P18475 · TORSO_DROME
- ProteinTyrosine-protein kinase receptor torso
- Genetor
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids923 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Probable receptor tyrosine kinase which is required for determination of anterior and posterior terminal structures in the embryo (PubMed:2927509, PubMed:8423783).
During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone Ptth (PubMed:19965758).
Binding to Ptth stimulates activation of canonical MAPK signaling leading to ERK phosphorylation (By similarity).
During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone Ptth (PubMed:19965758).
Binding to Ptth stimulates activation of canonical MAPK signaling leading to ERK phosphorylation (By similarity).
Catalytic activity
- ATP + L-tyrosyl-[protein] = ADP + H+ + O-phospho-L-tyrosyl-[protein]
Cofactor
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 | metal ion binding | |
Molecular Function | transmembrane receptor protein tyrosine kinase activity | |
Biological Process | chorion-containing eggshell pattern formation | |
Biological Process | gastrulation | |
Biological Process | germ cell migration | |
Biological Process | metamorphosis | |
Biological Process | negative phototaxis | |
Biological Process | negative regulation of hippo signaling | |
Biological Process | negative regulation of multicellular organism growth | |
Biological Process | pole cell fate determination | |
Biological Process | positive regulation of MAPK cascade | |
Biological Process | positive regulation of Ras protein signal transduction | |
Biological Process | terminal region determination | |
Biological Process | torso signaling pathway |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosine-protein kinase receptor torso
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP18475
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 21-399 | Extracellular | ||||
Sequence: GEMLLMDKISHDKTLLNVTACTQNCLEKGQMDFRSCLKDCRINGTFPGALRKVQENYQMNMICRTESEIVFQIDWVQHSRGTEPAPNATYIIRVDAVKDDNKETALYLSDDNFLILPGLESNSTHNITALAMHGDGSYSLIAKDQTFATLIRGYQPSKMGAVNLLRFVPQPDDLHHIAAEIEWKPSAESNCYFDMVSYSTNSVNMDEPLEVQFRDRKKLYRHTVDNLEFDKQYHVGVRTVNIMNRLESDLQWLPIAVPSCLDWYPYNYTLCPPHKPENLTVTQKQYLPNILALNITWARPRYLPDNYTLHIFDLFKGGTELNYTLDQNRSHFYVPKITVLGSHFEVHLVAQSAGGKNVSGLTLDKVHRGVLLSEGNMVK | ||||||
Transmembrane | 400-420 | Helical | ||||
Sequence: LVLFIIVPICCILMLCSLTFC | ||||||
Topological domain | 421-923 | Cytoplasmic | ||||
Sequence: RRNRSEVQALQMDAKDAKASEFHLSLMDSSGLLVTLSANESLEVMDELEVEPHSVLLQDVLGEGAFGLVRRGVYKKRQVAVKLLKDEPNDEDVYAFKCEIQMLKAVGKHPNIVGIVGYSTRFSNQMMLLIEYCSLGSLQNFLREEWKFRQEQNAIGLKKNLEQNVDNRRFNRLPRNSIHDRIEDINNSMLSTVEEESESDQTHSSRCETYTLTRITNAADNKGYGLEDIENIGGSYIPKTAEAPKDRPKRKLKPQPKKDSKQDFKSDNKKRIFENKEYFDCLDSSDTKPRIPLKYADLLDIAQQVAVGMEFLAQNKVVHRDLAARNVLISVDRSIKIADFGLSRDVYHENVYRKSGGSGKLPIKWLALESLTHQVYTSQSDVWSFGVLLYEITTLGGMPYPSVSPSDLLQLLRQGHRMKRPEGCTQEMFSLMESCWSSVPSHRPTFSALKHRLGGMILATNDVPERLKQLQAATESKLKSCDGLNSKVEQVPCEEELYLEPLN |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
RNAi-mediated knockdown in the prothoracic gland (PG) delays the onset of pupariation by prolonging the L3 larval stage. In addition, pupal size and, to a lesser extent, PG cell size are increased.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MLIFYAKYAFIFWFFVGSNQ | ||||||
Chain | PRO_0000024477 | 21-923 | Tyrosine-protein kinase receptor torso | |||
Sequence: GEMLLMDKISHDKTLLNVTACTQNCLEKGQMDFRSCLKDCRINGTFPGALRKVQENYQMNMICRTESEIVFQIDWVQHSRGTEPAPNATYIIRVDAVKDDNKETALYLSDDNFLILPGLESNSTHNITALAMHGDGSYSLIAKDQTFATLIRGYQPSKMGAVNLLRFVPQPDDLHHIAAEIEWKPSAESNCYFDMVSYSTNSVNMDEPLEVQFRDRKKLYRHTVDNLEFDKQYHVGVRTVNIMNRLESDLQWLPIAVPSCLDWYPYNYTLCPPHKPENLTVTQKQYLPNILALNITWARPRYLPDNYTLHIFDLFKGGTELNYTLDQNRSHFYVPKITVLGSHFEVHLVAQSAGGKNVSGLTLDKVHRGVLLSEGNMVKLVLFIIVPICCILMLCSLTFCRRNRSEVQALQMDAKDAKASEFHLSLMDSSGLLVTLSANESLEVMDELEVEPHSVLLQDVLGEGAFGLVRRGVYKKRQVAVKLLKDEPNDEDVYAFKCEIQMLKAVGKHPNIVGIVGYSTRFSNQMMLLIEYCSLGSLQNFLREEWKFRQEQNAIGLKKNLEQNVDNRRFNRLPRNSIHDRIEDINNSMLSTVEEESESDQTHSSRCETYTLTRITNAADNKGYGLEDIENIGGSYIPKTAEAPKDRPKRKLKPQPKKDSKQDFKSDNKKRIFENKEYFDCLDSSDTKPRIPLKYADLLDIAQQVAVGMEFLAQNKVVHRDLAARNVLISVDRSIKIADFGLSRDVYHENVYRKSGGSGKLPIKWLALESLTHQVYTSQSDVWSFGVLLYEITTLGGMPYPSVSPSDLLQLLRQGHRMKRPEGCTQEMFSLMESCWSSVPSHRPTFSALKHRLGGMILATNDVPERLKQLQAATESKLKSCDGLNSKVEQVPCEEELYLEPLN | ||||||
Glycosylation | 37 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 63 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 107 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 142 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 146 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 287 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 298 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 314 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 326 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 342 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 348 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 377 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 608 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
May be auto-phosphorylated on tyrosine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 475-874 | Protein kinase | ||||
Sequence: VLLQDVLGEGAFGLVRRGVYKKRQVAVKLLKDEPNDEDVYAFKCEIQMLKAVGKHPNIVGIVGYSTRFSNQMMLLIEYCSLGSLQNFLREEWKFRQEQNAIGLKKNLEQNVDNRRFNRLPRNSIHDRIEDINNSMLSTVEEESESDQTHSSRCETYTLTRITNAADNKGYGLEDIENIGGSYIPKTAEAPKDRPKRKLKPQPKKDSKQDFKSDNKKRIFENKEYFDCLDSSDTKPRIPLKYADLLDIAQQVAVGMEFLAQNKVVHRDLAARNVLISVDRSIKIADFGLSRDVYHENVYRKSGGSGKLPIKWLALESLTHQVYTSQSDVWSFGVLLYEITTLGGMPYPSVSPSDLLQLLRQGHRMKRPEGCTQEMFSLMESCWSSVPSHRPTFSALKHRLG | ||||||
Region | 656-687 | Disordered | ||||
Sequence: YIPKTAEAPKDRPKRKLKPQPKKDSKQDFKSD |
Sequence similarities
Belongs to the protein kinase superfamily. Tyr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P18475-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NameA
- Length923
- Mass (Da)105,201
- Last updated2005-08-30 v2
- Checksum746F46E1A4277ACF
P18475-3
- NameD
- Differences from canonical
- 389-393: Missing
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 125 | in Ref. 1; CAA33247 | ||||
Sequence: A → T | ||||||
Sequence conflict | 387 | in Ref. 1; CAA33247 | ||||
Sequence: H → P | ||||||
Alternative sequence | VSP_058212 | 389-393 | in isoform D | |||
Sequence: Missing | ||||||
Sequence conflict | 667 | in Ref. 1; CAA33247 | ||||
Sequence: R → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15150 EMBL· GenBank· DDBJ | CAA33247.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF59203.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | ABV53713.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | ABV53714.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY071403 EMBL· GenBank· DDBJ | AAL49025.1 EMBL· GenBank· DDBJ | mRNA |