P48994 · TRPL_DROME

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcation channel complex
Cellular Componentdendrite
Cellular ComponentinaD signaling complex
Cellular Componentmembrane
Cellular Componentplasma membrane
Cellular Componentrhabdomere
Cellular Componentrhabdomere microvillus membrane
Molecular Functioncalcium channel activity
Molecular Functioncalmodulin binding
Molecular Functionidentical protein binding
Molecular Functioninositol 1,4,5 trisphosphate binding
Molecular Functionmonoatomic cation channel activity
Molecular Functionmonoatomic ion transmembrane transporter activity
Molecular Functionprotein heterodimerization activity
Molecular Functionstore-operated calcium channel activity
Biological Processbody fluid secretion
Biological Processcalcium ion transmembrane transport
Biological Processcalcium ion transport
Biological Processcalcium-mediated signaling
Biological Processcellular response to anoxia
Biological Processdetection of light stimulus involved in visual perception
Biological Processmonoatomic cation transport
Biological Processmonoatomic ion transport
Biological Processphototransduction, visible light
Biological Processregulation of cytosolic calcium ion concentration
Biological Processresponse to light stimulus
Biological Processsensory perception of sound

Keywords

Protein family/group databases

    • 1.A.4.1.8the transient receptor potential ca2+/cation channel (trp-cc) family

Names & Taxonomy

Protein names

  • Recommended name
    Transient-receptor-potential-like protein

Gene names

    • Name
      trpl
    • ORF names
      CG18345

Organism names

  • Taxonomic identifier
  • Strains
    • Oregon-R
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    P48994
  • Secondary accessions
    • C6TPC1
    • Q0E9E3
    • Q8IH62
    • Q8MKU9
    • Q9V5B2

Proteomes

Organism-specific databases

Subcellular Location

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.

TypeIDPosition(s)Description
Topological domain1-340Cytoplasmic
Transmembrane341-361Helical
Topological domain362-373Extracellular
Transmembrane374-394Helical
Topological domain395-431Cytoplasmic
Transmembrane432-452Helical
Topological domain453-512Extracellular
Transmembrane513-533Helical
Topological domain534-548Cytoplasmic
Transmembrane549-569Helical
Topological domain570-645Extracellular
Transmembrane646-666Helical
Topological domain667-1124Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis702Abolishes interaction with Fkbp59.
Mutagenesis709Abolishes interaction with Fkbp59.
Mutagenesis713Disrupts Ca2+ inflow through the channel. Calmodulin has little effect on Ca2+ flow.
Mutagenesis814Does not abolish Ca2+ inflow through the channel. Calmodulin has no effect on initial rates.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002153591-1124Transient-receptor-potential-like protein

Proteomic databases

Expression

Tissue specificity

Expressed predominantly in the rhabdomeres of photoreceptor cells.

Gene expression databases

Interaction

Subunit

Forms heteromultimers with Trpgamma and, to a lower extent, with trp. Interacts with Fkbp59 in vivo and is found in the inaD signaling complex.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, repeat, compositional bias.

TypeIDPosition(s)Description
Region1-24Disordered
Repeat40-69ANK 1
Repeat78-107ANK 2
Repeat152-181ANK 3
Region710-728Calmodulin-binding 1
Region853-895Calmodulin-binding 2
Region978-1013Disordered
Compositional bias980-994Polar residues
Region1031-1124Disordered
Compositional bias1052-1072Polar residues
Compositional bias1088-1103Basic and acidic residues

Domain

Binding of calmodulin to binding site 1 is Ca2+ dependent, whereas binding of calmodulin to site 2 is Ca2+ independent.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,124
  • Mass (Da)
    127,750
  • Last updated
    2002-11-25 v2
  • Checksum
    AF6323BA27626583
MGRKKKLPTGVSSGVSHASSAPKSVGGCCVPLGLPQPLLLEEKKFLLAVERGDMPNVRRILQKALRHQHININCMDPLGRRALTLAIDNENLEMVELLVVMGVETKDALLHAINAEFVEAVELLLEHEELIYKEGEPYSWQKVDINTAMFAPDITPLMLAAHKNNFEILRILLDRGAAVPVPHDIRCGCEECVRLTAEDSLRHSLSRVNIYRALCSPSLICLTSNDPIITAFQLSWELRNLALTEQECKSEYMDLRRQCQKFAVDLLDQTRTSNELAIILNYDPQMSSYEPGDRMSLTRLVQAISYKQKKFVAHSNIQQLLSSIWYDGLPGFRRKSIVDKVICIAQVAVLFPLYCLIYMCAPNCRTGQLMRKPFMKFLIHASSYLFFLFILILVSQRADDDFVRIFGTTRMKKELAEQELRQRGQTPSKLELIVVMYVIGFVWEEVQEIFAVGMKSYLRNMWNFIDFLRNSLYVSVMCLRAFAYIQQATEIARDPQMAYIPREKWHDFDPQLIAEGLFAAANVFSALKLVHLFSINPHLGPLQISLGRMVIDIVKFFFIYTLVLFAFACGLNQLLWYFAALEKSKCYVLPGGEADWGSHGDSCMKWRRFGNLFESSQSLFWASFGMVGLDDFELSGIKSYTRFWGLLMFGSYSVINVIVLLNLLIAMMSNSYAMIDEHSDTEWKFARTKLWMSYFEDSATLPPPFNVLPSVKWVIRIFRKSSKTIDRQRSKKRKEQEQFSEYDNIMRSLVWRYVAAMHRKFENNPVSEDDINEVKSEINTMRYEMLEIFENSGMDVSSANKKERQPRPRRIKVWERRLMKGFQVAPVQNGCELDAFGNVNGQGEMQEIKVESIPSKPAKETAKERFQRVARTVLLQSTTHKWNVVLRAAKDSQIGRCTKNERKSLQNLGRAIEEAKRLIMLNPGCPSGRESPIRIEFEDEKTSTLLELLNQISAEISDSEKPKIRPIWRPPLKTVPARAMAANNTRSLTAPELKISRKSSPAPTPTPTPGVSHTALSQFRNRELPLCPSKLIANSAPSAPTAPPKKSAPTAPTPTYKPTTHAPFSVEGGNRENTRASDGVRSDNSNFDIHVVDLDEKGGHLGRDNVSDISSIASTSPQRPKHRN

Sequence caution

The sequence AAN71152.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict228-229in Ref. 1; AAA28979
Compositional bias980-994Polar residues
Compositional bias1052-1072Polar residues
Compositional bias1088-1103Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp