GenomeNet

Database: UniProt
Entry: TRP_DROME
LinkDB: TRP_DROME
Original site: 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   27-SEP-2017, entry version 169.
DE   RecName: Full=Transient receptor potential protein;
GN   Name=trp; ORFNames=CG7875;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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
RT   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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA   George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   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
RT   locus of Drosophila melanogaster.";
RL   Somat. Cell Mol. Genet. 13:661-669(1987).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7751943;
RA   Pollock J.A., Assaf A., Peretz A., Nichols C.D., Mojet M.H.,
RA   Hardie R.C., Minke B.;
RT   "TRP, a protein essential for inositide-mediated Ca2+ influx is
RT   localized adjacent to the calcium stores in Drosophila
RT   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;
RP   NORPA; 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
RT   TRP store-operated channel to a signaling complex.";
RL   Neuron 18:95-105(1997).
RN   [10]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10366618;
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;
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
RT   mutations in the trp gene of Drosophila.";
RL   J. Neurosci. 20:649-659(2000).
RN   [15]
RP   FUNCTION.
RX   PubMed=10908615;
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
RT   TRP Ca2+ channel causes massive degeneration of photoreceptors.";
RL   J. Biol. Chem. 277:33884-33889(2002).
RN   [18]
RP   REVIEW.
RX   PubMed=11707492;
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
CC       C (PLC)-mediated phototransduction. Ca(2+) influx may then feed
CC       back and inhibit PLC, thereby facilitating phosphatidylinositol
CC       4,5 bisphosphate (PIP2) recycling. Trp and trpl act together in
CC       the light response, though it is unclear whether as
CC       heteromultimers or as distinct units, and are activated by fatty
CC       acids and metabolic stress. Also required for olfactory adaptation
CC       and may be involved in olfactory system development.
CC       {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
CC       form the core of the inaD signaling complex. Other members of the
CC       complex include norpA (PLC), inaC (PKC), and possibly trpl, ninaC,
CC       FKBP59, calmodulin and rhodopsin. Forms homomultimers and
CC       heteromultimers with trpl. Interaction with trpl is mediated in
CC       part by the N-terminal region and the transmembrane domains. Also
CC       interacts, though to a lower extent, with Trpgamma.
CC       {ECO:0000269|PubMed:10896160, ECO:0000269|PubMed:10995445,
CC       ECO:0000269|PubMed:9010208, ECO:0000269|PubMed:9215637}.
CC   -!- INTERACTION:
CC       Q24008:inaD; NbExp=6; 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}.
CC       Note=Localized on plasma membrane loops found at the base of the
CC       rhabdomere, in close proximity to the calcium stores.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the rhabdomeres of
CC       photoreceptor cells. Expressed in the third antennal segment and
CC       in the olfactory segment at approximately 70 hours after puparium
CC       formation during antennal development.
CC       {ECO:0000269|PubMed:10366618, ECO:0000269|PubMed:10632594,
CC       ECO:0000269|PubMed:10995445, 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.
CC       STrpC subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ22416.1; Type=Frameshift; Positions=721; Evidence={ECO:0000305};
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   UniGene; Dm.21694; -.
DR   PDB; 5F67; X-ray; 1.76 A; C/D=1259-1275.
DR   PDBsum; 5F67; -.
DR   ProteinModelPortal; P19334; -.
DR   SMR; P19334; -.
DR   BioGrid; 68399; 25.
DR   IntAct; P19334; 5.
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   eggNOG; KOG3609; Eukaryota.
DR   eggNOG; ENOG410XQ0Y; LUCA.
DR   InParanoid; P19334; -.
DR   KO; K04967; -.
DR   OMA; GRMISGW; -.
DR   OrthoDB; EOG091G029I; -.
DR   PhylomeDB; P19334; -.
DR   Reactome; R-DME-3295583; TRP channels.
DR   SignaLink; P19334; -.
DR   ChiTaRS; trp; fly.
DR   GenomeRNAi; 43542; -.
DR   PRO; PR:P19334; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003861; -.
DR   ExpressionAtlas; P19334; 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:0005622; C:intracellular; IEA:GOC.
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:0015278; F:calcium-release channel activity; NAS:FlyBase.
DR   GO; GO:0005516; F:calmodulin binding; TAS:FlyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:FlyBase.
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; TAS:FlyBase.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IMP:FlyBase.
DR   GO; GO:0006816; P:calcium ion transport; IMP:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; TAS:FlyBase.
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: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:0030845; P:phospholipase C-inhibiting G-protein coupled receptor signaling pathway; IMP:FlyBase.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
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:0046154; P:rhodopsin metabolic process; 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   CDD; cd00204; ANK; 1.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR004729; TRP_channel.
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   TIGRFAMs; TIGR00870; trp; 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; Complete proteome; Ion channel;
KW   Ion transport; Membrane; Olfaction; Reference proteome; Repeat;
KW   Sensory transduction; Transmembrane; Transmembrane helix; Transport;
KW   Vision.
FT   CHAIN         1   1275       Transient receptor potential protein.
FT                                /FTId=PRO_0000215357.
FT   TOPO_DOM      1    366       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    367    387       Helical. {ECO:0000255}.
FT   TOPO_DOM    388    418       Extracellular. {ECO:0000255}.
FT   TRANSMEM    419    439       Helical. {ECO:0000255}.
FT   TOPO_DOM    440    450       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    451    471       Helical. {ECO:0000255}.
FT   TOPO_DOM    472    541       Extracellular. {ECO:0000255}.
FT   TRANSMEM    542    562       Helical. {ECO:0000255}.
FT   TOPO_DOM    563    609       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    610    630       Helical. {ECO:0000255}.
FT   TOPO_DOM    631    637       Extracellular. {ECO:0000255}.
FT   TRANSMEM    638    658       Helical. {ECO:0000255}.
FT   TOPO_DOM    659   1275       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       69     98       ANK 1.
FT   REPEAT      143    172       ANK 2.
FT   COMPBIAS   1161   1236       Asp-rich.
FT   MUTAGEN     500    500       P->T: In P365; photoreceptors respond
FT                                normally to light.
FT                                {ECO:0000269|PubMed:10632594,
FT                                ECO:0000269|PubMed:12107168}.
FT   MUTAGEN     531    531       H->N: In P365; photoreceptors respond
FT                                normally to light.
FT                                {ECO:0000269|PubMed:10632594,
FT                                ECO:0000269|PubMed:12107168}.
FT   MUTAGEN     550    550       F->I: In P365; defective in the response
FT                                to light due to rapid degeneration of
FT                                photoreceptors.
FT                                {ECO:0000269|PubMed:10632594,
FT                                ECO:0000269|PubMed:12107168}.
FT   MUTAGEN     867    867       S->F: In P365; photoreceptors respond
FT                                normally to light.
FT                                {ECO:0000269|PubMed:10632594,
FT                                ECO:0000269|PubMed:12107168}.
FT   MUTAGEN    1266   1266       V->D: Does not disrupt inaD binding.
FT                                {ECO:0000269|PubMed:10995445}.
FT   CONFLICT    188    188       M -> T (in Ref. 1 and 2). {ECO:0000305}.
FT   CONFLICT    222    222       A -> V (in Ref. 1; AAA28976).
FT                                {ECO:0000305}.
FT   CONFLICT    237    237       S -> T (in Ref. 5; AAQ22416).
FT                                {ECO:0000305}.
FT   CONFLICT    261    261       A -> T (in Ref. 5; AAQ22416).
FT                                {ECO:0000305}.
FT   CONFLICT    285    288       GQRQ -> ASSE (in Ref. 2; AAA56928).
FT                                {ECO:0000305}.
FT   CONFLICT    326    329       RRKQ -> PQE (in Ref. 2; AAA56928).
FT                                {ECO:0000305}.
FT   CONFLICT    365    374       KPFVKFITHS -> NPLSSSSRTP (in Ref. 2;
FT                                AAA56928). {ECO:0000305}.
FT   CONFLICT    785    785       N -> S (in Ref. 1; AAA28976).
FT                                {ECO:0000305}.
FT   CONFLICT   1008   1008       A -> P (in Ref. 1 and 2). {ECO:0000305}.
FT   CONFLICT   1197   1197       K -> R (in Ref. 5). {ECO:0000305}.
FT   STRAND     1262   1264       {ECO:0000244|PDB:5F67}.
FT   TURN       1265   1267       {ECO:0000244|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
//
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