Q9TSB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents