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1.A.4.1.8
TrpL (Trp-like), isoform A (1124 aas). A light-sensitive calcium channel that is required for inositide-mediated Ca2+ entry in the retina during phospholipase C (PLC)-mediated phototransduction (Lan et al. 1998; Chyb et al. 1999). It is required for vision in the dark and in dim light. and binds calmodulin. Trp and TrpL act together in the light response (Bähner et al. 2002). TrpL assembles in vivo as a homo-multimeric channe, not as a hetero-meric channels as reported previously (Katz et al. 2013).

Accession Number:P48994
Protein Name:Transient-receptor-potential-like protein
Length:1124
Molecular Weight:127750.00
Species:Drosophila melanogaster (Fruit fly) [7227]
Number of TMSs:9
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate Ca2+

Cross database links:

eggNOG: inNOG07559
Entrez Gene ID: 36003   
Pfam: PF00023    PF00520    PF08344   
KEGG: dme:Dmel_CG1834   

Gene Ontology

GO:0016027 C:inaD signaling complex
GO:0016021 C:integral to membrane
GO:0005622 C:intracellular
GO:0005516 F:calmodulin binding
GO:0046982 F:protein heterodimerization activity
GO:0015279 F:store-operated calcium channel activity
GO:0007589 P:body fluid secretion
GO:0019722 P:calcium-mediated signaling
GO:0071454 P:cellular response to anoxia
GO:0050908 P:detection of light stimulus involved in visual perception

References (15)

[1] “Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene.”  Phillips A.M.et.al.   1314616
[2] “The genome sequence of Drosophila melanogaster.”  Adams M.D.et.al.   10731132
[3] “Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.”  Misra S.et.al.   12537572
[4] “A Drosophila full-length cDNA resource.”  Stapleton M.et.al.   12537569
[5] “Identification and characterization of two distinct calmodulin-binding sites in the Trpl ion-channel protein of Drosophila melanogaster.”  Warr C.G.et.al.   8670063
[6] “Coassembly of TRP and TRPL produces a distinct store-operated conductance.”  Xu X.-Z.S.et.al.   9215637
[7] “The role of calmodulin-binding sites in the regulation of the Drosophila TRPL cation channel expressed in Xenopus laevis oocytes by ca2+, inositol 1,4,5-trisphosphate and GTP-binding proteins.”  Lan L.et.al.   9494079
[8] “Ca2+-dependent interaction of the trpl cation channel and calmodulin.”  Trost C.et.al.   10371201
[9] “Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL.”  Chyb S.et.al.   9930700
[10] “Metabolic stress reversibly activates the Drosophila light-sensitive channels TRP and TRPL in vivo.”  Agam K.et.al.   10908615
[11] “Direct activation of trpl cation channels by G alpha11 subunits.”  Obukhov A.G.et.al.   8918461
[12] “TRPgamma, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL.”  Xu X.-Z.S.et.al.   10896160
[13] “Regulation of Drosophila TRPL channels by immunophilin FKBP59.”  Goel M.et.al.   11514552
[14] “Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current.”  Baehner M.et.al.   11931743
[15] “Phototransduction in Drosophila melanogaster.”  Hardie R.C.et.al.   11707492

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FASTA formatted sequence
1:	MGRKKKLPTG VSSGVSHASS APKSVGGCCV PLGLPQPLLL EEKKFLLAVE RGDMPNVRRI 
61:	LQKALRHQHI NINCMDPLGR RALTLAIDNE NLEMVELLVV MGVETKDALL HAINAEFVEA 
121:	VELLLEHEEL IYKEGEPYSW QKVDINTAMF APDITPLMLA AHKNNFEILR ILLDRGAAVP 
181:	VPHDIRCGCE ECVRLTAEDS LRHSLSRVNI YRALCSPSLI CLTSNDPIIT AFQLSWELRN 
241:	LALTEQECKS EYMDLRRQCQ KFAVDLLDQT RTSNELAIIL NYDPQMSSYE PGDRMSLTRL 
301:	VQAISYKQKK FVAHSNIQQL LSSIWYDGLP GFRRKSIVDK VICIAQVAVL FPLYCLIYMC 
361:	APNCRTGQLM RKPFMKFLIH ASSYLFFLFI LILVSQRADD DFVRIFGTTR MKKELAEQEL 
421:	RQRGQTPSKL ELIVVMYVIG FVWEEVQEIF AVGMKSYLRN MWNFIDFLRN SLYVSVMCLR 
481:	AFAYIQQATE IARDPQMAYI PREKWHDFDP QLIAEGLFAA ANVFSALKLV HLFSINPHLG 
541:	PLQISLGRMV IDIVKFFFIY TLVLFAFACG LNQLLWYFAA LEKSKCYVLP GGEADWGSHG 
601:	DSCMKWRRFG NLFESSQSLF WASFGMVGLD DFELSGIKSY TRFWGLLMFG SYSVINVIVL 
661:	LNLLIAMMSN SYAMIDEHSD TEWKFARTKL WMSYFEDSAT LPPPFNVLPS VKWVIRIFRK 
721:	SSKTIDRQRS KKRKEQEQFS EYDNIMRSLV WRYVAAMHRK FENNPVSEDD INEVKSEINT 
781:	MRYEMLEIFE NSGMDVSSAN KKERQPRPRR IKVWERRLMK GFQVAPVQNG CELDAFGNVN 
841:	GQGEMQEIKV ESIPSKPAKE TAKERFQRVA RTVLLQSTTH KWNVVLRAAK DSQIGRCTKN 
901:	ERKSLQNLGR AIEEAKRLIM LNPGCPSGRE SPIRIEFEDE KTSTLLELLN QISAEISDSE 
961:	KPKIRPIWRP PLKTVPARAM AANNTRSLTA PELKISRKSS PAPTPTPTPG VSHTALSQFR 
1021:	NRELPLCPSK LIANSAPSAP TAPPKKSAPT APTPTYKPTT HAPFSVEGGN RENTRASDGV 
1081:	RSDNSNFDIH VVDLDEKGGH LGRDNVSDIS SIASTSPQRP KHRN