P56497 · EDNRB_CANLF
- ProteinEndothelin receptor type B
- GeneEDNRB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids442 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | endothelin receptor activity | |
Biological Process | calcium-mediated signaling | |
Biological Process | developmental pigmentation | |
Biological Process | endothelin receptor signaling pathway | |
Biological Process | enteric nervous system development | |
Biological Process | regulation of blood pressure | |
Biological Process | vasoconstriction |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameEndothelin receptor type B
- Short namesET-B; ET-BR
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionP56497
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: internalized after activation by endothelins.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 27-101 | Extracellular | ||||
Sequence: EERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCEGSIEIKETFK | ||||||
Transmembrane | 102-126 | Helical; Name=1 | ||||
Sequence: YINTVVSCLVFVLGIIGNSTLLRII | ||||||
Topological domain | 127-137 | Cytoplasmic | ||||
Sequence: YKNKCMRNGPN | ||||||
Transmembrane | 138-163 | Helical; Name=2 | ||||
Sequence: ILIASLALGDLLHIIIDIPITVYKLL | ||||||
Topological domain | 164-175 | Extracellular | ||||
Sequence: AEDWPFGVEMCK | ||||||
Transmembrane | 176-197 | Helical; Name=3 | ||||
Sequence: LVPFIQKASVGITVLSLCALSI | ||||||
Topological domain | 198-218 | Cytoplasmic | ||||
Sequence: DRYRAVASWSRIKGIGVPKWT | ||||||
Transmembrane | 219-243 | Helical; Name=4 | ||||
Sequence: AVEIVLIWVVSVVLAVPEAVGFDMI | ||||||
Topological domain | 244-271 | Extracellular | ||||
Sequence: TIDYKGRYLRICLLHPTQKTAFMQFYKT | ||||||
Transmembrane | 272-296 | Helical; Name=5 | ||||
Sequence: AKDWWLFSFYFCLPLAITAFFYTLM | ||||||
Topological domain | 297-324 | Cytoplasmic | ||||
Sequence: TCEMLRKKSGMQIALNDHLKQRREVAKT | ||||||
Transmembrane | 325-350 | Helical; Name=6 | ||||
Sequence: VFCLVLVFALCWLPLHLSRILKLTIY | ||||||
Topological domain | 351-362 | Extracellular | ||||
Sequence: DQNDPNRCELLS | ||||||
Transmembrane | 363-389 | Helical; Name=7 | ||||
Sequence: FLLVLDYIGINMASLNSCINPIALYLV | ||||||
Topological domain | 390-442 | Cytoplasmic | ||||
Sequence: SKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MQPPPSLCGRALVALVLACGLSRIWG | ||||||
Chain | PRO_0000012727 | 27-442 | Endothelin receptor type B | |||
Sequence: EERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCEGSIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIIIDIPITVYKLLAEDWPFGVEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAVGFDMITIDYKGRYLRICLLHPTQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTIYDQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS | ||||||
Glycosylation | 59 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 174↔255 | |||||
Sequence: CKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAVGFDMITIDYKGRYLRIC | ||||||
Modified residue | 305 | Phosphoserine | ||||
Sequence: S | ||||||
Lipidation | 402 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 403 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Lipidation | 405 | S-palmitoyl cysteine | ||||
Sequence: C | ||||||
Modified residue | 419 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 439 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 440 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 441 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 442 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 69-88 | Disordered | ||||
Sequence: AEVPKGDRTAGSPPRTISPP |
Sequence similarities
Belongs to the G-protein coupled receptor 1 family. Endothelin receptor subfamily. EDNRB sub-subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length442
- Mass (Da)49,722
- Last updated2005-04-12 v3
- Checksum3E9EE7AE581D7E15
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB183285 EMBL· GenBank· DDBJ | BAD83850.1 EMBL· GenBank· DDBJ | mRNA | ||
AF034530 EMBL· GenBank· DDBJ | AAC26970.1 EMBL· GenBank· DDBJ | mRNA |