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P48994 (TRPL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transient-receptor-potential-like protein
Gene names
Name:trpl
ORF Names:CG18345
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length1124 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A light-sensitive calcium channel that is required for inositide-mediated Ca2+ 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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.15

Subunit structure

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. Ref.7 Ref.13 Ref.14

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. Ref.8 Ref.15

Tissue specificity

Expressed predominantly in the rhabdomeres of photoreceptor cells. Ref.1

Domain

Binding of calmodulin to binding site 1 is Ca2+ dependent, whereas binding of calmodulin to site 2 is Ca2+ independent.

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. STrpC subfamily. [View classification]

Contains 3 ANK repeats.

Sequence caution

The sequence AAN71152.1 differs from that shown. Reason: Inron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11241124Transient-receptor-potential-like protein
PRO_0000215359

Regions

Topological domain1 – 340340Cytoplasmic Potential
Transmembrane341 – 36121Helical; Potential
Topological domain362 – 37312Extracellular Potential
Transmembrane374 – 39421Helical; Potential
Topological domain395 – 43137Cytoplasmic Potential
Transmembrane432 – 45221Helical; Potential
Topological domain453 – 51260Extracellular Potential
Transmembrane513 – 53321Helical; Potential
Topological domain534 – 54815Cytoplasmic Potential
Transmembrane549 – 56921Helical; Potential
Topological domain570 – 64576Extracellular Potential
Transmembrane646 – 66621Helical; Potential
Topological domain667 – 1124458Cytoplasmic Potential
Repeat40 – 6930ANK 1
Repeat78 – 10730ANK 2
Repeat152 – 18130ANK 3
Region710 – 72819Calmodulin-binding 1
Region853 – 89543Calmodulin-binding 2

Experimental info

Mutagenesis7021P → Q: Abolishes interaction with FKBP59. Ref.14
Mutagenesis7091P → Q: Abolishes interaction with FKBP59. Ref.14
Mutagenesis7131W → G: Disrupts Ca(2+) inflow through the channel. Calmodulin has little effect on Ca(2+) flow. Ref.8
Mutagenesis8141W → G: Does not abolish Ca(2+) inflow through the channel. Calmodulin has no effect on initial rates. Ref.8
Sequence conflict228 – 2292II → SS in AAA28979. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P48994 [UniParc].

Last modified November 25, 2002. Version 2.
Checksum: AF6323BA27626583

FASTA1,124127,750
        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

« Hide

References

« Hide 'large scale' references
[1]"Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene."
Phillips A.M., Bull A.L., Kelly L.E.
Neuron 8:631-642(1992) [PubMed: 1314616] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CALMODULIN-BINDING, TISSUE SPECIFICITY.
Strain: Oregon-R.
[2]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
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.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[5]Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
[6]"Identification and characterization of two distinct calmodulin-binding sites in the Trpl ion-channel protein of Drosophila melanogaster."
Warr C.G., Kelly L.E.
Biochem. J. 314:497-503(1996) [PubMed: 8670063] [Abstract]
Cited for: CALMODULIN-BINDING.
[7]"Coassembly of TRP and TRPL produces a distinct store-operated conductance."
Xu X.-Z.S., Li H.-S., Guggino W.B., Montell C.
Cell 89:1155-1164(1997) [PubMed: 9215637] [Abstract]
Cited for: INTERACTION WITH TRP.
[8]"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., Brereton H., Barritt G.J.
Biochem. J. 330:1149-1158(1998) [PubMed: 9494079] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-713 AND TRP-814.
[9]"Ca2+-dependent interaction of the trpl cation channel and calmodulin."
Trost C., Marquart A., Zimmer S., Philipp S., Cavalie A., Flockerzi V.
FEBS Lett. 451:257-263(1999) [PubMed: 10371201] [Abstract]
Cited for: CALMODULIN-BINDING.
[10]"Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL."
Chyb S., Raghu P., Hardie R.C.
Nature 397:255-259(1999) [PubMed: 9930700] [Abstract]
Cited for: FUNCTION.
[11]"Metabolic stress reversibly activates the Drosophila light-sensitive channels TRP and TRPL in vivo."
Agam K., von Campenhausen M., Levy S., Ben-Ami H.C., Cook B., Kirschfeld K., Minke B.
J. Neurosci. 20:5748-5755(2000) [PubMed: 10908615] [Abstract]
Cited for: FUNCTION.
[12]"Direct activation of trpl cation channels by G alpha11 subunits."
Obukhov A.G., Harteneck C., Zobel A., Harhammer R., Kalkbrenner F., Leopoldt D., Luckhoff A., Nurnberg B., Schultz G.
EMBO J. 15:5833-5838(1996) [PubMed: 8918461] [Abstract]
Cited for: FUNCTION.
[13]"TRPgamma, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL."
Xu X.-Z.S., Chien F., Butler A., Salkoff L., Montell C.
Neuron 26:647-657(2000) [PubMed: 10896160] [Abstract]
Cited for: INTERACTION WITH TRP-GAMMA.
[14]"Regulation of Drosophila TRPL channels by immunophilin FKBP59."
Goel M., Garcia R., Estacion M., Schilling W.P.
J. Biol. Chem. 276:38762-38773(2001) [PubMed: 11514552] [Abstract]
Cited for: INTERACTION WITH FKBP59, IDENTIFICATION IN A COMPLEX WITH INAD, MUTAGENESIS OF PRO-702 AND PRO-709.
[15]"Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current."
Baehner M., Frechter S., Da Silva N., Minke B., Paulsen R., Huber A.
Neuron 34:83-93(2002) [PubMed: 11931743] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]"Phototransduction in Drosophila melanogaster."
Hardie R.C.
J. Exp. Biol. 204:3403-3409(2001) [PubMed: 11707492] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M88185 mRNA. Translation: AAA28979.1.
AE013599 Genomic DNA. Translation: AAF58904.1.
AE013599 Genomic DNA. Translation: AAM68793.1.
AE013599 Genomic DNA. Translation: AAM68794.2.
BT001397 mRNA. Translation: AAN71152.1. Sequence problems.
BT099607 mRNA. Translation: ACU45760.1.
PIRJH0588.
RefSeqNP_476895.1. NM_057547.4.
NP_724822.1. NM_165694.2.
NP_724823.2. NM_165695.2.
UniGeneDm.546.

3D structure databases

ProteinModelPortalP48994.
SMRP48994. Positions 43-182.
ModBaseSearch...

Protein-protein interaction databases

IntActP48994. 1 interaction.
STRINGP48994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0088471; FBpp0087555; FBgn0005614.
FBtr0088473; FBpp0087557; FBgn0005614.
FBtr0301662; FBpp0290876; FBgn0005614.
GeneID36003.
KEGGdme:Dmel_CG18345.
UCSCCG18345-RA. d. melanogaster.

Organism-specific databases

CTD36003.
FlyBaseFBgn0005614. trpl.

Phylogenomic databases

eggNOGinNOG07559.
GeneTreeEMGT00050000000109.
InParanoidP48994.
OMADINTAMF.
OrthoDBEOG4TDZ13.
PhylomeDBP48994.

Gene expression databases

BgeeP48994.
GermOnlineCG18345. Drosophila melanogaster.

Family and domain databases

InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans.
IPR013555. TRP_2.
IPR004729. TRP_channel.
IPR002153. TRPC_channel.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
KOK13803.
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSPR01097. TRNSRECEPTRP.
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
TIGRFAMsTIGR00870. Trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio796287.

Entry information

Entry nameTRPL_DROME
AccessionPrimary (citable) accession number: P48994
Secondary accession number(s): C6TPC1 expand/collapse secondary AC list , Q0E9E3, Q8IH62, Q8MKU9, Q9V5B2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 25, 2002
Last modified: January 25, 2012
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents