A0A7J7F2E9 · A0A7J7F2E9_DICBM
- ProteinEphrin type-B receptor 3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1035 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
Catalytic activity
- L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 639-647 | ATP (UniProtKB | ChEBI) | |||
Binding site | 665 | ATP (UniProtKB | ChEBI) | |||
Active site | 758 | Proton acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | dendrite | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | transmembrane-ephrin receptor activity | |
Biological Process | axon guidance | |
Biological Process | protein phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEphrin type-B receptor 3
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7F2E9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 557-582 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-37 | ||||
Chain | PRO_5029473317 | 38-1035 | Ephrin type-B receptor 3 | ||
Disulfide bond | 81↔199 | ||||
Disulfide bond | 116↔126 | ||||
Keywords
- PTM
Interaction
Subunit
Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 39-217 | Eph LBD | |||
Domain | 339-454 | Fibronectin type-III | |||
Domain | 455-548 | Fibronectin type-III | |||
Domain | 633-933 | Protein kinase | |||
Domain | 962-1026 | SAM | |||
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,035
- Mass (Da)113,750
- Last updated2021-04-07 v1
- MD5 Checksum310767073D9F9F7DC80DBE5506642493
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACDTQ010001514 EMBL· GenBank· DDBJ | KAF5922220.1 EMBL· GenBank· DDBJ | Genomic DNA |