ID   BROWN_DROVI             Reviewed;         668 AA.
AC   Q24739;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Protein brown {ECO:0000303|PubMed:7635284};
DE            EC=7.6.2.- {ECO:0000250|UniProtKB:P12428};
DE            EC=7.6.2.6 {ECO:0000250|UniProtKB:P12428};
DE   AltName: Full=ATP-binding cassette transporter sub-family G member brown {ECO:0000305};
DE   AltName: Full=Broad substrate specificity ATP-binding cassette transporter brown {ECO:0000305};
GN   Name=bw {ECO:0000303|PubMed:7635284};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=7635284; DOI=10.1093/genetics/140.1.193;
RA   Martin-Morris L.E., Henikoff S.;
RT   "Conservation of brown gene trans-inactivation in Drosophila.";
RL   Genetics 140:193-199(1995).
CC   -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC       family which transports various molecules including bioamines,
CC       neurotransmitters and metabolic intermediates (By similarity). In the
CC       eye and probably in association with w/white, required for the
CC       transport of the eye red pigment precursor, guanine, into pigment cell
CC       granules (PubMed:7635284). In Malpighian tubules, involved in guanine
CC       uptake (By similarity). Probably in association with w/white, involved
CC       in aging-induced intestinal stem cell proliferation in the midgut by
CC       regulating tetrahydrofolate transport (By similarity).
CC       {ECO:0000250|UniProtKB:P12428, ECO:0000269|PubMed:7635284}.
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:0000250|UniProtKB:P12428};
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:0000250|UniProtKB:P12428};
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:0000250|UniProtKB:P12428};
CC   -!- SUBUNIT: May form a heterodimer with w/white.
CC       {ECO:0000250|UniProtKB:P12428}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in eyes. {ECO:0000269|PubMed:7635284}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L37035; AAA64466.1; -; Genomic_DNA.
DR   PIR; S55023; S55023.
DR   STRING; 7244.FBpp0234394; -.
DR   eggNOG; KOG0061; Eukaryota.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031409; F:pigment binding; IEA:UniProtKB-KW.
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; 2.
DR   TIGRFAMs; TIGR00955; 3a01204; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Membrane; Nucleotide-binding; Pigment; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..668
FT                   /note="Protein brown"
FT                   /id="PRO_0000093376"
FT   TOPO_DOM        1..412
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        434..453
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        475..490
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        491..511
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        512..524
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        525..545
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        546..561
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        562..582
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        583..637
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        638..658
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        659..668
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          31..328
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   668 AA;  75253 MW;  F96E9492A735E1E2 CRC64;
     MPMDEGDAQG SLLLEWKQLN YYVPAQEQSN YSFWNECRKQ RELGILHDVS GHLKTGDLIA
     ILGGSGAGKT TLLAAISQRL RGNLTGDVVL NGMAMERDQM TRISSFLREF EINVKTFTAY
     DDLYFMSHFK MHRRTTKSEK RQAVSDLLLA VGLRDAAHTR IQQLSGGERK RLSLAEELIT
     DPIFLFCDEP TTGLDSFSAY TVIKTLRHLC TRRRIAKHSL TQVYGEDSFA TPSDNGSSGS
     NSIEMEIVDN SHESLLQAMK ELPTLGVLNN SPNGTQKKAA ICSIHQPTSD IFELFTHIIL
     MDGGRIVYQG RTEQAAKFFT EGFMQPKNCN PADFYLKTLA DGQGSKNAGE LLRAKYEHET
     DGLYSGSWLL ARNYSGDYMK HVQNFKKIRW IYQVYLLVIR FMTEDLANIR SGLIGFGFFM
     TTAVTLSLMY SGVGGLTQRT VQDVGGSIFM LSNEMIFTFS YGVTYIFPAA LPIIRREVAE
     GTYSLSAYYV ALVLSFVPVA FFKGYMFLSV IYASIYYTRG FLLYITMGFL MSLSAIAAVG
     YGVFLSSLFE TDKMASECAA PFDLIFLIFG GTYMNVDSVP LLKYFSLFFY SNEALMYNFW
     IDIDNIACXV NDEHPCCQTG LEVLQQASFR TADYTFWLDC ASLLVVALVF HIVSFTLIRR
     YINRSGYY