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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
  • manganese ion transport Source: GO_Central
  • mitochondrion organization Source: FlyBase
  • olfactory learning Source: UniProtKB
  • phospholipase C-inhibiting G-protein coupled receptor signaling pathway Source: FlyBase
  • photoreceptor cell maintenance Source: FlyBase
  • phototransduction Source: FlyBase
  • phototransduction, visible light Source: FlyBase
  • protein localization Source: UniProtKB
  • regulation of cytosolic calcium ion concentration Source: GO_Central
  • response to light stimulus Source: UniProtKB
  • retina homeostasis Source: FlyBase
  • rhodopsin metabolic process Source: FlyBase
  • 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)DescriptionActionsGraphical viewLength
Topological domaini1 – 366CytoplasmicSequence analysisAdd BLAST366
Transmembranei367 – 387HelicalSequence analysisAdd BLAST21
Topological domaini388 – 418ExtracellularSequence analysisAdd BLAST31
Transmembranei419 – 439HelicalSequence analysisAdd BLAST21
Topological domaini440 – 450CytoplasmicSequence analysisAdd BLAST11
Transmembranei451 – 471HelicalSequence analysisAdd BLAST21
Topological domaini472 – 541ExtracellularSequence analysisAdd BLAST70
Transmembranei542 – 562HelicalSequence analysisAdd BLAST21
Topological domaini563 – 609CytoplasmicSequence analysisAdd BLAST47
Transmembranei610 – 630HelicalSequence analysisAdd BLAST21
Topological domaini631 – 637ExtracellularSequence analysis7
Transmembranei638 – 658HelicalSequence analysisAdd BLAST21
Topological domaini659 – 1275CytoplasmicSequence analysisAdd BLAST617

GO - Cellular componenti

  • cation channel complex Source: FlyBase
  • inaD signaling complex Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: GO_Central
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi500P → T in P365; photoreceptors respond normally to light. 2 Publications1
Mutagenesisi531H → N in P365; photoreceptors respond normally to light. 2 Publications1
Mutagenesisi550F → I in P365; defective in the response to light due to rapid degeneration of photoreceptors. 2 Publications1
Mutagenesisi867S → F in P365; photoreceptors respond normally to light. 2 Publications1
Mutagenesisi1266V → D: Does not disrupt inaD binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002153571 – 1275Transient receptor potential proteinAdd BLAST1275

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

BgeeiFBgn0003861.
ExpressionAtlasiP19334. baseline.
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 interactors.
IntActiP19334. 4 interactors.
STRINGi7227.FBpp0084879.

Structurei

Secondary structure

11275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1262 – 1264Combined sources3
Turni1265 – 1267Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati69 – 98ANK 1Add BLAST30
Repeati143 – 172ANK 2Add BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1161 – 1236Asp-richAdd BLAST76

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.
OMAiGRMISGW.
OrthoDBiEOG091G029I.
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 differs from that shown. Reason: Frameshift at position 721.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti188M → T (PubMed:2516726).Curated1
Sequence conflicti188M → T (PubMed:2482778).Curated1
Sequence conflicti222A → V in AAA28976 (PubMed:2516726).Curated1
Sequence conflicti237S → T in AAQ22416 (Ref. 5) Curated1
Sequence conflicti261A → T in AAQ22416 (Ref. 5) Curated1
Sequence conflicti285 – 288GQRQ → ASSE in AAA56928 (PubMed:2482778).Curated4
Sequence conflicti326 – 329RRKQ → PQE in AAA56928 (PubMed:2482778).Curated4
Sequence conflicti365 – 374KPFVKFITHS → NPLSSSSRTP in AAA56928 (PubMed:2482778).Curated10
Sequence conflicti785N → S in AAA28976 (PubMed:2516726).Curated1
Sequence conflicti1008A → P (PubMed:2516726).Curated1
Sequence conflicti1008A → P (PubMed:2482778).Curated1
Sequence conflicti1197K → R (Ref. 5) Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5F67X-ray1.76C/D1259-1275[»]
ProteinModelPortaliP19334.
SMRiP19334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68399. 7 interactors.
IntActiP19334. 4 interactors.
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.
OMAiGRMISGW.
OrthoDBiEOG091G029I.
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

BgeeiFBgn0003861.
ExpressionAtlasiP19334. baseline.
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...

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: November 30, 2016
This is version 162 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.