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Protein

Transient-receptor-potential-like protein

Gene

trpl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 Trpgamma. Activated by fatty acids, metabolic stress, inositols and GTP-binding proteins.5 Publications

GO - Molecular functioni

  • calcium channel activity Source: FlyBase
  • calmodulin binding Source: UniProtKB
  • cation channel activity Source: FlyBase
  • identical protein binding Source: FlyBase
  • ion transmembrane transporter activity Source: UniProtKB
  • light-activated ion channel activity Source: FlyBase
  • protein heterodimerization activity Source: UniProtKB
  • store-operated calcium channel activity Source: GO_Central

GO - Biological processi

  • body fluid secretion Source: FlyBase
  • calcium ion transmembrane transport Source: FlyBase
  • calcium ion transport Source: UniProtKB
  • calcium-mediated signaling Source: FlyBase
  • cation transport Source: FlyBase
  • cellular response to anoxia Source: FlyBase
  • detection of light stimulus involved in visual perception Source: UniProtKB
  • ion transport Source: UniProtKB
  • manganese ion transport Source: GO_Central
  • phototransduction, visible light Source: FlyBase
  • regulation of cytosolic calcium ion concentration Source: GO_Central
  • response to light stimulus Source: FlyBase
  • sensory perception of sound Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Sensory transduction, Transport, Vision

Keywords - Ligandi

Calcium, Calmodulin-binding

Enzyme and pathway databases

ReactomeiR-DME-3295583. TRP channels.
R-DME-5578775. Ion homeostasis.
R-DME-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP48994.

Protein family/group databases

TCDBi1.A.4.1.8. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient-receptor-potential-like protein
Gene namesi
Name:trpl
ORF Names:CG18345
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0005614. trpl.

Subcellular locationi

  • Membrane 2 Publications; Multi-pass membrane protein 2 Publications

  • 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 340340CytoplasmicSequence analysisAdd
BLAST
Transmembranei341 – 36121HelicalSequence analysisAdd
BLAST
Topological domaini362 – 37312ExtracellularSequence analysisAdd
BLAST
Transmembranei374 – 39421HelicalSequence analysisAdd
BLAST
Topological domaini395 – 43137CytoplasmicSequence analysisAdd
BLAST
Transmembranei432 – 45221HelicalSequence analysisAdd
BLAST
Topological domaini453 – 51260ExtracellularSequence analysisAdd
BLAST
Transmembranei513 – 53321HelicalSequence analysisAdd
BLAST
Topological domaini534 – 54815CytoplasmicSequence analysisAdd
BLAST
Transmembranei549 – 56921HelicalSequence analysisAdd
BLAST
Topological domaini570 – 64576ExtracellularSequence analysisAdd
BLAST
Transmembranei646 – 66621HelicalSequence analysisAdd
BLAST
Topological domaini667 – 1124458CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cation channel complex Source: FlyBase
  • dendrite Source: FlyBase
  • inaD signaling complex Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
  • intracellular Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • rhabdomere Source: FlyBase
  • rhabdomere microvillus membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi702 – 7021P → Q: Abolishes interaction with FKBP59. 1 Publication
Mutagenesisi709 – 7091P → Q: Abolishes interaction with FKBP59. 1 Publication
Mutagenesisi713 – 7131W → G: Disrupts Ca(2+) inflow through the channel. Calmodulin has little effect on Ca(2+) flow. 1 Publication
Mutagenesisi814 – 8141W → G: Does not abolish Ca(2+) inflow through the channel. Calmodulin has no effect on initial rates. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11241124Transient-receptor-potential-like proteinPRO_0000215359Add
BLAST

Proteomic databases

PaxDbiP48994.
PRIDEiP48994.

Expressioni

Tissue specificityi

Expressed predominantly in the rhabdomeres of photoreceptor cells.1 Publication

Gene expression databases

BgeeiP48994.
ExpressionAtlasiP48994. differential.
GenevisibleiP48994. DM.

Interactioni

Subunit structurei

Forms heteromultimers with Trpgamma and, to a lower extent, with trp. Interacts with FKBP59 in vivo and is found in the inaD signaling complex.3 Publications

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • identical protein binding Source: FlyBase
  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi61834. 4 interactions.
IntActiP48994. 2 interactions.
STRINGi7227.FBpp0290876.

Structurei

3D structure databases

ProteinModelPortaliP48994.
SMRiP48994. Positions 43-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati40 – 6930ANK 1Add
BLAST
Repeati78 – 10730ANK 2Add
BLAST
Repeati152 – 18130ANK 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni710 – 72819Calmodulin-binding 1Add
BLAST
Regioni853 – 89543Calmodulin-binding 2Add
BLAST

Domaini

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

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3609. Eukaryota.
ENOG410XQ0Y. LUCA.
GeneTreeiENSGT00760000119180.
InParanoidiP48994.
KOiK13803.
OMAiSQIGRCT.
OrthoDBiEOG776SP6.
PhylomeDBiP48994.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERiPTHR10117. PTHR10117. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSiPR01097. TRNSRECEPTRP.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRKKKLPTG VSSGVSHASS APKSVGGCCV PLGLPQPLLL EEKKFLLAVE
60 70 80 90 100
RGDMPNVRRI LQKALRHQHI NINCMDPLGR RALTLAIDNE NLEMVELLVV
110 120 130 140 150
MGVETKDALL HAINAEFVEA VELLLEHEEL IYKEGEPYSW QKVDINTAMF
160 170 180 190 200
APDITPLMLA AHKNNFEILR ILLDRGAAVP VPHDIRCGCE ECVRLTAEDS
210 220 230 240 250
LRHSLSRVNI YRALCSPSLI CLTSNDPIIT AFQLSWELRN LALTEQECKS
260 270 280 290 300
EYMDLRRQCQ KFAVDLLDQT RTSNELAIIL NYDPQMSSYE PGDRMSLTRL
310 320 330 340 350
VQAISYKQKK FVAHSNIQQL LSSIWYDGLP GFRRKSIVDK VICIAQVAVL
360 370 380 390 400
FPLYCLIYMC APNCRTGQLM RKPFMKFLIH ASSYLFFLFI LILVSQRADD
410 420 430 440 450
DFVRIFGTTR MKKELAEQEL RQRGQTPSKL ELIVVMYVIG FVWEEVQEIF
460 470 480 490 500
AVGMKSYLRN MWNFIDFLRN SLYVSVMCLR AFAYIQQATE IARDPQMAYI
510 520 530 540 550
PREKWHDFDP QLIAEGLFAA ANVFSALKLV HLFSINPHLG PLQISLGRMV
560 570 580 590 600
IDIVKFFFIY TLVLFAFACG LNQLLWYFAA LEKSKCYVLP GGEADWGSHG
610 620 630 640 650
DSCMKWRRFG NLFESSQSLF WASFGMVGLD DFELSGIKSY TRFWGLLMFG
660 670 680 690 700
SYSVINVIVL LNLLIAMMSN SYAMIDEHSD TEWKFARTKL WMSYFEDSAT
710 720 730 740 750
LPPPFNVLPS VKWVIRIFRK SSKTIDRQRS KKRKEQEQFS EYDNIMRSLV
760 770 780 790 800
WRYVAAMHRK FENNPVSEDD INEVKSEINT MRYEMLEIFE NSGMDVSSAN
810 820 830 840 850
KKERQPRPRR IKVWERRLMK GFQVAPVQNG CELDAFGNVN GQGEMQEIKV
860 870 880 890 900
ESIPSKPAKE TAKERFQRVA RTVLLQSTTH KWNVVLRAAK DSQIGRCTKN
910 920 930 940 950
ERKSLQNLGR AIEEAKRLIM LNPGCPSGRE SPIRIEFEDE KTSTLLELLN
960 970 980 990 1000
QISAEISDSE KPKIRPIWRP PLKTVPARAM AANNTRSLTA PELKISRKSS
1010 1020 1030 1040 1050
PAPTPTPTPG VSHTALSQFR NRELPLCPSK LIANSAPSAP TAPPKKSAPT
1060 1070 1080 1090 1100
APTPTYKPTT HAPFSVEGGN RENTRASDGV RSDNSNFDIH VVDLDEKGGH
1110 1120
LGRDNVSDIS SIASTSPQRP KHRN
Length:1,124
Mass (Da):127,750
Last modified:November 25, 2002 - v2
Checksum:iAF6323BA27626583
GO

Sequence cautioni

The sequence AAN71152.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2292II → SS in AAA28979 (PubMed:1314616).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJH0588.
RefSeqiNP_476895.1. NM_057547.5.
NP_724822.1. NM_165694.3.
NP_724823.2. NM_165695.2.
UniGeneiDm.546.

Genome annotation databases

EnsemblMetazoaiFBtr0088471; FBpp0087555; FBgn0005614.
FBtr0088473; FBpp0087557; FBgn0005614.
FBtr0301662; FBpp0290876; FBgn0005614.
GeneIDi36003.
KEGGidme:Dmel_CG18345.
UCSCiCG18345-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJH0588.
RefSeqiNP_476895.1. NM_057547.5.
NP_724822.1. NM_165694.3.
NP_724823.2. NM_165695.2.
UniGeneiDm.546.

3D structure databases

ProteinModelPortaliP48994.
SMRiP48994. Positions 43-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61834. 4 interactions.
IntActiP48994. 2 interactions.
STRINGi7227.FBpp0290876.

Protein family/group databases

TCDBi1.A.4.1.8. the transient receptor potential ca(2+) channel (trp-cc) family.

Proteomic databases

PaxDbiP48994.
PRIDEiP48994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088471; FBpp0087555; FBgn0005614.
FBtr0088473; FBpp0087557; FBgn0005614.
FBtr0301662; FBpp0290876; FBgn0005614.
GeneIDi36003.
KEGGidme:Dmel_CG18345.
UCSCiCG18345-RA. d. melanogaster.

Organism-specific databases

CTDi36003.
FlyBaseiFBgn0005614. trpl.

Phylogenomic databases

eggNOGiKOG3609. Eukaryota.
ENOG410XQ0Y. LUCA.
GeneTreeiENSGT00760000119180.
InParanoidiP48994.
KOiK13803.
OMAiSQIGRCT.
OrthoDBiEOG776SP6.
PhylomeDBiP48994.

Enzyme and pathway databases

ReactomeiR-DME-3295583. TRP channels.
R-DME-5578775. Ion homeostasis.
R-DME-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP48994.

Miscellaneous databases

ChiTaRSitrpl. fly.
GenomeRNAii36003.
PROiP48994.

Gene expression databases

BgeeiP48994.
ExpressionAtlasiP48994. differential.
GenevisibleiP48994. DM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERiPTHR10117. PTHR10117. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSiPR01097. TRNSRECEPTRP.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRPGAMMA.
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. "Phototransduction in Drosophila melanogaster."
    Hardie R.C.
    J. Exp. Biol. 204:3403-3409(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiTRPL_DROME
AccessioniPrimary (citable) accession number: P48994
Secondary accession number(s): C6TPC1
, Q0E9E3, Q8IH62, Q8MKU9, Q9V5B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 25, 2002
Last modified: July 6, 2016
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.