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Protein

Transient receptor potential protein

Gene

trp

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. Ca2+ influx may then feed back and inhibit PLC, thereby facilitating phosphatidylinositol 4,5 bisphosphate (PIP2) recycling. Trp and trpl act together in the light response, though it is unclear whether as heteromultimers or as distinct units, and are activated by fatty acids and metabolic stress. Also required for olfactory adaptation and may be involved in olfactory system development.5 Publications

GO - Molecular functioni

  • calcium channel activity Source: UniProtKB
  • calcium-release channel activity Source: FlyBase
  • calmodulin binding Source: FlyBase
  • identical protein binding Source: FlyBase
  • light-activated ion channel activity Source: FlyBase
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • store-operated calcium channel activity Source: FlyBase

GO - Biological processi

  • calcium ion transmembrane transport Source: FlyBase
  • calcium ion transport Source: UniProtKB
  • calcium-mediated signaling Source: FlyBase
  • cellular response to anoxia Source: FlyBase
  • detection of light stimulus involved in sensory perception Source: FlyBase
  • detection of light stimulus involved in visual perception Source: UniProtKB
  • light-induced release of internally sequestered calcium ion Source: FlyBase
  • olfactory learning Source: UniProtKB
  • phospholipase C-inhibiting G-protein coupled receptor signaling pathway Source: FlyBase
  • phototransduction, visible light Source: FlyBase
  • protein localization Source: UniProtKB
  • release of sequestered calcium ion into cytosol Source: GOC
  • response to light stimulus Source: UniProtKB
  • sensory perception of smell Source: UniProtKB-KW
  • sensory perception of sound Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Olfaction, 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.
SignaLinkiP19334.

Protein family/group databases

TCDBi1.A.4.1.1. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential protein
Gene namesi
Name:trp
ORF Names:CG7875
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0003861. trp.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 366366CytoplasmicSequence analysisAdd
BLAST
Transmembranei367 – 38721HelicalSequence analysisAdd
BLAST
Topological domaini388 – 41831ExtracellularSequence analysisAdd
BLAST
Transmembranei419 – 43921HelicalSequence analysisAdd
BLAST
Topological domaini440 – 45011CytoplasmicSequence analysisAdd
BLAST
Transmembranei451 – 47121HelicalSequence analysisAdd
BLAST
Topological domaini472 – 54170ExtracellularSequence analysisAdd
BLAST
Transmembranei542 – 56221HelicalSequence analysisAdd
BLAST
Topological domaini563 – 60947CytoplasmicSequence analysisAdd
BLAST
Transmembranei610 – 63021HelicalSequence analysisAdd
BLAST
Topological domaini631 – 6377ExtracellularSequence analysis
Transmembranei638 – 65821HelicalSequence analysisAdd
BLAST
Topological domaini659 – 1275617CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi500 – 5001P → T in P365; photoreceptors respond normally to light. 2 Publications
Mutagenesisi531 – 5311H → N in P365; photoreceptors respond normally to light. 2 Publications
Mutagenesisi550 – 5501F → I in P365; defective in the response to light due to rapid degeneration of photoreceptors. 2 Publications
Mutagenesisi867 – 8671S → F in P365; photoreceptors respond normally to light. 2 Publications
Mutagenesisi1266 – 12661V → D: Does not disrupt inaD binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12751275Transient receptor potential proteinPRO_0000215357Add
BLAST

Post-translational modificationi

Phosphorylated by inaC.1 Publication

Proteomic databases

PaxDbiP19334.
PRIDEiP19334.

Expressioni

Tissue specificityi

Expressed predominantly in the rhabdomeres of photoreceptor cells. Expressed in the third antennal segment and in the olfactory segment at approximately 70 hours after puparium formation during antennal development.4 Publications

Gene expression databases

BgeeiP19334.
ExpressionAtlasiP19334. differential.
GenevisibleiP19334. DM.

Interactioni

Subunit structurei

The C-terminus interacts with a PDZ domain of inaD to form the core of the inaD signaling complex. Other members of the complex include norpA (PLC), inaC (PKC), and possibly trpl, ninaC, FKBP59, calmodulin and rhodopsin. Forms homomultimers and heteromultimers with trpl. Interaction with trpl is mediated in part by the N-terminal region and the transmembrane domains. Also interacts, though to a lower extent, with Trpgamma.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
inaDQ240085EBI-165136,EBI-195326

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi68399. 7 interactions.
IntActiP19334. 4 interactions.
STRINGi7227.FBpp0084879.

Structurei

Secondary structure

1
1275
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1262 – 12643Combined sources
Turni1265 – 12673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5F67X-ray1.76C/D1259-1275[»]
ProteinModelPortaliP19334.
SMRiP19334. Positions 146-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati69 – 9830ANK 1Add
BLAST
Repeati143 – 17230ANK 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1161 – 123676Asp-richAdd
BLAST

Sequence similaritiesi

Contains 2 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3609. Eukaryota.
ENOG410XQ0Y. LUCA.
InParanoidiP19334.
KOiK04967.
OMAiKLAIRYK.
OrthoDBiEOG776SP6.
PhylomeDBiP19334.

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.
PfamiPF00520. 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.

P19334-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSNTESDAE KALGSRLDYD LMMAEEYILS DVEKNFILSC ERGDLPGVKK
60 70 80 90 100
ILEEYQGTDK FNINCTDPMN RSALISAIEN ENFDLMVILL EHNIEVGDAL
110 120 130 140 150
LHAISEEYVE AVEELLQWEE TNHKEGQPYS WEAVDRSKST FTVDITPLIL
160 170 180 190 200
AAHRNNYEIL KILLDRGATL PMPHDVKCGC DECVTSQMTD SLRHSQSRIN
210 220 230 240 250
AYRALSASSL IALSSRDPVL TAFQLSWELK RLQAMESEFR AEYTEMRQMV
260 270 280 290 300
QDFGTSLLDH ARTSMELEVM LNFNHEPSHD IWCLGQRQTL ERLKLAIRYK
310 320 330 340 350
QKTFVAHPNV QQLLAAIWYD GLPGFRRKQA SQQLMDVVKL GCSFPIYSLK
360 370 380 390 400
YILAPDSEGA KFMRKPFVKF ITHSCSYMFF LMLLGAASLR VVQITFELLA
410 420 430 440 450
FPWMLTMLED WRKHERGSLP GPIELAIITY IMALIFEELK SLYSDGLFEY
460 470 480 490 500
IMDLWNIVDY ISNMFYVTWI LCRATAWVIV HRDLWFRGID PYFPREHWHP
510 520 530 540 550
FDPMLLSEGA FAAGMVFSYL KLVHIFSINP HLGPLQVSLG RMIIDIIKFF
560 570 580 590 600
FIYTLVLFAF GCGLNQLLWY YAELEKNKCY HLHPDVADFD DQEKACTIWR
610 620 630 640 650
RFSNLFETSQ SLFWASFGLV DLVSFDLAGI KSFTRFWALL MFGSYSVINI
660 670 680 690 700
IVLLNMLIAM MSNSYQIISE RADTEWKFAR SQLWMSYFED GGTIPPPFNL
710 720 730 740 750
CPNMKMLRKT LGRKRPSRTK SFMRKSMERA QTLHDKVMKL LVRRYITAEQ
760 770 780 790 800
RRRDDYGITE DDIIEVRQDI SSLRFELLEI FTNNNWDVPD IEKKSQGVAR
810 820 830 840 850
TTKGKVMERR ILKDFQIGFV ENLKQEMSES ESGRDIFSSL AKVIGRKKTQ
860 870 880 890 900
KGDKDWNAIA RKNTFASDPI GSKRSSMQRH SQRSLRRKII EQANEGLQMN
910 920 930 940 950
QTQLIEFNPN LGDVTRATRV AYVKFMRKKM AADEVSLADD EGAPNGEGEK
960 970 980 990 1000
KPLDASGSKK SITSGGTGGG ASMLAAAALR ASVKNVDEKS GADGKPGTMG
1010 1020 1030 1040 1050
KPTDDKKAGD DKDKQQPPKD SKPSAGGPKP GDQKPTPGAG APKPQAAGTI
1060 1070 1080 1090 1100
SKPGESQKKD APAPPTKPGD TKPAAPKPGE SAKPEAAAKK EESSKTEASK
1110 1120 1130 1140 1150
PAATNGAAKS AAPSAPSDAK PDSKLKPGAA GAPEATKATN GASKPDEKKS
1160 1170 1180 1190 1200
GPEEPKKAAG DSKPGDDAKD KDKKPGDDKD KKPGDDKDKK PADNNDKKPA
1210 1220 1230 1240 1250
DDKDKKPGDD KDKKPGDDKD KKPSDDKDKK PADDKDKKPA AAPLKPAIKV
1260 1270
GQSSAAAGGE RGKSTVTGRM ISGWL
Length:1,275
Mass (Da):142,594
Last modified:September 27, 2005 - v3
Checksum:i4376C1B853868B4C
GO

Sequence cautioni

The sequence AAQ22416.1 differs from that shown. Reason: Frameshift at position 721. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881M → T (PubMed:2516726).Curated
Sequence conflicti188 – 1881M → T (PubMed:2482778).Curated
Sequence conflicti222 – 2221A → V in AAA28976 (PubMed:2516726).Curated
Sequence conflicti237 – 2371S → T in AAQ22416 (Ref. 5) Curated
Sequence conflicti261 – 2611A → T in AAQ22416 (Ref. 5) Curated
Sequence conflicti285 – 2884GQRQ → ASSE in AAA56928 (PubMed:2482778).Curated
Sequence conflicti326 – 3294RRKQ → PQE in AAA56928 (PubMed:2482778).Curated
Sequence conflicti365 – 37410KPFVKFITHS → NPLSSSSRTP in AAA56928 (PubMed:2482778).Curated
Sequence conflicti785 – 7851N → S in AAA28976 (PubMed:2516726).Curated
Sequence conflicti1008 – 10081A → P (PubMed:2516726).Curated
Sequence conflicti1008 – 10081A → P (PubMed:2482778).Curated
Sequence conflicti1197 – 11971K → R (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34394 Genomic DNA. Translation: AAA28976.1.
M21306 Genomic DNA. Translation: AAA56928.1.
AE014297 Genomic DNA. Translation: AAF56970.1.
BT009947 mRNA. Translation: AAQ22416.1. Frameshift.
M18634 Genomic DNA. Translation: AAA28977.1.
PIRiJN0015.
JU0092.
RefSeqiNP_476768.1. NM_057420.4.
UniGeneiDm.21694.

Genome annotation databases

EnsemblMetazoaiFBtr0085513; FBpp0084879; FBgn0003861.
GeneIDi43542.
KEGGidme:Dmel_CG7875.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34394 Genomic DNA. Translation: AAA28976.1.
M21306 Genomic DNA. Translation: AAA56928.1.
AE014297 Genomic DNA. Translation: AAF56970.1.
BT009947 mRNA. Translation: AAQ22416.1. Frameshift.
M18634 Genomic DNA. Translation: AAA28977.1.
PIRiJN0015.
JU0092.
RefSeqiNP_476768.1. NM_057420.4.
UniGeneiDm.21694.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5F67X-ray1.76C/D1259-1275[»]
ProteinModelPortaliP19334.
SMRiP19334. Positions 146-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68399. 7 interactions.
IntActiP19334. 4 interactions.
STRINGi7227.FBpp0084879.

Protein family/group databases

TCDBi1.A.4.1.1. the transient receptor potential ca(2+) channel (trp-cc) family.

Proteomic databases

PaxDbiP19334.
PRIDEiP19334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085513; FBpp0084879; FBgn0003861.
GeneIDi43542.
KEGGidme:Dmel_CG7875.

Organism-specific databases

CTDi43542.
FlyBaseiFBgn0003861. trp.

Phylogenomic databases

eggNOGiKOG3609. Eukaryota.
ENOG410XQ0Y. LUCA.
InParanoidiP19334.
KOiK04967.
OMAiKLAIRYK.
OrthoDBiEOG776SP6.
PhylomeDBiP19334.

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.
SignaLinkiP19334.

Miscellaneous databases

ChiTaRSitrp. fly.
GenomeRNAii43542.
PROiP19334.

Gene expression databases

BgeeiP19334.
ExpressionAtlasiP19334. differential.
GenevisibleiP19334. 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.
PfamiPF00520. 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. "Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction."
    Montell C., Rubin G.M.
    Neuron 2:1313-1323(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Oregon-R.
  2. "Proper function of the Drosophila trp gene product during pupal development is important for normal visual transduction in the adult."
    Wong F., Schaefer E.L., Roop B.C., Lamendola J.N., Johnson-Seaton D., Shao D.
    Neuron 3:81-94(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Overlapping transcription units in the transient receptor potential locus of Drosophila melanogaster."
    Wong F., Yuh Z.T., Schaefer E.L., Roop B.C., Ally A.H.
    Somat. Cell Mol. Genet. 13:661-669(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1126-1275.
  7. "TRP, a protein essential for inositide-mediated Ca2+ influx is localized adjacent to the calcium stores in Drosophila photoreceptors."
    Pollock J.A., Assaf A., Peretz A., Nichols C.D., Mojet M.H., Hardie R.C., Minke B.
    J. Neurosci. 15:3747-3760(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "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: HOMOMULTIMERIZATION, INTERACTION WITH TRPL.
  9. "Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex."
    Chevesich J., Kreuz A.J., Montell C.
    Neuron 18:95-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH INAD; NORPA; RHODOPSIN AND CALMODULIN.
  10. "Olfactory adaptation depends on the Trp Ca2+ channel in Drosophila."
    Stortkuhl K.F., Hovemann B.T., Carlson J.R.
    J. Neurosci. 19:4839-4846(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  11. "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.
  12. "Reversible phosphorylation of the signal transduction complex in Drosophila photoreceptors."
    Liu M., Parker L.L., Wadzinski B.E., Shieh B.-H.
    J. Biol. Chem. 275:12194-12199(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  13. "TRP and the PDZ protein, INAD, form the core complex required for retention of the signalplex in Drosophila photoreceptor cells."
    Li H.-S., Montell C.
    J. Cell Biol. 150:1411-1422(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INAD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF VAL-1266.
  14. "Novel mechanism of massive photoreceptor degeneration caused by mutations in the trp gene of Drosophila."
    Yoon J., Ben-Ami H.C., Hong Y.S., Park S., Strong L.L.R., Bowman J.D., Geng C., Baek K., Minke B., Pak W.L.
    J. Neurosci. 20:649-659(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF PRO-500; HIS-531; PHE-550 AND SER-867.
  15. "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.
  16. "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.
  17. "Single amino acid change in the fifth transmembrane segment of the TRP Ca2+ channel causes massive degeneration of photoreceptors."
    Hong Y.S., Park S., Geng C., Baek K., Bowman J.D., Yoon J., Pak W.L.
    J. Biol. Chem. 277:33884-33889(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-500; HIS-531; PHE-550 AND SER-867.
  18. "Phototransduction in Drosophila melanogaster."
    Hardie R.C.
    J. Exp. Biol. 204:3403-3409(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiTRP_DROME
AccessioniPrimary (citable) accession number: P19334
Secondary accession number(s): Q7YU76, Q9VAE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: September 27, 2005
Last modified: June 8, 2016
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.