S52A3_OSMMO
ID S52A3_OSMMO Reviewed; 410 AA.
AC C1BKZ7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Solute carrier family 52, riboflavin transporter, member 3;
DE AltName: Full=Riboflavin transporter 2;
DE Short=RFT2;
GN Name=slc52a3; Synonyms=rft2;
OS Osmerus mordax (Rainbow smelt) (Atherina mordax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Stomiati; Osmeriformes; Osmeridae;
OC Osmerus.
OX NCBI_TaxID=8014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA von Schalburg K., Leong J., Cooper G., Davidson W.S., Koop B.F.;
RT "Osmerus mordax full-length cDNAs.";
RL Submitted (MAR-2009) 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:0000250|UniProtKB:Q9NQ40}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC ChEBI:CHEBI:57986; Evidence={ECO:0000250|UniProtKB:Q9NQ40};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
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DR EMBL; BT075276; ACO09700.1; -; mRNA.
DR AlphaFoldDB; C1BKZ7; -.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929; PTHR12929; 2.
DR Pfam; PF06237; DUF1011; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..410
FT /note="Solute carrier family 52, riboflavin transporter,
FT member 3"
FT /id="PRO_0000399795"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 410 AA; 44571 MW; 102A226C32BDE98A CRC64;
MAILIYALAC AFGLGSWLAI NGLWVELPII VTTLPEGWEL PSYLTVIIQL ANLGPLLVTL
MHKLCPGRLK ESVVIYTILC IGVLACFLLA FFLGRDNCGG WGPAQRSLLH HYFLPGTSGL
HLLSHLPALH DAAACPLHHH TEGGDTYVLQ TQYLPPNFTT EVFFFFLAVM MCISLAAFWK
LNRLPRTFEV STENLVPDSV SSVCSGLDNP AVRTNSQKHL CEVTSQARPL LTKSGHSMFQ
LTFIYLMVVW VNGTTNGLLP SVQTYSCMPY GNLAYHLSAA LASVANPVAC IVAMFFPKRS
LVFLGLLCVM GTGFASYNMA MAAMSPCPLL QKSALGEAII VLSWVFFTGS LSYVKVMVGV
ILRDESHSAL VWCGAAAQIG SLIGSVIMFP LINMYNLFQS GDTCSTKCPL