ID   RFT2_SALSA              Reviewed;         458 AA.
AC   B5X4H8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Riboflavin transporter 2;
DE            Short=RFT2;
GN   Name=rft2;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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|UniProtKB:Q9NQ40};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC       {ECO:0000305}.
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DR   EMBL; BT045947; ACI34209.1; -; mRNA.
DR   RefSeq; NP_001133955.1; NM_001140483.1.
DR   AlphaFoldDB; B5X4H8; -.
DR   Ensembl; ENSSSAT00000142134; ENSSSAP00000107332; ENSSSAG00000076975.
DR   GeneID; 100195454; -.
DR   KEGG; sasa:100195454; -.
DR   CTD; 100195454; -.
DR   OrthoDB; 757564at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa02.
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; 1.
DR   Pfam; PF06237; DUF1011; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..458
FT                   /note="Riboflavin transporter 2"
FT                   /id="PRO_0000399796"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          249..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..269
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   458 AA;  49216 MW;  E6053E8134D5BC3D CRC64;
     MTLLTHVLAC LFGMGSWVAI NGIWVELPLI VPEIPEGWYL PSYLTVLIQM ANVGPLFVTL
     MHRFRPGKLD ERPVIYSIVG LGVVATFLLA FFWKHTVPLA GATHSVPLLV LCFLLSVVDC
     TSSVTFLPFM MRLGPQYLTT YFVGEGVSGL VPAVVALVQG VGVVHCRNAT VASLANGTLG
     VNSTVGASGE LQAQYQPANF SAQVFFLFLS AMMVVCLAAF LLLNHHPAVA REKKCEQYFN
     GGLAEEKSDQ ALSLSHRPQE EKPMISSPDS HRRARQSSFG TGFYSGPELA FIFVVLAWVN
     ALTNAVLPSV QSYSCLPYGN QAYHLAATMA AVANPVACFI AMFLPLRSLV LIGLLTIVGT
     GFGTYIMAMA TLSPCPLLVH SASGTTLIVI AWVLFVLTLS YVKVIIGVIL RDEGHSALVW
     CGAVVQLGSM LGALSMFPLV SVYGLFKSGD PCNTKCTK