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P28088 (EDNRB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endothelin B receptor

Short name=ET-B
Short name=ET-BR
Alternative name(s):
Endothelin receptor non-selective type
Gene names
Name:EDNRB
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processenteric nervous system development

Inferred from electronic annotation. Source: Ensembl

enteric smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

macrophage chemotaxis

Inferred from electronic annotation. Source: Ensembl

melanocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cellular protein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron maturation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

neural crest cell migration

Inferred from electronic annotation. Source: Ensembl

peripheral nervous system development

Inferred from electronic annotation. Source: Ensembl

posterior midgut development

Inferred from electronic annotation. Source: Ensembl

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of pH

Inferred from electronic annotation. Source: Ensembl

vein smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionendothelin receptor activity

Inferred from electronic annotation. Source: Ensembl

peptide hormone binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.1 Ref.5
Chain27 – 441415Endothelin B receptor
PRO_0000012726

Regions

Topological domain27 – 10074Extracellular Potential
Transmembrane101 – 12525Helical; Name=1; Potential
Topological domain126 – 13611Cytoplasmic Potential
Transmembrane137 – 16226Helical; Name=2; Potential
Topological domain163 – 17412Extracellular Potential
Transmembrane175 – 19622Helical; Name=3; Potential
Topological domain197 – 21721Cytoplasmic Potential
Transmembrane218 – 24225Helical; Name=4; Potential
Topological domain243 – 27028Extracellular Potential
Transmembrane271 – 29525Helical; Name=5; Potential
Topological domain296 – 32328Cytoplasmic Potential
Transmembrane324 – 34926Helical; Name=6; Potential
Topological domain350 – 36112Extracellular Potential
Transmembrane362 – 38827Helical; Name=7; Potential
Topological domain389 – 44153Cytoplasmic Potential

Amino acid modifications

Modified residue3041Phosphoserine Ref.5
Modified residue4181Phosphoserine Ref.5
Modified residue4341Phosphoserine Probable
Modified residue4351Phosphoserine Probable
Modified residue4381Phosphotyrosine Ref.5
Modified residue4391Phosphoserine Ref.5
Modified residue4401Phosphoserine Ref.5
Modified residue4411Phosphoserine Ref.5
Lipidation4021S-palmitoyl cysteine Ref.5
Lipidation4041S-palmitoyl cysteine Ref.5
Disulfide bond173 ↔ 254 By similarity

Sequences

Sequence LengthMass (Da)Tools
P28088 [UniParc].

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

FASTA44149,371
        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' 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, PALMITOYLATION AT CYS-402 AND CYS-404, PHOSPHORYLATION AT SER-304; SER-418; TYR-438; SER-439; SER-440 AND SER-441, IDENTIFICATION BY MASS SPECTROMETRY.
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.
PIRA41591.
RefSeqNP_776734.1. NM_174309.2.
XP_005213931.1. XM_005213874.1.
UniGeneBt.487.

3D structure databases

ProteinModelPortalP28088.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000043840.

Chemistry

BindingDBP28088.
ChEMBLCHEMBL4401.

Protein family/group databases

GPCRDBSearch...

Proteomic databases

PRIDEP28088.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000006979; ENSBTAP00000006979; ENSBTAG00000005299.
GeneID281750.
KEGGbta:281750.

Organism-specific databases

CTD1910.

Phylogenomic databases

eggNOGNOG278704.
GeneTreeENSGT00690000101856.
HOGENOMHOG000272623.
HOVERGENHBG051443.
InParanoidP28088.
KOK04198.
OMALHIVIDI.
OrthoDBEOG7HHWS4.
TreeFamTF331292.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000499. Endthln_rcpt.
IPR001112. ETB_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00571. ENDOTHELINBR.
PR00366. ENDOTHELINR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805669.

Entry information

Entry nameEDNRB_BOVIN
AccessionPrimary (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: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries