WHITE_DROME
ID WHITE_DROME Reviewed; 687 AA.
AC P10090; Q9V3A2; Q9XY33;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Protein white;
DE EC=7.6.2.- {ECO:0000305|PubMed:117796, ECO:0000305|PubMed:18310115, ECO:0000305|PubMed:33820991, ECO:0000305|PubMed:6788034, ECO:0000305|PubMed:812484};
DE EC=7.6.2.6 {ECO:0000305|PubMed:117796};
DE AltName: Full=ATP-binding cassette transporter sub-family G member white {ECO:0000303|PubMed:33820991};
DE AltName: Full=Broad substrate specificity ATP-binding cassette transporter white {ECO:0000305};
GN Name=w {ECO:0000312|FlyBase:FBgn0003996};
GN ORFNames=CG2759 {ECO:0000312|FlyBase:FBgn0003996};
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 [MRNA].
RC TISSUE=Head;
RX PubMed=2109311; DOI=10.1093/nar/18.6.1633;
RA Pepling M., Mount S.M.;
RT "Sequence of a cDNA from the Drosophila melanogaster white gene.";
RL Nucleic Acids Res. 18:1633-1633(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6084717; DOI=10.1016/0022-2836(84)90021-4;
RA O'Hare K., Murphy C., Levis R., Rubin G.M.;
RT "DNA sequence of the white locus of Drosophila melanogaster.";
RL J. Mol. Biol. 180:437-455(1984).
RN [3]
RP SEQUENCE REVISION TO 25-29 AND 616.
RA O'Hare K.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11156992; DOI=10.1093/genetics/157.2.727;
RA Lukacsovich T., Asztalos Z., Awano W., Baba K., Kondo S., Niwa S.,
RA Yamamoto D.;
RT "Dual-tagging gene trap of novel genes in Drosophila melanogaster.";
RL Genetics 157:727-742(2001).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-331.
RX PubMed=2503416; DOI=10.1093/genetics/122.3.595;
RA Tearle R.G., Belote J.M., McKeown M., Baker B.S., Howells A.J.;
RT "Cloning and characterization of the scarlet gene of Drosophila
RT melanogaster.";
RL Genetics 122:595-606(1989).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=812484; DOI=10.1007/bf00484918;
RA Sullivan D.T., Sullivan M.C.;
RT "Transport defects as the physiological basis for eye color mutants of
RT Drosophila melanogaster.";
RL Biochem. Genet. 13:603-613(1975).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=117796; DOI=10.1007/bf00498891;
RA Sullivan D.T., Bell L.A., Paton D.R., Sullivan M.C.;
RT "Purine transport by malpighian tubules of pteridine-deficient eye color
RT mutants of Drosophila melanogaster.";
RL Biochem. Genet. 17:565-573(1979).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=6788034; DOI=10.1007/bf00484342;
RA Sullivan D.T., Bell L.A., Paton D.R., Sullivan M.C.;
RT "Genetic and functional analysis of tryptophan transport in Malpighian
RT tubules of Drosophila.";
RL Biochem. Genet. 18:1109-1130(1980).
RN [12]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ILE-581 AND GLY-588.
RX PubMed=8144619; DOI=10.1016/s0021-9258(17)34070-x;
RA Ewart G.D., Cannell D., Cox G.B., Howells A.J.;
RT "Mutational analysis of the traffic ATPase (ABC) transporters involved in
RT uptake of eye pigment precursors in Drosophila melanogaster. Implications
RT for structure-function relationships.";
RL J. Biol. Chem. 269:10370-10377(1994).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF LEU-49; HIS-298; GLY-509; GLY-589 AND PHE-590.
RX PubMed=10407069; DOI=10.1016/s0005-2736(99)00064-4;
RA Mackenzie S.M., Brooker M.R., Gill T.R., Cox G.B., Howells A.J.,
RA Ewart G.D.;
RT "Mutations in the white gene of Drosophila melanogaster affecting ABC
RT transporters that determine eye colouration.";
RL Biochim. Biophys. Acta 1419:173-185(1999).
RN [14]
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11294610; DOI=10.1023/a:1004115718597;
RA Mackenzie S.M., Howells A.J., Cox G.B., Ewart G.D.;
RT "Sub-cellular localisation of the white/scarlet ABC transporter to pigment
RT granule membranes within the compound eye of Drosophila melanogaster.";
RL Genetica 108:239-252(2000).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18310115; DOI=10.1242/jeb.014837;
RA Evans J.M., Day J.P., Cabrero P., Dow J.A., Davies S.A.;
RT "A new role for a classical gene: white transports cyclic GMP.";
RL J. Exp. Biol. 211:890-899(2008).
RN [16]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18931318; DOI=10.1242/jeb.021162;
RA Borycz J., Borycz J.A., Kubow A., Lloyd V., Meinertzhagen I.A.;
RT "Drosophila ABC transporter mutants white, brown and scarlet have altered
RT contents and distribution of biogenic amines in the brain.";
RL J. Exp. Biol. 211:3454-3466(2008).
RN [17]
RP DISRUPTION PHENOTYPE.
RX PubMed=27029736; DOI=10.1534/genetics.115.185066;
RA Xiao C., Robertson R.M.;
RT "Timing of Locomotor Recovery from Anoxia Modulated by the white Gene in
RT Drosophila.";
RL Genetics 203:787-797(2016).
RN [18]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-49 AND GLY-589.
RX PubMed=28794482; DOI=10.1038/s41598-017-08155-y;
RA Xiao C., Qiu S., Robertson R.M.;
RT "The white gene controls copulation success in Drosophila melanogaster.";
RL Sci. Rep. 7:7712-7712(2017).
RN [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29367274; DOI=10.1242/jeb.168419;
RA Tejeda-Guzman C., Rosas-Arellano A., Kroll T., Webb S.M.,
RA Barajas-Aceves M., Osorio B., Missirlis F.;
RT "Biogenesis of zinc storage granules in Drosophila melanogaster.";
RL J. Exp. Biol. 221:0-0(2018).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33820991; DOI=10.1038/s42255-021-00375-x;
RA Sasaki A., Nishimura T., Takano T., Naito S., Yoo S.K.;
RT "white regulates proliferative homeostasis of intestinal stem cells during
RT ageing in Drosophila.";
RL Nat. Metab. 3:546-557(2021).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family which transports various molecules including bioamines,
CC neurotransmitters, metabolic intermediates and second messengers
CC (PubMed:812484, PubMed:117796, PubMed:6788034, PubMed:10407069,
CC PubMed:18310115, PubMed:18931318, PubMed:33820991). In the eye,
CC required for the transport of the eye red and brown pigment precursors,
CC guanine and tryptophan, into pigment cell granules (PubMed:10407069,
CC PubMed:8144619). Probably in association with bw/brown, involved in the
CC transport of guanine (PubMed:117796). Probably in association with
CC st/scarlet involved in the transport of kynurenine and probably
CC tryptophan (PubMed:812484). Involved in the transport of kynurenine in
CC pupal eyes (PubMed:812484). May play a role in histamine uptake by the
CC lamina epithelial glia which surrounds photoreceptors R1-R6
CC (PubMed:18931318). In Malpighian tubules, involved in the transport of
CC cGMP, guanine, xanthine, riboflavin, kynurenine and tryptophan
CC (PubMed:812484, PubMed:117796, PubMed:6788034, PubMed:18310115).
CC Probably in association with br/brown, involved in aging-induced
CC intestinal stem cell proliferation in the midgut by regulating
CC tetrahydrofolate transport (PubMed:33820991). Probably in association
CC with st/scarlet, plays a role in zinc storage granule biogenesis in
CC Malpighian tubule principal epithelial cells (PubMed:29367274).
CC {ECO:0000269|PubMed:10407069, ECO:0000269|PubMed:117796,
CC ECO:0000269|PubMed:18310115, ECO:0000269|PubMed:18931318,
CC ECO:0000269|PubMed:29367274, ECO:0000269|PubMed:33820991,
CC ECO:0000269|PubMed:6788034, ECO:0000269|PubMed:812484,
CC ECO:0000269|PubMed:8144619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP
CC + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57746, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:18310115};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + guanine(out) + H2O = ADP + guanine(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:20832, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16235, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.6.2.6;
CC Evidence={ECO:0000305|PubMed:117796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate +
CC riboflavin(out); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57986, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:117796, ECO:0000305|PubMed:33820991};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate(out) + ATP + H2O = (6S)-5,6,7,8-
CC tetrahydrofolate(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:68592,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57453, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:33820991};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-tryptophan(out) = ADP + H(+) + L-tryptophan(in)
CC + phosphate; Xref=Rhea:RHEA:68584, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:6788034, ECO:0000269|PubMed:812484,
CC ECO:0000305|PubMed:33820991};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-kynurenine(out) = ADP + H(+) + L-kynurenine(in)
CC + phosphate; Xref=Rhea:RHEA:68580, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57959, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:33820991, ECO:0000305|PubMed:812484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xanthine(out) = ADP + H(+) + phosphate +
CC xanthine(in); Xref=Rhea:RHEA:68576, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17712, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:117796, ECO:0000305|PubMed:33820991};
CC -!- SUBUNIT: May form a heterodimer with bw/brown (Probable). May form a
CC heterodimer with st/scarlet (Probable). {ECO:0000305|PubMed:11294610,
CC ECO:0000305|PubMed:18931318, ECO:0000305|PubMed:8144619}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:11294610, ECO:0000269|PubMed:33820991}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Co-localizes with st/scarlet to
CC pigment granules within pigment cells and retinula cells of the
CC compound eye. {ECO:0000269|PubMed:11294610}.
CC -!- TISSUE SPECIFICITY: Expressed in the head (at protein level)
CC (PubMed:11294610). Expressed in the eye, specifically in retina primary
CC pigment cells, in the basement membrane of the base of secondary and
CC tertiary pigment cells, and in retinula cells (at protein level)
CC (PubMed:18931318, PubMed:11294610). Expressed in the retina underlying
CC lamina in the epithelial glia that surrounds the array of lamina
CC cartridges (at protein level) (PubMed:18931318). Weakly expressed in
CC photoreceptors, specifically in terminals of R1-R6, R7 and R8 (at
CC protein level) (PubMed:18931318). Expressed at very low levels in
CC medulla and central brain (at protein level) (PubMed:18931318).
CC Expressed in principal cells of the Malpighian tubules
CC (PubMed:33820991). {ECO:0000269|PubMed:11294610,
CC ECO:0000269|PubMed:18931318, ECO:0000269|PubMed:33820991}.
CC -!- INDUCTION: Up-regulated during aging in intestinal stem cells.
CC {ECO:0000269|PubMed:33820991}.
CC -!- DISRUPTION PHENOTYPE: Eyes are white due to a defect in color pigment
CC production (PubMed:18310115, PubMed:33820991). Malpighian tubules
CC appear clear or white (PubMed:18310115, PubMed:29367274). Loss of
CC st/scarlet protein in the pigment cells and retinula cells of the
CC compound eye (PubMed:11294610). Transport of cGMP, but not cAMP, is
CC inhibited in Malpighian tubules; however, basal fluid transport rates
CC or rates stimulated by cGMP in the tubules are normal
CC (PubMed:18310115). In Malpighian tubules, uptake of guanine, xanthine
CC and riboflavin is impaired while uptake of hypoxanthine, guanosine and
CC adenine is not affected (PubMed:117796). In Malpighian tubules,
CC kynurenine and tryptophan uptake is impaired; however, incorporation of
CC tryptophan into proteins is not affected (PubMed:6788034,
CC PubMed:812484). In pupal eyes, kynurenine uptake is impaired
CC (PubMed:812484). In the head, 50% reduction in histamine levels, 60%
CC reduction in dopamine levels and 32% reduction in serotonin (5-HT)
CC levels (PubMed:18931318). Specifically, histamine levels are reduced in
CC the retina, the retina lamina and the central brain (PubMed:18931318).
CC In addition, in lamina photoreceptor terminals R1-R6, numbers of
CC synaptic vesicles and capitate projections, which are sites of
CC endocytosis of vesicle membrane, are reduced (PubMed:18931318). In
CC young and old flies, reduces the levels of several metabolites,
CC including tryptophan, kynurenine, kynurenic acid, 3-hydroxykynurenine,
CC guanosine, xanthine, riboflavin and tetrahydrofolate, and increases the
CC levels of guanine (PubMed:33820991). Inhibits aging-induced intestinal
CC stem cell proliferation (PubMed:33820991). 3-fold reduction in
CC Malpighian tubule zinc stores (PubMed:29367274). Severe reduction of
CC copulation success and reduced courting activities in males
CC (PubMed:28794482). RNAi-mediated knockdown in central nervous system
CC causes a delay in locomotor recovery from anoxia with no effect on eye
CC pigmentation (PubMed:27029736). RNAi-mediated knockdown in serotonergic
CC neurons, causes a delay in locomotor recovery from anoxia
CC (PubMed:27029736). {ECO:0000269|PubMed:11294610,
CC ECO:0000269|PubMed:117796, ECO:0000269|PubMed:18310115,
CC ECO:0000269|PubMed:18931318, ECO:0000269|PubMed:27029736,
CC ECO:0000269|PubMed:28794482, ECO:0000269|PubMed:29367274,
CC ECO:0000269|PubMed:33820991, ECO:0000269|PubMed:6788034,
CC ECO:0000269|PubMed:812484}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; X51749; CAA36038.1; -; mRNA.
DR EMBL; X02974; CAA26716.2; -; Genomic_DNA.
DR EMBL; AB028139; BAA78210.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45826.1; -; Genomic_DNA.
DR EMBL; AL133506; CAB65847.1; -; Genomic_DNA.
DR EMBL; X76202; CAA53795.1; -; Genomic_DNA.
DR PIR; S08635; FYFFW.
DR RefSeq; NP_476787.1; NM_057439.2.
DR AlphaFoldDB; P10090; -.
DR SMR; P10090; -.
DR BioGRID; 57802; 80.
DR DIP; DIP-388N; -.
DR IntAct; P10090; 1.
DR STRING; 7227.FBpp0070468; -.
DR TCDB; 3.A.1.204.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P10090; -.
DR PRIDE; P10090; -.
DR EnsemblMetazoa; FBtr0070490; FBpp0070468; FBgn0003996.
DR GeneID; 31271; -.
DR KEGG; dme:Dmel_CG2759; -.
DR CTD; 31271; -.
DR FlyBase; FBgn0003996; w.
DR VEuPathDB; VectorBase:FBgn0003996; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000167029; -.
DR HOGENOM; CLU_000604_57_6_1; -.
DR InParanoid; P10090; -.
DR PhylomeDB; P10090; -.
DR Reactome; R-DME-1369062; ABC transporters in lipid homeostasis.
DR SignaLink; P10090; -.
DR BioGRID-ORCS; 31271; 0 hits in 1 CRISPR screen.
DR ChiTaRS; w; fly.
DR GenomeRNAi; 31271; -.
DR PRO; PR:P10090; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003996; Expressed in Malpighian tubule and 11 other tissues.
DR ExpressionAtlas; P10090; baseline and differential.
DR Genevisible; P10090; DM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0090740; C:integral component of pigment granule membrane; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0048770; C:pigment granule; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:1905948; F:ABC-type 3',5'-cyclic GMP transmembrane transporter activity; IMP:FlyBase.
DR GO; GO:0008558; F:ABC-type guanine transporter activity; IMP:FlyBase.
DR GO; GO:0005275; F:amine transmembrane transporter activity; IMP:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015208; F:guanine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015196; F:L-tryptophan transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0042907; F:xanthine transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IMP:FlyBase.
DR GO; GO:0042401; P:cellular biogenic amine biosynthetic process; IMP:FlyBase.
DR GO; GO:0070731; P:cGMP transport; IMP:FlyBase.
DR GO; GO:0048072; P:compound eye pigmentation; IMP:FlyBase.
DR GO; GO:0042441; P:eye pigment metabolic process; TAS:FlyBase.
DR GO; GO:0006856; P:eye pigment precursor transport; IEP:FlyBase.
DR GO; GO:0042332; P:gravitaxis; IMP:FlyBase.
DR GO; GO:0015854; P:guanine transport; IMP:UniProtKB.
DR GO; GO:0051615; P:histamine uptake; IGI:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0007613; P:memory; IMP:FlyBase.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
DR GO; GO:0032218; P:riboflavin transport; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015827; P:tryptophan transport; IMP:UniProtKB.
DR GO; GO:0042906; P:xanthine transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005284; Pigment_permease/Abcg.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00955; 3a01204; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Nucleotide-binding; Pigment; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..687
FT /note="Protein white"
FT /id="PRO_0000093382"
FT TOPO_DOM 1..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..460
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 461..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..531
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 569..589
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 590..644
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 93..341
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130..137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 49
FT /note="L->R: In cf; 70% decrease in drosopterin (eye red
FT pigment) levels, 36% decrease in xanthommatin (eye brown
FT pigment) levels and severe defect of copulation success;
FT when associated with E-589."
FT /evidence="ECO:0000269|PubMed:10407069,
FT ECO:0000269|PubMed:28794482"
FT MUTAGEN 298
FT /note="H->N: In crr; 89% decrease in drosopterin (eye red
FT pigment) levels and 81% decrease in xanthommatin (eye brown
FT pigment) levels."
FT /evidence="ECO:0000269|PubMed:10407069"
FT MUTAGEN 509
FT /note="G->D: In Et87; 98% decrease in drosopterin (eye red
FT pigment) levels and undetectable levels of xanthommatin
FT (eye brown pigment)."
FT /evidence="ECO:0000269|PubMed:10407069"
FT MUTAGEN 581
FT /note="Missing: In Bwx; eyes are brown due to a reduction
FT in red pigment production."
FT /evidence="ECO:0000269|PubMed:8144619"
FT MUTAGEN 588
FT /note="G->S: In co2; normal eye color. Eyes are brown due
FT to a reduction in red pigment production in a bw/brown 6 or
FT T50 mutant background."
FT /evidence="ECO:0000269|PubMed:8144619"
FT MUTAGEN 589
FT /note="G->E: In cf; 70% decrease in drosopterin (eye red
FT pigment) levels, 36% decrease in xanthommatin (eye brown
FT pigment) levels and severe defect of copulation success;
FT when associated with R-49."
FT /evidence="ECO:0000269|PubMed:10407069,
FT ECO:0000269|PubMed:28794482"
FT MUTAGEN 590
FT /note="F->G: In sat; 96% decrease in drosopterin (eye red
FT pigment) levels and 21% decrease in xanthommatin (eye brown
FT pigment) levels."
FT /evidence="ECO:0000269|PubMed:10407069"
FT CONFLICT 25..29
FT /note="GDSGA -> LIFEIPYHCRVTAD (in Ref. 4; BAA78210)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="L -> R (in Ref. 5; AAF45826 and 7; CAB65847)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..371
FT /note="VGAQCPTNYNPADFYVQVLAVVPGREIESRDRIAKIC -> ITLHLNSYPAW
FT VPSVLPTTIRRTFTYRCWPLCPDGRSSPVIGSPRYG (in Ref. 4; BAA78210)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="G -> A (in Ref. 2; CAA26716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 75673 MW; 24AFAD799DE0D396 CRC64;
MGQEDQELLI RGGSKHPSAE HLNNGDSGAA SQSCINQGFG QAKNYGTLLP PSPPEDSGSG
SGQLAENLTY AWHNMDIFGA VNQPGSGWRQ LVNRTRGLFC NERHIPAPRK HLLKNVCGVA
YPGELLAVMG SSGAGKTTLL NALAFRSPQG IQVSPSGMRL LNGQPVDAKE MQARCAYVQQ
DDLFIGSLTA REHLIFQAMV RMPRHLTYRQ RVARVDQVIQ ELSLSKCQHT IIGVPGRVKG
LSGGERKRLA FASEALTDPP LLICDEPTSG LDSFTAHSVV QVLKKLSQKG KTVILTIHQP
SSELFELFDK ILLMAEGRVA FLGTPSEAVD FFSYVGAQCP TNYNPADFYV QVLAVVPGRE
IESRDRIAKI CDNFAISKVA RDMEQLLATK NLEKPLEQPE NGYTYKATWF MQFRAVLWRS
WLSVLKEPLL VKVRLIQTTM VAILIGLIFL GQQLTQVGVM NINGAIFLFL TNMTFQNVFA
TINVFTSELP VFMREARSRL YRCDTYFLGK TIAELPLFLT VPLVFTAIAY PMIGLRAGVL
HFFNCLALVT LVANVSTSFG YLISCASSST SMALSVGPPV IIPFLLFGGF FLNSGSVPVY
LKWLSYLSWF RYANEGLLIN QWADVEPGEI SCTSSNTTCP SSGKVILETL NFSAADLPLD
YVGLAILIVS FRVLAYLALR LRARRKE
