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Database: UniProt
Entry: U6D0L7_NEOVI
LinkDB: U6D0L7_NEOVI
Original site: U6D0L7_NEOVI 
ID   U6D0L7_NEOVI            Unreviewed;       256 AA.
AC   U6D0L7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Riboflavin transporter {ECO:0000256|RuleBase:RU368035};
DE   Flags: Fragment;
GN   Name=RFT2 {ECO:0000313|EMBL:CCP75423.1};
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Neogale.
OX   NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP75423.1};
RN   [1] {ECO:0000313|EMBL:CCP75423.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pool of brain {ECO:0000313|EMBL:CCP75423.1};
RA   Anistoroaei R., Christensen K.;
RT   "An American mink transcriptome.";
RL   Submitted (NOV-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU368035}.
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DR   EMBL; HAAF01003598; CCP75423.1; -; mRNA.
DR   AlphaFoldDB; U6D0L7; -.
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; SOLUTE CARRIER FAMILY 52; 1.
DR   PANTHER; PTHR12929:SF4; SOLUTE CARRIER FAMILY 52, RIBOFLAVIN TRANSPORTER, MEMBER 3; 1.
DR   Pfam; PF06237; SLC52_ribofla_tr; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane {ECO:0000256|RuleBase:RU368035};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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        25..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368035"
FT   TRANSMEM        55..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368035"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368035"
FT   TRANSMEM        218..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU368035"
FT   REGION          184..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CCP75423.1"
FT   NON_TER         256
FT                   /evidence="ECO:0000313|EMBL:CCP75423.1"
SQ   SEQUENCE   256 AA;  27805 MW;  D78D4B7D58AC5EF6 CRC64;
     PLACTLFAFL WNVTSWVLDG HHSIAFMVLT FFLALVDCTS SVTFLPFMSR LSARYLTTFF
     VGEGLSGLLP ALVALAQGSG LTTCVNVTQP SDTTPSSETT GKEVFLQVAN VTLMSDLTRT
     TQSAVHLESR YLPANFSPLV FFLLLSFMMA CCLTAFFVLQ RQPRPRESSI EDLLTSQVTL
     HSIRPREGED LGPPDPGACI KAQGHPEEKT DSKHPGQLAF IYILVAFVNA LTNGVLPSVQ
     PSPCLSYGPV AYHLSA
//
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