ID A0A0H5S3G9_BRUMA Unreviewed; 434 AA.
AC A0A0H5S3G9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Riboflavin transporter {ECO:0000256|RuleBase:RU368035};
GN ORFNames=Bm6613 {ECO:0000313|EMBL:CRZ23210.1,
GN ECO:0000313|WormBase:Bm6613}, BM_Bm6613 {ECO:0000313|EMBL:CRZ23210.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|EMBL:CRZ23210.1};
RN [1] {ECO:0000313|EMBL:CRZ23210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ23210.1};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CRZ23210.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ23210.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
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; LN856835; CRZ23210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5S3G9; -.
DR WormBase; Bm6613; BM40950; WBGene00226874; -.
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 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 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 75..96
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 300..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 355..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT TRANSMEM 399..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT REGION 218..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 47403 MW; CD09B54388EAD945 CRC64;
MTIKLSTYIC IVLFGSTSWL STNSVWLELP LLTEKLPEGW SLPSYLTVVV QIASIGPLIY
SIIRKLSKVS IPIPAMILTL LIFCCLCTVL MALFWSQTIF LFGQERSVVL MILLFGMALV
NATSNVLFMP YMATFHDSYL TAYFVGMGLS ALFPSIVSIL QGSGNNCVVV NGTSIQTSGI
LQFGVKEFNF IMLSWMLLAT VAFVCLIFLK NAKIAGKKEP STDQSPMKLS PSVDEPGSPS
SREFNPLNQC AETYGAENRS RTNNLRFMLL LFLIASISAQ MNGIVPSVQS YASLPFSQKT
YHLGLTLSNI VSPIVCFLPL FVKINGLPVL VLLTMVSTVL TGLIIAFAAM SPTPILQFSA
WGSVLIIIVV VCSVALNSFL RTVLATVLGN DTNDREMRLF WGGLFIQVGS LLGSIAMFPL
INILHLFIPA PPCQ
//
