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1.A.4.1.8
TrpL (Trp-like), isoform A (1124 aas).  Assembles in vivo as homomultimeric channes, not as heteromeric channels with Trp as had been reported (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

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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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