ID A7T9F1_NEMVE Unreviewed; 103 AA.
AC A7T9F1;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Riboflavin transporter {ECO:0000256|RuleBase:RU368035};
DE Flags: Fragment;
GN ORFNames=NEMVEDRAFT_v1g46044 {ECO:0000313|EMBL:EDO27376.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO27376.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO27376.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 x CH6 {ECO:0000313|EMBL:EDO27376.1};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU368035}.
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DR EMBL; DS473344; EDO27376.1; -; Genomic_DNA.
DR RefSeq; XP_001619476.1; XM_001619426.1.
DR AlphaFoldDB; A7T9F1; -.
DR STRING; 45351.A7T9F1; -.
DR EnsemblMetazoa; EDO27376; EDO27376; NEMVEDRAFT_v1g46044.
DR eggNOG; KOG4255; Eukaryota.
DR HOGENOM; CLU_2270508_0_0_1; -.
DR InParanoid; A7T9F1; -.
DR PhylomeDB; A7T9F1; -.
DR Proteomes; UP000001593; 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:UP000001593};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..103
FT /note="Riboflavin transporter"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012158038"
FT TRANSMEM 61..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368035"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDO27376.1"
FT NON_TER 103
FT /evidence="ECO:0000313|EMBL:EDO27376.1"
SQ SEQUENCE 103 AA; 11192 MW; 96678896B3D612D3 CRC64;
FLLVILAIVN GLSNGIIPAI QSYACIPYSY YIYHLTLTLS NIANPITCLM FPLLRVKSIP
VITFLCGVYC VMCTYIIIIA SQSPDVLLRC GDTGAALIVS ISM
//
