Q98949 · TYRO3_CHICK
- ProteinTyrosine-protein kinase receptor TYRO3
- GeneTYRO3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids873 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, enhances PI3-kinase activity and activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes (By similarity).
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Cellular Component | receptor complex | |
Molecular Function | ATP binding | |
Molecular Function | transmembrane receptor protein tyrosine kinase activity | |
Biological Process | cell adhesion | |
Biological Process | cell migration | |
Biological Process | nervous system development | |
Biological Process | phagocytosis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein kinase receptor TYRO3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionQ98949
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 29-416 | Extracellular | ||||
Sequence: AGMKFTGSPIKLKVSQGQPVKLNCSLEGMEDPEMLWIKDGAVVQSVDQVYIPVDEDHWIGFLSLKSVERTDSGKYWCQVENGGKKEESQQVWLIVEGVPYFTVEPEDVSVSPNAPFHMACAAVGPPEPVTIVWWMGDSRVGLPDISPSILNVSGINQSTMFSCEAHNVKGLSSSRTATVQIKAMPLPPLNVTVSQVTSSNASVVWVPGFDGRAPLHSCTLQVAESPDGQEVSTEVAPVPPFAYGVQGLKHSTNYSVRVQCSNEMGSSPFTERVYFQTLELAPSSTPQNIHVIQRDPGLVLEWEGVAPDVLKENVLGYRLEWIQDNVTQGEMIVQDTKANLTTWNPLKDLIIRVCVLNSAGCGPWSDLFLLEAQEVMGGQRQPPYGTSW | ||||||
Transmembrane | 417-437 | Helical | ||||
Sequence: VPVALGILTALVTAVALALIL | ||||||
Topological domain | 438-873 | Cytoplasmic | ||||
Sequence: LRKRRKETRFGHAFGSVVGRGDPAVHFRAARSFNREGPELIEATLESVGISDELKTKLKDVLIQEQQFTLGRMLGKGEFGSVREALLKLDDGSFQKVAVKMLKADIFTSTDIEEFLREAACMKEFDHPHVTKLIGVSLRSRPKGRLPIPMVILPFMKHGDLHAFLLMSRIGENPFNLPLQTLLKFMIDIASGMEYLSSKNFIHRDLAARNCMLDENMNVSVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNLYTTHSDVWAFGVTMWEIVTRGQTPYAGIENAEIYNYLISGNRLKQPPECLEDVYDLMCRCWHPEPKLRPSFGVLRSQLEMIRGRMSTLSLSQDPLYVNIGKDKESSVSDPAVHTSFGNTDGDETIAGAAAAAITSDYRYIMSPLCLGDDVEGERHPEGQEGENKSLLYELETEGEKSC |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-28 | |||||
Sequence: MELRRSMALPRLLLLGLWAAALRDGAVA | ||||||
Chain | PRO_0000346114 | 29-873 | Tyrosine-protein kinase receptor TYRO3 | |||
Sequence: AGMKFTGSPIKLKVSQGQPVKLNCSLEGMEDPEMLWIKDGAVVQSVDQVYIPVDEDHWIGFLSLKSVERTDSGKYWCQVENGGKKEESQQVWLIVEGVPYFTVEPEDVSVSPNAPFHMACAAVGPPEPVTIVWWMGDSRVGLPDISPSILNVSGINQSTMFSCEAHNVKGLSSSRTATVQIKAMPLPPLNVTVSQVTSSNASVVWVPGFDGRAPLHSCTLQVAESPDGQEVSTEVAPVPPFAYGVQGLKHSTNYSVRVQCSNEMGSSPFTERVYFQTLELAPSSTPQNIHVIQRDPGLVLEWEGVAPDVLKENVLGYRLEWIQDNVTQGEMIVQDTKANLTTWNPLKDLIIRVCVLNSAGCGPWSDLFLLEAQEVMGGQRQPPYGTSWVPVALGILTALVTAVALALILLRKRRKETRFGHAFGSVVGRGDPAVHFRAARSFNREGPELIEATLESVGISDELKTKLKDVLIQEQQFTLGRMLGKGEFGSVREALLKLDDGSFQKVAVKMLKADIFTSTDIEEFLREAACMKEFDHPHVTKLIGVSLRSRPKGRLPIPMVILPFMKHGDLHAFLLMSRIGENPFNLPLQTLLKFMIDIASGMEYLSSKNFIHRDLAARNCMLDENMNVSVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNLYTTHSDVWAFGVTMWEIVTRGQTPYAGIENAEIYNYLISGNRLKQPPECLEDVYDLMCRCWHPEPKLRPSFGVLRSQLEMIRGRMSTLSLSQDPLYVNIGKDKESSVSDPAVHTSFGNTDGDETIAGAAAAAITSDYRYIMSPLCLGDDVEGERHPEGQEGENKSLLYELETEGEKSC | ||||||
Glycosylation | 51 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 52↔105 | |||||
Sequence: CSLEGMEDPEMLWIKDGAVVQSVDQVYIPVDEDHWIGFLSLKSVERTDSGKYWC | ||||||
Disulfide bond | 148↔191 | |||||
Sequence: CAAVGPPEPVTIVWWMGDSRVGLPDISPSILNVSGINQSTMFSC | ||||||
Glycosylation | 179 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 184 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 218 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 228 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 281 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 353 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 367 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 673 | Phosphotyrosine; by autocatalysis | ||||
Sequence: Y |
Post-translational modification
Autophosphorylated on tyrosine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Detected in embryonic retina (at protein level). detected in brain, retina, kidney and in retinal Mueller glia-like cells.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-116 | Ig-like C2-type 1 | ||||
Sequence: AGMKFTGSPIKLKVSQGQPVKLNCSLEGMEDPEMLWIKDGAVVQSVDQVYIPVDEDHWIGFLSLKSVERTDSGKYWCQVENGGKKEES | ||||||
Domain | 127-208 | Ig-like C2-type 2 | ||||
Sequence: PYFTVEPEDVSVSPNAPFHMACAAVGPPEPVTIVWWMGDSRVGLPDISPSILNVSGINQSTMFSCEAHNVKGLSSSRTATVQ | ||||||
Domain | 215-308 | Fibronectin type-III 1 | ||||
Sequence: PPLNVTVSQVTSSNASVVWVPGFDGRAPLHSCTLQVAESPDGQEVSTEVAPVPPFAYGVQGLKHSTNYSVRVQCSNEMGSSPFTERVYFQTLEL | ||||||
Domain | 310-403 | Fibronectin type-III 2 | ||||
Sequence: PSSTPQNIHVIQRDPGLVLEWEGVAPDVLKENVLGYRLEWIQDNVTQGEMIVQDTKANLTTWNPLKDLIIRVCVLNSAGCGPWSDLFLLEAQEV | ||||||
Domain | 505-776 | Protein kinase | ||||
Sequence: FTLGRMLGKGEFGSVREALLKLDDGSFQKVAVKMLKADIFTSTDIEEFLREAACMKEFDHPHVTKLIGVSLRSRPKGRLPIPMVILPFMKHGDLHAFLLMSRIGENPFNLPLQTLLKFMIDIASGMEYLSSKNFIHRDLAARNCMLDENMNVSVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNLYTTHSDVWAFGVTMWEIVTRGQTPYAGIENAEIYNYLISGNRLKQPPECLEDVYDLMCRCWHPEPKLRPSFGVLRSQLEMI | ||||||
Region | 845-873 | Disordered | ||||
Sequence: VEGERHPEGQEGENKSLLYELETEGEKSC |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length873
- Mass (Da)96,402
- Last updated1997-02-01 v1
- Checksum6294E173C5D8104E
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U70045 EMBL· GenBank· DDBJ | AAC60041.1 EMBL· GenBank· DDBJ | mRNA |