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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).

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