TRP_DROME
ID TRP_DROME Reviewed; 1275 AA.
AC P19334; Q7YU76; Q9VAE1;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Transient receptor potential protein;
GN Name=trp; ORFNames=CG7875;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=2516726; DOI=10.1016/0896-6273(89)90069-x;
RA Montell C., Rubin G.M.;
RT "Molecular characterization of the Drosophila trp locus: a putative
RT integral membrane protein required for phototransduction.";
RL Neuron 2:1313-1323(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2482778; DOI=10.1016/0896-6273(89)90117-7;
RA Wong F., Schaefer E.L., Roop B.C., Lamendola J.N., Johnson-Seaton D.,
RA Shao D.;
RT "Proper function of the Drosophila trp gene product during pupal
RT development is important for normal visual transduction in the adult.";
RL Neuron 3:81-94(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1126-1275.
RX PubMed=3118483; DOI=10.1007/bf01534486;
RA Wong F., Yuh Z.T., Schaefer E.L., Roop B.C., Ally A.H.;
RT "Overlapping transcription units in the transient receptor potential locus
RT of Drosophila melanogaster.";
RL Somat. Cell Mol. Genet. 13:661-669(1987).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=7751943; DOI=10.1523/jneurosci.15-05-03747.1995;
RA Pollock J.A., Assaf A., Peretz A., Nichols C.D., Mojet M.H., Hardie R.C.,
RA Minke B.;
RT "TRP, a protein essential for inositide-mediated Ca2+ influx is localized
RT adjacent to the calcium stores in Drosophila photoreceptors.";
RL J. Neurosci. 15:3747-3760(1995).
RN [8]
RP HOMOMULTIMERIZATION, AND INTERACTION WITH TRPL.
RX PubMed=9215637; DOI=10.1016/s0092-8674(00)80302-5;
RA Xu X.-Z.S., Li H.-S., Guggino W.B., Montell C.;
RT "Coassembly of TRP and TRPL produces a distinct store-operated
RT conductance.";
RL Cell 89:1155-1164(1997).
RN [9]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH INAD; NORPA;
RP RHODOPSIN AND CALMODULIN.
RX PubMed=9010208; DOI=10.1016/s0896-6273(01)80049-0;
RA Chevesich J., Kreuz A.J., Montell C.;
RT "Requirement for the PDZ domain protein, INAD, for localization of the TRP
RT store-operated channel to a signaling complex.";
RL Neuron 18:95-105(1997).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10366618; DOI=10.1523/jneurosci.19-12-04839.1999;
RA Stortkuhl K.F., Hovemann B.T., Carlson J.R.;
RT "Olfactory adaptation depends on the Trp Ca2+ channel in Drosophila.";
RL J. Neurosci. 19:4839-4846(1999).
RN [11]
RP FUNCTION.
RX PubMed=9930700; DOI=10.1038/16703;
RA Chyb S., Raghu P., Hardie R.C.;
RT "Polyunsaturated fatty acids activate the Drosophila light-sensitive
RT channels TRP and TRPL.";
RL Nature 397:255-259(1999).
RN [12]
RP PHOSPHORYLATION.
RX PubMed=10766855; DOI=10.1074/jbc.275.16.12194;
RA Liu M., Parker L.L., Wadzinski B.E., Shieh B.-H.;
RT "Reversible phosphorylation of the signal transduction complex in
RT Drosophila photoreceptors.";
RL J. Biol. Chem. 275:12194-12199(2000).
RN [13]
RP INTERACTION WITH INAD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF VAL-1266.
RX PubMed=10995445; DOI=10.1083/jcb.150.6.1411;
RA Li H.-S., Montell C.;
RT "TRP and the PDZ protein, INAD, form the core complex required for
RT retention of the signalplex in Drosophila photoreceptor cells.";
RL J. Cell Biol. 150:1411-1422(2000).
RN [14]
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-500; HIS-531; PHE-550 AND
RP SER-867.
RX PubMed=10632594; DOI=10.1523/jneurosci.20-02-00649.2000;
RA Yoon J., Ben-Ami H.C., Hong Y.S., Park S., Strong L.L.R., Bowman J.D.,
RA Geng C., Baek K., Minke B., Pak W.L.;
RT "Novel mechanism of massive photoreceptor degeneration caused by mutations
RT in the trp gene of Drosophila.";
RL J. Neurosci. 20:649-659(2000).
RN [15]
RP FUNCTION.
RX PubMed=10908615; DOI=10.1523/jneurosci.20-15-05748.2000;
RA Agam K., von Campenhausen M., Levy S., Ben-Ami H.C., Cook B.,
RA Kirschfeld K., Minke B.;
RT "Metabolic stress reversibly activates the Drosophila light-sensitive
RT channels TRP and TRPL in vivo.";
RL J. Neurosci. 20:5748-5755(2000).
RN [16]
RP INTERACTION WITH TRPGAMMA.
RX PubMed=10896160; DOI=10.1016/s0896-6273(00)81201-5;
RA Xu X.-Z.S., Chien F., Butler A., Salkoff L., Montell C.;
RT "TRPgamma, a Drosophila TRP-related subunit, forms a regulated cation
RT channel with TRPL.";
RL Neuron 26:647-657(2000).
RN [17]
RP MUTAGENESIS OF PRO-500; HIS-531; PHE-550 AND SER-867.
RX PubMed=12107168; DOI=10.1074/jbc.m204075200;
RA Hong Y.S., Park S., Geng C., Baek K., Bowman J.D., Yoon J., Pak W.L.;
RT "Single amino acid change in the fifth transmembrane segment of the TRP
RT Ca2+ channel causes massive degeneration of photoreceptors.";
RL J. Biol. Chem. 277:33884-33889(2002).
RN [18]
RP REVIEW.
RX PubMed=11707492; DOI=10.1242/jeb.204.20.3403;
RA Hardie R.C.;
RT "Phototransduction in Drosophila melanogaster.";
RL J. Exp. Biol. 204:3403-3409(2001).
CC -!- FUNCTION: A light-sensitive calcium channel that is required for
CC inositide-mediated Ca(2+) entry in the retina during phospholipase C
CC (PLC)-mediated phototransduction. Ca(2+) influx may then feed back and
CC inhibit PLC, thereby facilitating phosphatidylinositol 4,5 bisphosphate
CC (PIP2) recycling. Trp and trpl act together in the light response,
CC though it is unclear whether as heteromultimers or as distinct units,
CC and are activated by fatty acids and metabolic stress. Also required
CC for olfactory adaptation and may be involved in olfactory system
CC development. {ECO:0000269|PubMed:10366618, ECO:0000269|PubMed:10908615,
CC ECO:0000269|PubMed:2482778, ECO:0000269|PubMed:2516726,
CC ECO:0000269|PubMed:9930700}.
CC -!- SUBUNIT: The C-terminus interacts with a PDZ domain of inaD to form the
CC core of the inaD signaling complex. Other members of the complex
CC include norpA (PLC), inaC (PKC), and possibly trpl, ninaC, Fkbp59,
CC calmodulin and rhodopsin. Forms homomultimers and heteromultimers with
CC trpl. Interaction with trpl is mediated in part by the N-terminal
CC region and the transmembrane domains. Also interacts, though to a lower
CC extent, with Trpgamma. {ECO:0000269|PubMed:10896160,
CC ECO:0000269|PubMed:10995445, ECO:0000269|PubMed:9010208,
CC ECO:0000269|PubMed:9215637}.
CC -!- INTERACTION:
CC P19334; Q24008: inaD; NbExp=10; IntAct=EBI-165136, EBI-195326;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10995445,
CC ECO:0000305|PubMed:2516726, ECO:0000305|PubMed:7751943,
CC ECO:0000305|PubMed:9010208}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:10995445, ECO:0000305|PubMed:2516726,
CC ECO:0000305|PubMed:7751943, ECO:0000305|PubMed:9010208}. Note=Localized
CC on plasma membrane loops found at the base of the rhabdomere, in close
CC proximity to the calcium stores.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the rhabdomeres of
CC photoreceptor cells. Expressed in the third antennal segment and in the
CC olfactory segment at approximately 70 hours after puparium formation
CC during antennal development. {ECO:0000269|PubMed:10366618,
CC ECO:0000269|PubMed:10632594, ECO:0000269|PubMed:10995445,
CC ECO:0000269|PubMed:2516726}.
CC -!- PTM: Phosphorylated by inaC. {ECO:0000269|PubMed:10766855}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ22416.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M34394; AAA28976.1; -; Genomic_DNA.
DR EMBL; M21306; AAA56928.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56970.1; -; Genomic_DNA.
DR EMBL; BT009947; AAQ22416.1; ALT_FRAME; mRNA.
DR EMBL; M18634; AAA28977.1; -; Genomic_DNA.
DR PIR; JN0015; JN0015.
DR PIR; JU0092; JU0092.
DR RefSeq; NP_476768.1; NM_057420.4.
DR PDB; 5F67; X-ray; 1.76 A; C/D=1259-1275.
DR PDB; 7CQH; X-ray; 2.15 A; A=899-940.
DR PDB; 7CQV; X-ray; 1.78 A; B=783-862.
DR PDBsum; 5F67; -.
DR PDBsum; 7CQH; -.
DR PDBsum; 7CQV; -.
DR AlphaFoldDB; P19334; -.
DR SMR; P19334; -.
DR BioGRID; 68399; 25.
DR IntAct; P19334; 6.
DR STRING; 7227.FBpp0084879; -.
DR TCDB; 1.A.4.1.1; the transient receptor potential ca(2+) channel (trp-cc) family.
DR PaxDb; P19334; -.
DR PRIDE; P19334; -.
DR EnsemblMetazoa; FBtr0085513; FBpp0084879; FBgn0003861.
DR GeneID; 43542; -.
DR KEGG; dme:Dmel_CG7875; -.
DR CTD; 43542; -.
DR FlyBase; FBgn0003861; trp.
DR VEuPathDB; VectorBase:FBgn0003861; -.
DR eggNOG; KOG3609; Eukaryota.
DR HOGENOM; CLU_005716_0_0_1; -.
DR InParanoid; P19334; -.
DR OMA; NEGLQMD; -.
DR PhylomeDB; P19334; -.
DR Reactome; R-DME-3295583; TRP channels.
DR Reactome; R-DME-5578775; Ion homeostasis.
DR Reactome; R-DME-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 43542; 0 hits in 3 CRISPR screens.
DR ChiTaRS; trp; fly.
DR GenomeRNAi; 43542; -.
DR PRO; PR:P19334; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003861; Expressed in head capsule and 9 other tissues.
DR ExpressionAtlas; P19334; baseline and differential.
DR Genevisible; P19334; DM.
DR GO; GO:0034703; C:cation channel complex; IPI:FlyBase.
DR GO; GO:0016027; C:inaD signaling complex; IPI:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016028; C:rhabdomere; IDA:UniProtKB.
DR GO; GO:0035997; C:rhabdomere microvillus membrane; IDA:FlyBase.
DR GO; GO:0005262; F:calcium channel activity; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:FlyBase.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0010461; F:light-activated ion channel activity; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:FlyBase.
DR GO; GO:0006816; P:calcium ion transport; IMP:UniProtKB.
DR GO; GO:0071454; P:cellular response to anoxia; IGI:FlyBase.
DR GO; GO:0050962; P:detection of light stimulus involved in sensory perception; IMP:FlyBase.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:UniProtKB.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:FlyBase.
DR GO; GO:0008377; P:light-induced release of internally sequestered calcium ion; IDA:FlyBase.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR GO; GO:0007603; P:phototransduction, visible light; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0009416; P:response to light stimulus; IMP:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:FlyBase.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013555; TRP_dom.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell membrane; Ion channel; Ion transport; Membrane;
KW Olfaction; Reference proteome; Repeat; Sensory transduction; Transmembrane;
KW Transmembrane helix; Transport; Vision.
FT CHAIN 1..1275
FT /note="Transient receptor potential protein"
FT /id="PRO_0000215357"
FT TOPO_DOM 1..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..418
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..541
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..637
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..1275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 69..98
FT /note="ANK 1"
FT REPEAT 143..172
FT /note="ANK 2"
FT REGION 933..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 500
FT /note="P->T: In P365; photoreceptors respond normally to
FT light."
FT /evidence="ECO:0000269|PubMed:10632594,
FT ECO:0000269|PubMed:12107168"
FT MUTAGEN 531
FT /note="H->N: In P365; photoreceptors respond normally to
FT light."
FT /evidence="ECO:0000269|PubMed:10632594,
FT ECO:0000269|PubMed:12107168"
FT MUTAGEN 550
FT /note="F->I: In P365; defective in the response to light
FT due to rapid degeneration of photoreceptors."
FT /evidence="ECO:0000269|PubMed:10632594,
FT ECO:0000269|PubMed:12107168"
FT MUTAGEN 867
FT /note="S->F: In P365; photoreceptors respond normally to
FT light."
FT /evidence="ECO:0000269|PubMed:10632594,
FT ECO:0000269|PubMed:12107168"
FT MUTAGEN 1266
FT /note="V->D: Does not disrupt inaD binding."
FT /evidence="ECO:0000269|PubMed:10995445"
FT CONFLICT 188
FT /note="M -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="A -> V (in Ref. 1; AAA28976)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="S -> T (in Ref. 5; AAQ22416)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="A -> T (in Ref. 5; AAQ22416)"
FT /evidence="ECO:0000305"
FT CONFLICT 285..288
FT /note="GQRQ -> ASSE (in Ref. 2; AAA56928)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..329
FT /note="RRKQ -> PQE (in Ref. 2; AAA56928)"
FT /evidence="ECO:0000305"
FT CONFLICT 365..374
FT /note="KPFVKFITHS -> NPLSSSSRTP (in Ref. 2; AAA56928)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="N -> S (in Ref. 1; AAA28976)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="A -> P (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1197
FT /note="K -> R (in Ref. 5)"
FT /evidence="ECO:0000305"
FT HELIX 802..813
FT /evidence="ECO:0007829|PDB:7CQV"
FT HELIX 817..826
FT /evidence="ECO:0007829|PDB:7CQV"
FT HELIX 836..844
FT /evidence="ECO:0007829|PDB:7CQV"
FT HELIX 917..925
FT /evidence="ECO:0007829|PDB:7CQH"
FT HELIX 927..935
FT /evidence="ECO:0007829|PDB:7CQH"
FT STRAND 1262..1264
FT /evidence="ECO:0007829|PDB:5F67"
FT TURN 1265..1267
FT /evidence="ECO:0007829|PDB:5F67"
SQ SEQUENCE 1275 AA; 142594 MW; 4376C1B853868B4C CRC64;
MGSNTESDAE KALGSRLDYD LMMAEEYILS DVEKNFILSC ERGDLPGVKK ILEEYQGTDK
FNINCTDPMN RSALISAIEN ENFDLMVILL EHNIEVGDAL LHAISEEYVE AVEELLQWEE
TNHKEGQPYS WEAVDRSKST FTVDITPLIL AAHRNNYEIL KILLDRGATL PMPHDVKCGC
DECVTSQMTD SLRHSQSRIN AYRALSASSL IALSSRDPVL TAFQLSWELK RLQAMESEFR
AEYTEMRQMV QDFGTSLLDH ARTSMELEVM LNFNHEPSHD IWCLGQRQTL ERLKLAIRYK
QKTFVAHPNV QQLLAAIWYD GLPGFRRKQA SQQLMDVVKL GCSFPIYSLK YILAPDSEGA
KFMRKPFVKF ITHSCSYMFF LMLLGAASLR VVQITFELLA FPWMLTMLED WRKHERGSLP
GPIELAIITY IMALIFEELK SLYSDGLFEY IMDLWNIVDY ISNMFYVTWI LCRATAWVIV
HRDLWFRGID PYFPREHWHP FDPMLLSEGA FAAGMVFSYL KLVHIFSINP HLGPLQVSLG
RMIIDIIKFF FIYTLVLFAF GCGLNQLLWY YAELEKNKCY HLHPDVADFD DQEKACTIWR
RFSNLFETSQ SLFWASFGLV DLVSFDLAGI KSFTRFWALL MFGSYSVINI IVLLNMLIAM
MSNSYQIISE RADTEWKFAR SQLWMSYFED GGTIPPPFNL CPNMKMLRKT LGRKRPSRTK
SFMRKSMERA QTLHDKVMKL LVRRYITAEQ RRRDDYGITE DDIIEVRQDI SSLRFELLEI
FTNNNWDVPD IEKKSQGVAR TTKGKVMERR ILKDFQIGFV ENLKQEMSES ESGRDIFSSL
AKVIGRKKTQ KGDKDWNAIA RKNTFASDPI GSKRSSMQRH SQRSLRRKII EQANEGLQMN
QTQLIEFNPN LGDVTRATRV AYVKFMRKKM AADEVSLADD EGAPNGEGEK KPLDASGSKK
SITSGGTGGG ASMLAAAALR ASVKNVDEKS GADGKPGTMG KPTDDKKAGD DKDKQQPPKD
SKPSAGGPKP GDQKPTPGAG APKPQAAGTI SKPGESQKKD APAPPTKPGD TKPAAPKPGE
SAKPEAAAKK EESSKTEASK PAATNGAAKS AAPSAPSDAK PDSKLKPGAA GAPEATKATN
GASKPDEKKS GPEEPKKAAG DSKPGDDAKD KDKKPGDDKD KKPGDDKDKK PADNNDKKPA
DDKDKKPGDD KDKKPGDDKD KKPSDDKDKK PADDKDKKPA AAPLKPAIKV GQSSAAAGGE
RGKSTVTGRM ISGWL
