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UniProtKB/Swiss-Prot entry P48994


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TRPL_DROME
Primary accession number P48994
Secondary accession numbers Q0E9E3 Q8IH62 Q8MKU9 Q9V5B2
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on November 25, 2002 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 78)
Name and origin of the protein
Protein name Transient-receptor-potential-like protein
Synonyms None
Gene name
Name: trpl
ORFNames: CG18345
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), CALMODULIN-BINDING, AND TISSUE SPECIFICITY.
STRAIN=Oregon-R;
DOI=10.1016/0896-6273(92)90085-R; PubMed=1314616 [NCBI, ExPASy, EBI, Israel, Japan]
Phillips A.M., Bull A.L., Kelly L.E.;
"Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene.";
Neuron 8:631-642(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
CALMODULIN-BINDING.
PubMed=8670063 [NCBI, ExPASy, EBI, Israel, Japan]
Warr C.G., Kelly L.E.;
"Identification and characterization of two distinct calmodulin-binding sites in the Trpl ion-channel protein of Drosophila melanogaster.";
Biochem. J. 314:497-503(1996).
[6]
INTERACTION WITH TRP.
DOI=10.1016/S0092-8674(00)80302-5; PubMed=9215637 [NCBI, ExPASy, EBI, Israel, Japan]
Xu X.-Z.S., Li H.-S., Guggino W.B., Montell C.;
"Coassembly of TRP and TRPL produces a distinct store-operated conductance.";
Cell 89:1155-1164(1997).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-713 AND TRP-814.
PubMed=9494079 [NCBI, ExPASy, EBI, Israel, Japan]
Lan L., Brereton H., Barritt G.J.;
"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.";
Biochem. J. 330:1149-1158(1998).
[8]
CALMODULIN-BINDING.
DOI=10.1016/S0014-5793(99)00588-8; PubMed=10371201 [NCBI, ExPASy, EBI, Israel, Japan]
Trost C., Marquart A., Zimmer S., Philipp S., Cavalie A., Flockerzi V.;
"Ca2+-dependent interaction of the trpl cation channel and calmodulin.";
FEBS Lett. 451:257-263(1999).
[9]
FUNCTION.
DOI=10.1038/16703; PubMed=9930700 [NCBI, ExPASy, EBI, Israel, Japan]
Chyb S., Raghu P., Hardie R.C.;
"Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL.";
Nature 397:255-259(1999).
[10]
FUNCTION.
PubMed=10908615 [NCBI, ExPASy, EBI, Israel, Japan]
Agam K., von Campenhausen M., Levy S., Ben-Ami H.C., Cook B., Kirschfeld K., Minke B.;
"Metabolic stress reversibly activates the Drosophila light-sensitive channels TRP and TRPL in vivo.";
J. Neurosci. 20:5748-5755(2000).
[11]
FUNCTION.
PubMed=8918461 [NCBI, ExPASy, EBI, Israel, Japan]
Obukhov A.G., Harteneck C., Zobel A., Harhammer R., Kalkbrenner F., Leopoldt D., Luckhoff A., Nurnberg B., Schultz G.;
"Direct activation of trpl cation channels by G alpha11 subunits.";
EMBO J. 15:5833-5838(1996).
[12]
INTERACTION WITH TRP-GAMMA.
DOI=10.1016/S0896-6273(00)81201-5; PubMed=10896160 [NCBI, ExPASy, EBI, Israel, Japan]
Xu X.-Z.S., Chien F., Butler A., Salkoff L., Montell C.;
"TRPgamma, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL.";
Neuron 26:647-657(2000).
[13]
INTERACTION WITH FKBP59, IDENTIFICATION IN A COMPLEX WITH INAD, AND MUTAGENESIS OF PRO-702 AND PRO-709.
DOI=10.1074/jbc.M104125200; PubMed=11514552 [NCBI, ExPASy, EBI, Israel, Japan]
Goel M., Garcia R., Estacion M., Schilling W.P.;
"Regulation of Drosophila TRPL channels by immunophilin FKBP59.";
J. Biol. Chem. 276:38762-38773(2001).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
DOI=10.1016/S0896-6273(02)00630-X; PubMed=11931743 [NCBI, ExPASy, EBI, Israel, Japan]
Baehner M., Frechter S., Da Silva N., Minke B., Paulsen R., Huber A.;
"Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current.";
Neuron 34:83-93(2002).
[15]
REVIEW.
PubMed=11707492 [NCBI, ExPASy, EBI, Israel, Japan]
Hardie R.C.;
"Phototransduction in Drosophila melanogaster.";
J. Exp. Biol. 204:3403-3409(2001).
Comments
  • FUNCTION: A light-sensitive calcium channel that is required for inositide-mediated Ca(2+) 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 trp-gamma. Activated by fatty acids, metabolic stress, inositols and GTP-binding proteins.
  • SUBUNIT: Forms heteromultimers with trp-gamma and, to a lower extent, with trp. Interacts with FKBP59 in vivo and is found in the inaD signaling complex.
  • SUBCELLULAR LOCATION: 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.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameA
    SynonymsB
    Isoform IDP48994-1
    This is the isoform sequence displayed in this entry.
    NameC
    Isoform IDP48994-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_015739.
  • TISSUE SPECIFICITY: Expressed predominantly in the rhabdomeres of photoreceptor cells.
  • DOMAIN: Binding of calmodulin to binding site 1 is Ca(2+) dependent, whereas binding of calmodulin to site 2 is Ca(2+) independent.
  • SIMILARITY: Belongs to the transient receptor family. STrpC subfamily.
  • SIMILARITY: Contains 3 ANK repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M88185; AAA28979.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAF58904.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE013599; AAM68794.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT001397; AAN71152.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JH0588; JH0588.
RefSeq NP_476895.1; -.
NP_724822.1; -.
NP_724823.1; -.
UniGene Dm.546
3D structure databases
ModBase P48994.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-003682-MON; -.
DMEL-XXX-02:DMEL-XXX-02-003684-MON; -.
Organism-specific databases
FlyBase FBgn0005614; trpl.
Gene expression databases
ArrayExpress P48994; -.
GermOnline CG18345; Drosophila melanogaster.
Ontologies
GO
GO:0016027; Cellular component: inaD signaling complex (inferred from physical interaction from UniProtKB).
GO:0016021; Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0005622; Cellular component: intracellular (inferred from direct assay from UniProtKB).
GO:0005516; Molecular function: calmodulin binding (inferred from direct assay from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0015279; Molecular function: store-operated calcium channel activity (non-traceable author statement from FlyBase).
GO:0007589; Biological process: body fluid secretion (inferred from mutant phenotype from FlyBase).
GO:0006816; Biological process: calcium ion transport (inferred from sequence or structural similarity from UniProtKB).
GO:0019722; Biological process: calcium-mediated signaling (inferred from mutant phenotype from FlyBase).
GO:0050908; Biological process: detection of light stimulus involved in visual perception (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR002110; ANK.
IPR005821; Ion_trans.
IPR002153; Trans_rcpt.
IPR013555; TRP_2.
IPR004729; TRP_channel.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.20; ANK; 1.
Pfam PF00023; Ank; 2.
PF00520; Ion_trans; 1.
PF08344; TRP_2; 1.
Pfam graphical view of domain structure.
PRINTS PR01415; ANKYRIN.
PR01097; TRNSRECEPTRP.
SMART SM00248; ANK; 2.
SMART graphical view of domain structure.
TIGRFAMs TIGR00870; trp; 1.
PROSITE PS50297; ANK_REP_REGION; 1.
PS50088; ANK_REPEAT; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P48994.
Genome annotation databases
Ensembl CG18345; Drosophila melanogaster. [Contig view]
GeneID 36003; -.
KEGG dme:Dmel_CG18345; -.
Phylogenomic databases
HOGENOM P48994; -.
Other
ProtoNet P48994.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ANK repeat; Calcium; Calcium channel; Calcium transport; Calmodulin-binding; Complete proteome; Ion transport; Ionic channel; Membrane; Repeat; Sensory transduction; Transmembrane; Transport; Vision.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1124  1124     Transient-receptor-potential-like protein. PRO_0000215359
TOPO_DOM   1    340  340     Cytoplasmic (Potential). 
TRANSMEM   341    361  21     Potential. 
TOPO_DOM   362    373  12     Extracellular (Potential). 
TRANSMEM   374    394  21     Potential. 
TOPO_DOM   395    431  37     Cytoplasmic (Potential). 
TRANSMEM   432    452  21     Potential. 
TOPO_DOM   453    512  60     Extracellular (Potential). 
TRANSMEM   513    533  21     Potential. 
TOPO_DOM   534    548  15     Cytoplasmic (Potential). 
TRANSMEM   549    569  21     Potential. 
TOPO_DOM   570    645  76     Extracellular (Potential). 
TRANSMEM   646    666  21     Potential. 
TOPO_DOM   667   1124  458     Cytoplasmic (Potential). 
REPEAT   40     69  30     ANK 1. 
REPEAT   78    107  30     ANK 2. 
REPEAT   152    181  30     ANK 3. 
REGION   710    728  19     Calmodulin-binding 1. 
REGION   853    895  43     Calmodulin-binding 2. 
VAR_SEQ   1    358        Missing (in isoform C). VSP_015739
MUTAGEN   702    702        P->Q: Abolishes interaction with FKBP59. 
MUTAGEN   709    709        P->Q: Abolishes interaction with FKBP59. 
MUTAGEN   713    713        W->G: Disrupts Ca(2+) inflow through the channel. Calmodulin has little effect on Ca(2+) flow. 
MUTAGEN   814    814        W->G: Does not abolish Ca(2+) inflow through the channel. Calmodulin has no effect on initial rates. 
CONFLICT   228    229        II -> SS (in Ref. 1; AAA28979). 
Sequence information
Length: 1124 AA [This is the length of the unprocessed precursor] Molecular weight: 127750 Da [This is the MW of the unprocessed precursor] CRC64: AF6323BA27626583 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGRKKKLPTG VSSGVSHASS APKSVGGCCV PLGLPQPLLL EEKKFLLAVE RGDMPNVRRI 

        70         80         90        100        110        120 
LQKALRHQHI NINCMDPLGR RALTLAIDNE NLEMVELLVV MGVETKDALL HAINAEFVEA 

       130        140        150        160        170        180 
VELLLEHEEL IYKEGEPYSW QKVDINTAMF APDITPLMLA AHKNNFEILR ILLDRGAAVP 

       190        200        210        220        230        240 
VPHDIRCGCE ECVRLTAEDS LRHSLSRVNI YRALCSPSLI CLTSNDPIIT AFQLSWELRN 

       250        260        270        280        290        300 
LALTEQECKS EYMDLRRQCQ KFAVDLLDQT RTSNELAIIL NYDPQMSSYE PGDRMSLTRL 

       310        320        330        340        350        360 
VQAISYKQKK FVAHSNIQQL LSSIWYDGLP GFRRKSIVDK VICIAQVAVL FPLYCLIYMC 

       370        380        390        400        410        420 
APNCRTGQLM RKPFMKFLIH ASSYLFFLFI LILVSQRADD DFVRIFGTTR MKKELAEQEL 

       430        440        450        460        470        480 
RQRGQTPSKL ELIVVMYVIG FVWEEVQEIF AVGMKSYLRN MWNFIDFLRN SLYVSVMCLR 

       490        500        510        520        530        540 
AFAYIQQATE IARDPQMAYI PREKWHDFDP QLIAEGLFAA ANVFSALKLV HLFSINPHLG 

       550        560        570        580        590        600 
PLQISLGRMV IDIVKFFFIY TLVLFAFACG LNQLLWYFAA LEKSKCYVLP GGEADWGSHG 

       610        620        630        640        650        660 
DSCMKWRRFG NLFESSQSLF WASFGMVGLD DFELSGIKSY TRFWGLLMFG SYSVINVIVL 

       670        680        690        700        710        720 
LNLLIAMMSN SYAMIDEHSD TEWKFARTKL WMSYFEDSAT LPPPFNVLPS VKWVIRIFRK 

       730        740        750        760        770        780 
SSKTIDRQRS KKRKEQEQFS EYDNIMRSLV WRYVAAMHRK FENNPVSEDD INEVKSEINT 

       790        800        810        820        830        840 
MRYEMLEIFE NSGMDVSSAN KKERQPRPRR IKVWERRLMK GFQVAPVQNG CELDAFGNVN 

       850        860        870        880        890        900 
GQGEMQEIKV ESIPSKPAKE TAKERFQRVA RTVLLQSTTH KWNVVLRAAK DSQIGRCTKN 

       910        920        930        940        950        960 
ERKSLQNLGR AIEEAKRLIM LNPGCPSGRE SPIRIEFEDE KTSTLLELLN QISAEISDSE 

       970        980        990       1000       1010       1020 
KPKIRPIWRP PLKTVPARAM AANNTRSLTA PELKISRKSS PAPTPTPTPG VSHTALSQFR 

      1030       1040       1050       1060       1070       1080 
NRELPLCPSK LIANSAPSAP TAPPKKSAPT APTPTYKPTT HAPFSVEGGN RENTRASDGV 

      1090       1100       1110       1120 
RSDNSNFDIH VVDLDEKGGH LGRDNVSDIS SIASTSPQRP KHRN 

P48994 in FASTA format

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View entry in raw text format (no links)
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