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Protein white

 WHITE_DROME             Reviewed;         687 AA.
P10090; Q9V3A2; Q9XY33;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 2.
13-FEB-2019, entry version 173.
RecName: Full=Protein white;
Name=w; ORFNames=CG2759;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Head;
PubMed=2109311; DOI=10.1093/nar/18.6.1633;
Pepling M., Mount S.M.;
"Sequence of a cDNA from the Drosophila melanogaster white gene.";
Nucleic Acids Res. 18:1633-1633(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6084717; DOI=10.1016/0022-2836(84)90021-4;
O'Hare K., Murphy C., Levis R., Rubin G.M.;
"DNA sequence of the white locus of Drosophila melanogaster.";
J. Mol. Biol. 180:437-455(1984).
[3]
SEQUENCE REVISION TO 25-29 AND 616.
O'Hare K.;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11156992;
Lukacsovich T., Asztalos Z., Awano W., Baba K., Kondo S., Niwa S.,
Yamamoto D.;
"Dual-tagging gene trap of novel genes in Drosophila melanogaster.";
Genetics 157:727-742(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[6]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R;
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-331.
PubMed=2503416;
Tearle R.G., Belote J.M., McKeown M., Baker B.S., Howells A.J.;
"Cloning and characterization of the scarlet gene of Drosophila
melanogaster.";
Genetics 122:595-606(1989).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11294610; DOI=10.1023/A:1004115718597;
Mackenzie S.M., Howells A.J., Cox G.B., Ewart G.D.;
"Sub-cellular localisation of the white/scarlet ABC transporter to
pigment granule membranes within the compound eye of Drosophila
melanogaster.";
Genetica 108:239-252(2000).
-!- FUNCTION: Part of a membrane-spanning permease system necessary
for the transport of pigment precursors into pigment cells
responsible for eye color. White dimerize with brown for the
transport of guanine. Scarlet and white complex transports a
metabolic intermediate (such as 3-hydroxy kynurenine) from the
cytoplasm into the pigment granules.
{ECO:0000269|PubMed:11294610}.
-!- SUBUNIT: Heterodimer of white with either brown or scarlet.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11294610};
Multi-pass membrane protein {ECO:0000269|PubMed:11294610}.
Cytoplasmic granule membrane {ECO:0000269|PubMed:11294610}; Multi-
pass membrane protein {ECO:0000269|PubMed:11294610}. Note=Pigment
granules within pigment cells and retinula cells of the compound
eye (when complexed with st).
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X51749; CAA36038.1; -; mRNA.
EMBL; X02974; CAA26716.2; -; Genomic_DNA.
EMBL; AB028139; BAA78210.1; -; Genomic_DNA.
EMBL; AE014298; AAF45826.1; -; Genomic_DNA.
EMBL; AL133506; CAB65847.1; -; Genomic_DNA.
EMBL; X76202; CAA53795.1; -; Genomic_DNA.
PIR; S08635; FYFFW.
RefSeq; NP_476787.1; NM_057439.2.
UniGene; Dm.19661; -.
ProteinModelPortal; P10090; -.
SMR; P10090; -.
BioGrid; 57802; 80.
DIP; DIP-388N; -.
IntAct; P10090; 1.
STRING; 7227.FBpp0070468; -.
TCDB; 3.A.1.204.1; the atp-binding cassette (abc) superfamily.
PaxDb; P10090; -.
PRIDE; P10090; -.
GeneID; 31271; -.
KEGG; dme:Dmel_CG2759; -.
CTD; 31271; -.
FlyBase; FBgn0003996; w.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
InParanoid; P10090; -.
KO; K21396; -.
PhylomeDB; P10090; -.
ChiTaRS; w; fly.
GenomeRNAi; 31271; -.
PRO; PR:P10090; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0003996; Expressed in 18 organ(s), highest expression level in Malpighian tubule.
Genevisible; P10090; DM.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
GO; GO:0090740; C:integral component of pigment granule membrane; IDA:FlyBase.
GO; GO:0048770; C:pigment granule; IDA:FlyBase.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:1905948; F:3',5'-cyclic GMP transmembrane-transporting ATPase activity; IMP:FlyBase.
GO; GO:0005275; F:amine transmembrane transporter activity; IMP:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0005395; F:eye pigment precursor transporter activity; IMP:FlyBase.
GO; GO:0008558; F:guanine-transporting ATPase activity; IMP:FlyBase.
GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IMP:FlyBase.
GO; GO:0042401; P:cellular biogenic amine biosynthetic process; IMP:FlyBase.
GO; GO:0070731; P:cGMP transport; IMP:FlyBase.
GO; GO:0048072; P:compound eye pigmentation; IMP:FlyBase.
GO; GO:0042441; P:eye pigment metabolic process; TAS:FlyBase.
GO; GO:0006856; P:eye pigment precursor transport; IEP:FlyBase.
GO; GO:0042332; P:gravitaxis; IMP:FlyBase.
GO; GO:0051615; P:histamine uptake; IGI:FlyBase.
GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
GO; GO:0007613; P:memory; IMP:FlyBase.
GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
GO; GO:0055085; P:transmembrane transport; IMP:FlyBase.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005284; Pigment_permease/Abcg.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00955; 3a01204; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Membrane; Nucleotide-binding; Pigment;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 687 Protein white.
/FTId=PRO_0000093382.
TRANSMEM 435 453 Helical. {ECO:0000255}.
TRANSMEM 465 485 Helical. {ECO:0000255}.
TRANSMEM 515 533 Helical. {ECO:0000255}.
TRANSMEM 542 563 Helical. {ECO:0000255}.
TRANSMEM 576 594 Helical. {ECO:0000255}.
TRANSMEM 659 678 Helical. {ECO:0000255}.
DOMAIN 93 341 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 130 137 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CONFLICT 25 29 GDSGA -> LIFEIPYHCRVTAD (in Ref. 4;
BAA78210). {ECO:0000305}.
CONFLICT 49 49 L -> R (in Ref. 5; AAF45826 and 7;
CAB65847). {ECO:0000305}.
CONFLICT 335 371 VGAQCPTNYNPADFYVQVLAVVPGREIESRDRIAKIC ->
ITLHLNSYPAWVPSVLPTTIRRTFTYRCWPLCPDGRSSPVI
GSPRYG (in Ref. 4; BAA78210).
{ECO:0000305}.
CONFLICT 616 616 G -> A (in Ref. 2; CAA26716).
{ECO:0000305}.
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


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