Reviewed, UniProtKB/Swiss-Prot P48994 (TRPL_DROME)

Names and origin

Protein names

Recommended name:
    Transient-receptor-potential-like protein

Gene names

Name:	trpl
ORF Names:	CG18345

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1124 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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 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.
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.
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.
Sequence similarities	Belongs to the transient receptor family. STrpC subfamily. Contains 3 ANK repeats.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Sensory transduction Transport Vision
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	ANK repeat Repeat Transmembrane
Ligand	Calcium Calmodulin-binding
Molecular function	Calcium channel Ionic channel
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	body fluid secretion Inferred from mutant phenotype. Source: FlyBase calcium ion transport Ref.1 Ref.13 Inferred from sequence or structural similarity. Source: UniProtKB calcium-mediated signaling Inferred from mutant phenotype. Source: FlyBase detection of light stimulus involved in visual perception Ref.1 Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	inaD signaling complex Ref.13 Inferred from physical interaction. Source: UniProtKB integral to membrane Ref.1 Non-traceable author statement. Source: UniProtKB intracellular Ref.14 Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW calmodulin binding Ref.5 Ref.8 Ref.15 Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Ref.6 Inferred from physical interaction. Source: UniProtKB store-operated calcium channel activity Non-traceable author statement. Source: FlyBase
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P48994-1)

Also known as: B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform C (identifier: P48994-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-358: Missing.

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1124	1124	Transient-receptor-potential-like protein		PRO_0000215359
Regions
	Topological domain	1 – 340	340	Cytoplasmic Potential
	Transmembrane	341 – 361	21	Potential
	Topological domain	362 – 373	12	Extracellular Potential
	Transmembrane	374 – 394	21	Potential
	Topological domain	395 – 431	37	Cytoplasmic Potential
	Transmembrane	432 – 452	21	Potential
	Topological domain	453 – 512	60	Extracellular Potential
	Transmembrane	513 – 533	21	Potential
	Topological domain	534 – 548	15	Cytoplasmic Potential
	Transmembrane	549 – 569	21	Potential
	Topological domain	570 – 645	76	Extracellular Potential
	Transmembrane	646 – 666	21	Potential
	Topological domain	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
Natural variations
	Alternative sequence	1 – 358	358	Missing in isoform C.		VSP_015739
Experimental info
	Mutagenesis	702	1	P → Q: Abolishes interaction with FKBP59
	Mutagenesis	709	1	P → Q: Abolishes interaction with FKBP59
	Mutagenesis	713	1	W → G: Disrupts Ca(2+) inflow through the channel. Calmodulin has little effect on Ca(2+) flow
	Mutagenesis	814	1	W → G: Does not abolish Ca(2+) inflow through the channel. Calmodulin has no effect on initial rates
	Sequence conflict	228 – 229	2	II → SS in AAA28979. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (B) [UniParc]. Last modified November 25, 2002. Version 2. Checksum: AF6323BA27626583	FASTA	1,124	127,750
	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
	Isoform C [UniParc]. Checksum: 7605D50537198966		766	87,382
	10 20 30 40 50 60 MCAPNCRTGQ LMRKPFMKFL IHASSYLFFL FILILVSQRA DDDFVRIFGT TRMKKELAEQ 70 80 90 100 110 120 ELRQRGQTPS KLELIVVMYV IGFVWEEVQE IFAVGMKSYL RNMWNFIDFL RNSLYVSVMC 130 140 150 160 170 180 LRAFAYIQQA TEIARDPQMA YIPREKWHDF DPQLIAEGLF AAANVFSALK LVHLFSINPH 190 200 210 220 230 240 LGPLQISLGR MVIDIVKFFF IYTLVLFAFA CGLNQLLWYF AALEKSKCYV LPGGEADWGS 250 260 270 280 290 300 HGDSCMKWRR FGNLFESSQS LFWASFGMVG LDDFELSGIK SYTRFWGLLM FGSYSVINVI 310 320 330 340 350 360 VLLNLLIAMM SNSYAMIDEH SDTEWKFART KLWMSYFEDS ATLPPPFNVL PSVKWVIRIF 370 380 390 400 410 420 RKSSKTIDRQ RSKKRKEQEQ FSEYDNIMRS LVWRYVAAMH RKFENNPVSE DDINEVKSEI 430 440 450 460 470 480 NTMRYEMLEI FENSGMDVSS ANKKERQPRP RRIKVWERRL MKGFQVAPVQ NGCELDAFGN 490 500 510 520 530 540 VNGQGEMQEI KVESIPSKPA KETAKERFQR VARTVLLQST THKWNVVLRA AKDSQIGRCT 550 560 570 580 590 600 KNERKSLQNL GRAIEEAKRL IMLNPGCPSG RESPIRIEFE DEKTSTLLEL LNQISAEISD 610 620 630 640 650 660 SEKPKIRPIW RPPLKTVPAR AMAANNTRSL TAPELKISRK SSPAPTPTPT PGVSHTALSQ 670 680 690 700 710 720 FRNRELPLCP SKLIANSAPS APTAPPKKSA PTAPTPTYKP TTHAPFSVEG GNRENTRASD 730 740 750 760 GVRSDNSNFD IHVVDLDEKG GHLGRDNVSD ISSIASTSPQ RPKHRN

References

	« Hide 'large scale' referencesShow '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] (ISOFORM A), 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: 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. , 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, ALTERNATIVE SPLICING.
[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] (ISOFORM C). Strain: Berkeley. Tissue: Head.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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
EMBLGenBankDDBJ	M88185 mRNA. Translation: AAA28979.1. AE013599 Genomic DNA. Translation: AAF58904.1. AE013599 Genomic DNA. Translation: AAM68794.1. BT001397 mRNA. Translation: AAN71152.1. Different initiation.
PIR	JH0588.
RefSeq	NP_476895.1. NP_724822.1. NP_724823.1.
UniGene	Dm.546
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P48994.
Genome annotation databases
Ensembl	CG18345. Drosophila melanogaster. [Contig view]
GeneID	36003.
KEGG	dme:Dmel_CG18345.
Organism-specific databases
FlyBase	FBgn0005614. trpl.
Phylogenomic databases
HOGENOM	P48994.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-003682-MON. DMEL-XXX-02:DMEL-XXX-02-003684-MON.
Gene expression databases
ArrayExpress	P48994.
GermOnline	CG18345. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002110. ANK. IPR005821. Ion_trans. IPR002153. Trans_rcpt. IPR013555. TRP_2. IPR004729. TRP_channel. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit.
Pfam	PF00023. Ank. 2 hits. PF00520. Ion_trans. 1 hit. PF08344. TRP_2. 1 hit. [Graphical view]
PRINTS	PR01415. ANKYRIN. PR01097. TRNSRECEPTRP.
SMART	SM00248. ANK. 2 hits. [Graphical view]
TIGRFAMs	TIGR00870. trp. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	796287.

Entry information

Entry name

TRPL_DROME

Accession

Primary (citable) accession number: P48994
Secondary accession number(s): Q0E9E3 , Q8IH62, Q8MKU9, Q9V5B2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 25, 2002
Last modified:	November 25, 2008
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project