SCRT_DROME
ID SCRT_DROME Reviewed; 666 AA.
AC P45843; Q6NP00; Q6NR69; Q9VV67;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Protein scarlet;
DE EC=7.6.2.- {ECO:0000269|PubMed:33820991, ECO:0000269|PubMed:812484};
DE AltName: Full=ATP-binding cassette transporter sub-family G member scarlet {ECO:0000305};
DE AltName: Full=Broad substrate specificity ATP-binding cassette transporter scarlet {ECO:0000305};
GN Name=st {ECO:0000312|FlyBase:FBgn0003515};
GN ORFNames=CG4314 {ECO:0000312|FlyBase:FBgn0003515};
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].
RC STRAIN=Canton-S;
RX PubMed=8544833; DOI=10.1007/bf00418037;
RA ten Have J.F., Green M.M., Howells A.J.;
RT "Molecular characterization of spontaneous mutations at the scarlet locus
RT of Drosophila melanogaster.";
RL Mol. Gen. Genet. 249:673-681(1995).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 200-306, AND DEVELOPMENTAL STAGE.
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 [6]
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [9]
RP FUNCTION, 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 [10]
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 [11]
RP FUNCTION, CATALYTIC ACTIVITY, 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 and metabolic intermediates (PubMed:812484,
CC PubMed:18931318, PubMed:33820991). In the eye and probably in
CC association with w/white, required for the transport of the eye brown
CC pigment precursors, kynurenine and probably tryptophan, into pigment
CC cell granules (PubMed:812484, PubMed:10407069). In Malpighian tubules
CC and pupal eyes, involved in kynurenine transport (PubMed:812484).
CC Probably in association with w/white, plays a role in zinc storage
CC granule biogenesis in Malpighian tubule principal epithelial cells
CC (PubMed:29367274). {ECO:0000269|PubMed:10407069,
CC ECO:0000269|PubMed:18931318, ECO:0000269|PubMed:29367274,
CC ECO:0000269|PubMed:33820991, ECO:0000269|PubMed:812484}.
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:0000269|PubMed:33820991, ECO:0000269|PubMed:812484};
CC -!- SUBUNIT: May form a heterodimer with w/white.
CC {ECO:0000305|PubMed:11294610}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:11294610}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11294610}. Note=Co-localizes with w/white 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 eye, specifically in primary
CC pigment cells, secondary pigment cells and retinula cells (at protein
CC level). {ECO:0000269|PubMed:11294610}.
CC -!- DEVELOPMENTAL STAGE: Expressed in early and late larvae, in pupae and,
CC to a lesser extent, in adults. {ECO:0000269|PubMed:2503416}.
CC -!- DISRUPTION PHENOTYPE: Eyes are scarlet due to a defect in brown pigment
CC production (PubMed:10407069). In larval Malpighian tubules and pupal
CC eyes, kynurenine uptake is impaired resulting in a severe decrease in
CC 3-hydroxykynurenine production (PubMed:812484). In the head, levels of
CC neurotransmitters histamine, dopamine and serotonin are reduced
CC (PubMed:18931318). In addition, in lamina photoreceptor terminals R1-
CC R6, numbers of synaptic vesicles and capitate projections, which are
CC sites of endocytosis of vesicle membrane, are reduced
CC (PubMed:18931318). Reduces the levels of several metabolites, including
CC tryptophan, kynurenine, 3-hydroxykynurenine, guanosine, and, to a
CC lesser extent, xanthine and riboflavin, and increases the levels of
CC guanine and tetrahydrofolate (PubMed:33820991). 3-fold reduction in
CC Malpighian tubule zinc stores (PubMed:29367274).
CC {ECO:0000269|PubMed:10407069, ECO:0000269|PubMed:18931318,
CC ECO:0000269|PubMed:29367274, ECO:0000269|PubMed:33820991,
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; U39739; AAA82056.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49455.1; -; Genomic_DNA.
DR EMBL; BT010208; AAQ23526.1; -; mRNA.
DR EMBL; BT011131; AAR82798.1; -; mRNA.
DR EMBL; X76201; CAA53794.1; -; Genomic_DNA.
DR RefSeq; NP_524108.1; NM_079384.5.
DR AlphaFoldDB; P45843; -.
DR SMR; P45843; -.
DR BioGRID; 65140; 4.
DR IntAct; P45843; 2.
DR STRING; 7227.FBpp0075149; -.
DR TCDB; 3.A.1.204.17; the atp-binding cassette (abc) superfamily.
DR PaxDb; P45843; -.
DR DNASU; 39836; -.
DR EnsemblMetazoa; FBtr0075391; FBpp0075149; FBgn0003515.
DR GeneID; 39836; -.
DR KEGG; dme:Dmel_CG4314; -.
DR UCSC; CG4314-RA; d. melanogaster.
DR CTD; 20837; -.
DR FlyBase; FBgn0003515; st.
DR VEuPathDB; VectorBase:FBgn0003515; -.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_6_1; -.
DR InParanoid; P45843; -.
DR OMA; DYIIMIT; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; P45843; -.
DR BioGRID-ORCS; 39836; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39836; -.
DR PRO; PR:P45843; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003515; Expressed in adult Malpighian tubule (Drosophila) and 17 other tissues.
DR ExpressionAtlas; P45843; baseline and differential.
DR Genevisible; P45843; DM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
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:0031409; F:pigment binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015842; P:aminergic neurotransmitter loading into synaptic vesicle; IMP:FlyBase.
DR GO; GO:0006856; P:eye pigment precursor transport; IEP:FlyBase.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IMP:FlyBase.
DR GO; GO:0055085; P:transmembrane 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..666
FT /note="Protein scarlet"
FT /id="PRO_0000093378"
FT TOPO_DOM 1..417
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..444
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..490
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..518
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..639
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 661..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 69..316
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 26..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 126
FT /note="P -> T (in Ref. 4; AAQ23526)"
FT /evidence="ECO:0000305"
FT CONFLICT 149..150
FT /note="IS -> NH (in Ref. 1; AAA82056)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..164
FT /note="LT -> VS (in Ref. 1; AAA82056)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="Y -> N (in Ref. 4; AAQ23526)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="F -> Y (in Ref. 4; AAQ23526)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..401
FT /note="SL -> IV (in Ref. 1; AAA82056)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="S -> T (in Ref. 1; AAA82056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 74458 MW; AA4BB9AD69BFB947 CRC64;
MSDSDSKRID VEAPERVEQH ELQVMPVGST IEVPSLDSTP KLSKRNSSER SLPLRSYSKW
SPTEQGATLV WRDLCVYTNV GGSGQRMKRI INNSTGAIQP GTLMALMGSS GSGKTTLMST
LAFRQPAGTV VQGDILINGR RIGPFMHRIS GYVYQDDLFL GSLTVLEHLN FMAHLRLDRR
VSKEERRLII KELLERTGLL SAAQTRIGSG DDKKVLSGGE RKRLAFAVEL LNNPVILFCD
EPTTGLDSYS AQQLVATLYE LAQKGTTILC TIHQPSSQLF DNFNNVMLLA DGRVAFTGSP
QHALSFFANH GYYCPEAYNP ADFLIGVLAT DPGYEQASQR SAQHLCDQFA VSSAAKQRDM
LVNLEIHMAQ SGNFPFDTEV ESFRGVAWYK RFHVVWLRAS LTLLRDPTIQ WLRFIQKIAM
AFIIGACFAG TTEPSQLGVQ AVQGALFIMI SENTYHPMYS VLNLFPQGFP LFMRETRSGL
YSTGQYYAAN ILALLPGMII EPLIFVIICY WLTGLRSTFY AFGVTAMCVV LVMNVATACG
CFFSTAFNSV PLAMAYLVPL DYIFMITSGI FIQVNSLPVA FWWTQFLSWM LYANEAMTAA
QWSGVQNITC FQESADLPCF HTGQDVLDKY SFNESNVYRN LLAMVGLYFG FHLLGYYCLW
RRARKL
