ID B4JTR6_DROGR Unreviewed; 477 AA.
AC B4JTR6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Riboflavin transporter {ECO:0000256|RuleBase:RU368035};
GN Name=Dgri\GH17475 {ECO:0000313|EMBL:EDV91495.1};
GN ORFNames=Dgri_GH17475 {ECO:0000313|EMBL:EDV91495.1};
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070};
RN [1] {ECO:0000313|EMBL:EDV91495.1, ECO:0000313|Proteomes:UP000001070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Plasma membrane transporter mediating the uptake by cells of
CC the water soluble vitamin B2/riboflavin that plays a key role in
CC biochemical oxidation-reduction reactions of the carbohydrate, lipid,
CC and amino acid metabolism. {ECO:0000256|RuleBase:RU368035}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC ChEBI:CHEBI:57986; Evidence={ECO:0000256|ARBA:ARBA00000215,
CC ECO:0000256|RuleBase:RU368035};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU368035}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368035}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000256|ARBA:ARBA00006366, ECO:0000256|RuleBase:RU368035}.
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DR EMBL; CH916374; EDV91495.1; -; Genomic_DNA.
DR RefSeq; XP_001994866.1; XM_001994830.1.
DR AlphaFoldDB; B4JTR6; -.
DR STRING; 7222.B4JTR6; -.
DR EnsemblMetazoa; FBtr0152889; FBpp0151381; FBgn0124945.
DR EnsemblMetazoa; FBtr0458552; FBpp0409035; FBgn0124945.
DR GeneID; 6568415; -.
DR KEGG; dgr:6568415; -.
DR eggNOG; KOG4255; Eukaryota.
DR HOGENOM; CLU_034789_1_0_1; -.
DR InParanoid; B4JTR6; -.
DR OMA; FMAMFLH; -.
DR OrthoDB; 5477759at2759; -.
DR PhylomeDB; B4JTR6; -.
DR Proteomes; UP000001070; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929:SF10; RIBOFLAVIN TRANSPORTER; 1.
DR PANTHER; PTHR12929; SOLUTE CARRIER FAMILY 52; 1.
DR Pfam; PF06237; SLC52_ribofla_tr; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU368035};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368035};
KW Reference proteome {ECO:0000313|Proteomes:UP000001070};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368035};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368035}; Transport {ECO:0000256|RuleBase:RU368035}.
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 105..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 258..277
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 407..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 442..464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
SQ SEQUENCE 477 AA; 52087 MW; 603A851101BD2CB9 CRC64;
MAGANNVGHH SGAVYSVLST PNHAGAEPLD FDRCARDEPS ELSPIFNWRT ISKKMEHKTI
DVFKNRNLLV DLLAIFFGIG TWLGVNGTFI QLPLLVNEAP EGWSLPSYLS VMVQIGNLGP
LLYTVYQKYS PWKLNDGLTI HAVLAIGTLS CLLTAFVYNQ TASLAGNEHS VALFVLTIFT
ALNACTSSVL FMPYMGRFKE QYMVMYFIGE GLSGLLPSVT ALVQGIGDTG RCVLVNVTES
GEEIYQKETQ PPLFDTKLFF LILFGLMVLS YIGYTLLNAL PVARREYADV TVSKGNKYEY
SQDGNQQLSR GQYAALLVLI GSISLFSNGM FPSIQSYSSA PYGTRAYHLA ATLSVIANPV
ACFMAMFLHF TSLRIIYLLS SLAALLTSYV FTTAVLSPYP PLYDETIGVV LVVTAWTLLI
GVVSYTKLGI TTVMRSQGGQ SLVWVGGITQ LGSAIGAISI FFAINYTRFF QAAESLC
//
