P48994 · TRPL_DROME
- ProteinTransient-receptor-potential-like protein
- Genetrpl
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1124 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
A light-sensitive calcium channel that is required for inositide-mediated Ca2+ entry in the retina during phospholipase C (PLC)-mediated phototransduction. Required for vision in the dark and in dim light. Binds calmodulin. Trp and trpl act together in the light response, although it is unclear whether as heteromultimers or distinct units. Also forms a functional cation channel with Trpgamma. Activated by fatty acids, metabolic stress, inositols and GTP-binding proteins.
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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Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTransient-receptor-potential-like protein
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionP48994
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Cell projection, rhabdomere membrane ; Multi-pass membrane protein
Note: In the dark, there is 20 fold more rhabdomeral trpl protein forming plasma membrane channels than in the light. In the light, the protein translocates to an intracellular compartment. Protein levels remain unchanged in light and dark conditions.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-340 | Cytoplasmic | ||||
Sequence: MGRKKKLPTGVSSGVSHASSAPKSVGGCCVPLGLPQPLLLEEKKFLLAVERGDMPNVRRILQKALRHQHININCMDPLGRRALTLAIDNENLEMVELLVVMGVETKDALLHAINAEFVEAVELLLEHEELIYKEGEPYSWQKVDINTAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVPHDIRCGCEECVRLTAEDSLRHSLSRVNIYRALCSPSLICLTSNDPIITAFQLSWELRNLALTEQECKSEYMDLRRQCQKFAVDLLDQTRTSNELAIILNYDPQMSSYEPGDRMSLTRLVQAISYKQKKFVAHSNIQQLLSSIWYDGLPGFRRKSIVDK | ||||||
Transmembrane | 341-361 | Helical | ||||
Sequence: VICIAQVAVLFPLYCLIYMCA | ||||||
Topological domain | 362-373 | Extracellular | ||||
Sequence: PNCRTGQLMRKP | ||||||
Transmembrane | 374-394 | Helical | ||||
Sequence: FMKFLIHASSYLFFLFILILV | ||||||
Topological domain | 395-431 | Cytoplasmic | ||||
Sequence: SQRADDDFVRIFGTTRMKKELAEQELRQRGQTPSKLE | ||||||
Transmembrane | 432-452 | Helical | ||||
Sequence: LIVVMYVIGFVWEEVQEIFAV | ||||||
Topological domain | 453-512 | Extracellular | ||||
Sequence: GMKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYIQQATEIARDPQMAYIPREKWHDFDPQL | ||||||
Transmembrane | 513-533 | Helical | ||||
Sequence: IAEGLFAAANVFSALKLVHLF | ||||||
Topological domain | 534-548 | Cytoplasmic | ||||
Sequence: SINPHLGPLQISLGR | ||||||
Transmembrane | 549-569 | Helical | ||||
Sequence: MVIDIVKFFFIYTLVLFAFAC | ||||||
Topological domain | 570-645 | Extracellular | ||||
Sequence: GLNQLLWYFAALEKSKCYVLPGGEADWGSHGDSCMKWRRFGNLFESSQSLFWASFGMVGLDDFELSGIKSYTRFWG | ||||||
Transmembrane | 646-666 | Helical | ||||
Sequence: LLMFGSYSVINVIVLLNLLIA | ||||||
Topological domain | 667-1124 | Cytoplasmic | ||||
Sequence: MMSNSYAMIDEHSDTEWKFARTKLWMSYFEDSATLPPPFNVLPSVKWVIRIFRKSSKTIDRQRSKKRKEQEQFSEYDNIMRSLVWRYVAAMHRKFENNPVSEDDINEVKSEINTMRYEMLEIFENSGMDVSSANKKERQPRPRRIKVWERRLMKGFQVAPVQNGCELDAFGNVNGQGEMQEIKVESIPSKPAKETAKERFQRVARTVLLQSTTHKWNVVLRAAKDSQIGRCTKNERKSLQNLGRAIEEAKRLIMLNPGCPSGRESPIRIEFEDEKTSTLLELLNQISAEISDSEKPKIRPIWRPPLKTVPARAMAANNTRSLTAPELKISRKSSPAPTPTPTPGVSHTALSQFRNRELPLCPSKLIANSAPSAPTAPPKKSAPTAPTPTYKPTTHAPFSVEGGNRENTRASDGVRSDNSNFDIHVVDLDEKGGHLGRDNVSDISSIASTSPQRPKHRN |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 702 | Abolishes interaction with Fkbp59. | ||||
Sequence: P → Q | ||||||
Mutagenesis | 709 | Abolishes interaction with Fkbp59. | ||||
Sequence: P → Q | ||||||
Mutagenesis | 713 | Disrupts Ca2+ inflow through the channel. Calmodulin has little effect on Ca2+ flow. | ||||
Sequence: W → G | ||||||
Mutagenesis | 814 | Does not abolish Ca2+ inflow through the channel. Calmodulin has no effect on initial rates. | ||||
Sequence: W → G |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215359 | 1-1124 | Transient-receptor-potential-like protein | |||
Sequence: MGRKKKLPTGVSSGVSHASSAPKSVGGCCVPLGLPQPLLLEEKKFLLAVERGDMPNVRRILQKALRHQHININCMDPLGRRALTLAIDNENLEMVELLVVMGVETKDALLHAINAEFVEAVELLLEHEELIYKEGEPYSWQKVDINTAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVPHDIRCGCEECVRLTAEDSLRHSLSRVNIYRALCSPSLICLTSNDPIITAFQLSWELRNLALTEQECKSEYMDLRRQCQKFAVDLLDQTRTSNELAIILNYDPQMSSYEPGDRMSLTRLVQAISYKQKKFVAHSNIQQLLSSIWYDGLPGFRRKSIVDKVICIAQVAVLFPLYCLIYMCAPNCRTGQLMRKPFMKFLIHASSYLFFLFILILVSQRADDDFVRIFGTTRMKKELAEQELRQRGQTPSKLELIVVMYVIGFVWEEVQEIFAVGMKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYIQQATEIARDPQMAYIPREKWHDFDPQLIAEGLFAAANVFSALKLVHLFSINPHLGPLQISLGRMVIDIVKFFFIYTLVLFAFACGLNQLLWYFAALEKSKCYVLPGGEADWGSHGDSCMKWRRFGNLFESSQSLFWASFGMVGLDDFELSGIKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFARTKLWMSYFEDSATLPPPFNVLPSVKWVIRIFRKSSKTIDRQRSKKRKEQEQFSEYDNIMRSLVWRYVAAMHRKFENNPVSEDDINEVKSEINTMRYEMLEIFENSGMDVSSANKKERQPRPRRIKVWERRLMKGFQVAPVQNGCELDAFGNVNGQGEMQEIKVESIPSKPAKETAKERFQRVARTVLLQSTTHKWNVVLRAAKDSQIGRCTKNERKSLQNLGRAIEEAKRLIMLNPGCPSGRESPIRIEFEDEKTSTLLELLNQISAEISDSEKPKIRPIWRPPLKTVPARAMAANNTRSLTAPELKISRKSSPAPTPTPTPGVSHTALSQFRNRELPLCPSKLIANSAPSAPTAPPKKSAPTAPTPTYKPTTHAPFSVEGGNRENTRASDGVRSDNSNFDIHVVDLDEKGGHLGRDNVSDISSIASTSPQRPKHRN |
Proteomic databases
Expression
Tissue specificity
Expressed predominantly in the rhabdomeres of photoreceptor cells.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MGRKKKLPTGVSSGVSHASSAPKS | ||||||
Repeat | 40-69 | ANK 1 | ||||
Sequence: LEEKKFLLAVERGDMPNVRRILQKALRHQH | ||||||
Repeat | 78-107 | ANK 2 | ||||
Sequence: LGRRALTLAIDNENLEMVELLVVMGVETKD | ||||||
Repeat | 152-181 | ANK 3 | ||||
Sequence: PDITPLMLAAHKNNFEILRILLDRGAAVPV | ||||||
Region | 710-728 | Calmodulin-binding 1 | ||||
Sequence: SVKWVIRIFRKSSKTIDRQ | ||||||
Region | 853-895 | Calmodulin-binding 2 | ||||
Sequence: IPSKPAKETAKERFQRVARTVLLQSTTHKWNVVLRAAKDSQIG | ||||||
Region | 978-1013 | Disordered | ||||
Sequence: RAMAANNTRSLTAPELKISRKSSPAPTPTPTPGVSH | ||||||
Compositional bias | 980-994 | Polar residues | ||||
Sequence: MAANNTRSLTAPELK | ||||||
Region | 1031-1124 | Disordered | ||||
Sequence: LIANSAPSAPTAPPKKSAPTAPTPTYKPTTHAPFSVEGGNRENTRASDGVRSDNSNFDIHVVDLDEKGGHLGRDNVSDISSIASTSPQRPKHRN | ||||||
Compositional bias | 1052-1072 | Polar residues | ||||
Sequence: PTPTYKPTTHAPFSVEGGNRE | ||||||
Compositional bias | 1088-1103 | Basic and acidic residues | ||||
Sequence: DIHVVDLDEKGGHLGR |
Domain
Binding of calmodulin to binding site 1 is Ca2+ dependent, whereas binding of calmodulin to site 2 is Ca2+ independent.
Sequence similarities
Belongs to the transient receptor (TC 1.A.4) family. STrpC subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,124
- Mass (Da)127,750
- Last updated2002-11-25 v2
- ChecksumAF6323BA27626583
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 228-229 | in Ref. 1; AAA28979 | ||||
Sequence: II → SS | ||||||
Compositional bias | 980-994 | Polar residues | ||||
Sequence: MAANNTRSLTAPELK | ||||||
Compositional bias | 1052-1072 | Polar residues | ||||
Sequence: PTPTYKPTTHAPFSVEGGNRE | ||||||
Compositional bias | 1088-1103 | Basic and acidic residues | ||||
Sequence: DIHVVDLDEKGGHLGR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M88185 EMBL· GenBank· DDBJ | AAA28979.1 EMBL· GenBank· DDBJ | mRNA | ||
AE013599 EMBL· GenBank· DDBJ | AAF58904.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAM68793.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE013599 EMBL· GenBank· DDBJ | AAM68794.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT001397 EMBL· GenBank· DDBJ | AAN71152.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BT099607 EMBL· GenBank· DDBJ | ACU45760.1 EMBL· GenBank· DDBJ | mRNA |