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1.A.4.1.1
Transient receptor potential (TRP) protein.  Assembles in vivo as a homomultimeric channel, not as a heteromeric channel with TrpL as the subunit (Katz et al. 2013).  It is a light-sensitive calcium channel that is required for inositide-mediated Ca2+ entry in the retina during phospholipase C (PLC)-mediated phototransduction. Ca2+ influx may then feed back and inhibit PLC, thereby facilitating phosphatidylinositol 4,5 bisphosphate (PIP2) recycling. Trp and trpl act together in the light response, though it is unclear whether as heteromultimers or as distinct units, and are activated by fatty acids and metabolic stress. It is also required for olfactory adaptation and may be involved in olfactory system development (Störtkuhl et al. 1999). Mechanical force activates the light-dependent channels TRP and TRPL in excised patches from the rhabdomere of Drosophila photoreceptors (Delgado et al. 2024).

Accession Number:P19334
Protein Name:TRP
Length:1275
Molecular Weight:142594.00
Species:Drosophila melanogaster (Fruit fly) [7227]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate calcium(2+)

Cross database links:

RefSeq: NP_476768.1   
Entrez Gene ID: 43542   
Pfam: PF00023    PF00520    PF08344   
KEGG: dme:Dmel_CG7875   

Gene Ontology

GO:0016027 C:inaD signaling complex
GO:0016021 C:integral to membrane
GO:0005516 F:calmodulin binding
GO:0005218 F:intracellular ligand-gated calcium channel ...
GO:0046982 F:protein heterodimerization activity
GO:0042803 F:protein homodimerization activity
GO:0015279 F:store-operated calcium channel activity
GO:0006816 P:calcium ion transport
GO:0019722 P:calcium-mediated signaling
GO:0030845 P:inhibition of phospholipase C activity invo...
GO:0008377 P:light-induced release of internally sequest...
GO:0008355 P:olfactory learning
GO:0008104 P:protein localization
GO:0007608 P:sensory perception of smell
GO:0055085 P:transmembrane transport

References (17)

[1] “Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction.”  Montell C.et.al.   2516726
[2] “Proper function of the Drosophila trp gene product during pupal development is important for normal visual transduction in the adult.”  Wong F.et.al.   2482778
[3] “The genome sequence of Drosophila melanogaster.”  Adams M.D.et.al.   10731132
[4] “Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.”  Misra S.et.al.   12537572
[5] “Overlapping transcription units in the transient receptor potential locus of Drosophila melanogaster.”  Wong F.et.al.   3118483
[6] “TRP, a protein essential for inositide-mediated Ca2+ influx is localized adjacent to the calcium stores in Drosophila photoreceptors.”  Pollock J.A.et.al.   7751943
[7] “Coassembly of TRP and TRPL produces a distinct store-operated conductance.”  Xu X.-Z.S.et.al.   9215637
[8] “Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex.”  Chevesich J.et.al.   9010208
[9] “Olfactory adaptation depends on the Trp Ca2+ channel in Drosophila.”  Stortkuhl K.F.et.al.   10366618
[10] “Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL.”  Chyb S.et.al.   9930700
[11] “Reversible phosphorylation of the signal transduction complex in Drosophila photoreceptors.”  Liu M.et.al.   10766855
[12] “TRP and the PDZ protein, INAD, form the core complex required for retention of the signalplex in Drosophila photoreceptor cells.”  Li H.-S.et.al.   10995445
[13] “Novel mechanism of massive photoreceptor degeneration caused by mutations in the trp gene of Drosophila.”  Yoon J.et.al.   10632594
[14] “Metabolic stress reversibly activates the Drosophila light-sensitive channels TRP and TRPL in vivo.”  Agam K.et.al.   10908615
[15] “TRPgamma, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL.”  Xu X.-Z.S.et.al.   10896160
[16] “Single amino acid change in the fifth transmembrane segment of the TRP Ca2+ channel causes massive degeneration of photoreceptors.”  Hong Y.S.et.al.   12107168
[17] “Phototransduction in Drosophila melanogaster.”  Hardie R.C.et.al.   11707492
Structure:
5F67     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MGSNTESDAE KALGSRLDYD LMMAEEYILS DVEKNFILSC ERGDLPGVKK ILEEYQGTDK 
61:	FNINCTDPMN RSALISAIEN ENFDLMVILL EHNIEVGDAL LHAISEEYVE AVEELLQWEE 
121:	TNHKEGQPYS WEAVDRSKST FTVDITPLIL AAHRNNYEIL KILLDRGATL PMPHDVKCGC 
181:	DECVTSQMTD SLRHSQSRIN AYRALSASSL IALSSRDPVL TAFQLSWELK RLQAMESEFR 
241:	AEYTEMRQMV QDFGTSLLDH ARTSMELEVM LNFNHEPSHD IWCLGQRQTL ERLKLAIRYK 
301:	QKTFVAHPNV QQLLAAIWYD GLPGFRRKQA SQQLMDVVKL GCSFPIYSLK YILAPDSEGA 
361:	KFMRKPFVKF ITHSCSYMFF LMLLGAASLR VVQITFELLA FPWMLTMLED WRKHERGSLP 
421:	GPIELAIITY IMALIFEELK SLYSDGLFEY IMDLWNIVDY ISNMFYVTWI LCRATAWVIV 
481:	HRDLWFRGID PYFPREHWHP FDPMLLSEGA FAAGMVFSYL KLVHIFSINP HLGPLQVSLG 
541:	RMIIDIIKFF FIYTLVLFAF GCGLNQLLWY YAELEKNKCY HLHPDVADFD DQEKACTIWR 
601:	RFSNLFETSQ SLFWASFGLV DLVSFDLAGI KSFTRFWALL MFGSYSVINI IVLLNMLIAM 
661:	MSNSYQIISE RADTEWKFAR SQLWMSYFED GGTIPPPFNL CPNMKMLRKT LGRKRPSRTK 
721:	SFMRKSMERA QTLHDKVMKL LVRRYITAEQ RRRDDYGITE DDIIEVRQDI SSLRFELLEI 
781:	FTNNNWDVPD IEKKSQGVAR TTKGKVMERR ILKDFQIGFV ENLKQEMSES ESGRDIFSSL 
841:	AKVIGRKKTQ KGDKDWNAIA RKNTFASDPI GSKRSSMQRH SQRSLRRKII EQANEGLQMN 
901:	QTQLIEFNPN LGDVTRATRV AYVKFMRKKM AADEVSLADD EGAPNGEGEK KPLDASGSKK 
961:	SITSGGTGGG ASMLAAAALR ASVKNVDEKS GADGKPGTMG KPTDDKKAGD DKDKQQPPKD 
1021:	SKPSAGGPKP GDQKPTPGAG APKPQAAGTI SKPGESQKKD APAPPTKPGD TKPAAPKPGE 
1081:	SAKPEAAAKK EESSKTEASK PAATNGAAKS AAPSAPSDAK PDSKLKPGAA GAPEATKATN 
1141:	GASKPDEKKS GPEEPKKAAG DSKPGDDAKD KDKKPGDDKD KKPGDDKDKK PADNNDKKPA 
1201:	DDKDKKPGDD KDKKPGDDKD KKPSDDKDKK PADDKDKKPA AAPLKPAIKV GQSSAAAGGE 
1261:	RGKSTVTGRM ISGWL