S52AA_CAEEL
ID S52AA_CAEEL Reviewed; 427 AA.
AC Q3LFN0;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Riboflavin transporter rft-1 {ECO:0000303|PubMed:23483992};
DE AltName: Full=Solute carrier family 52, riboflavin transporter rft-1 {ECO:0000305};
GN Name=rft-1 {ECO:0000303|PubMed:23483992, ECO:0000312|WormBase:Y47D7A.16a};
GN ORFNames=Y47D7A.16 {ECO:0000312|WormBase:Y47D7A.16a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23483992; DOI=10.1371/journal.pone.0058190;
RA Biswas A., Elmatari D., Rothman J., LaMunyon C.W., Said H.M.;
RT "Identification and functional characterization of the Caenorhabditis
RT elegans riboflavin transporters rft-1 and rft-2.";
RL PLoS ONE 8:E58190-E58190(2013).
CC -!- FUNCTION: Riboflavin transporter. Riboflavin transport is Na(+)-
CC independent but pH-sensitive. {ECO:0000269|PubMed:23483992}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC ChEBI:CHEBI:57986; Evidence={ECO:0000269|PubMed:23483992};
CC -!- ACTIVITY REGULATION: Activity is strongly inhibited by riboflavin
CC analogs, such as lumiflavin and lumichrome.
CC {ECO:0000269|PubMed:23483992}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5. {ECO:0000269|PubMed:23483992};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine.
CC {ECO:0000269|PubMed:23483992}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at L1 larval stage and to a
CC lesser extent in adults. {ECO:0000269|PubMed:23483992}.
CC -!- INDUCTION: Down-regulated by high levels of riboflavin.
CC {ECO:0000269|PubMed:23483992}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a severe reduction
CC in the number of laid eggs; the few laid eggs fail to hatch.
CC {ECO:0000269|PubMed:23483992}.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
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DR EMBL; BX284605; CCD69385.2; -; Genomic_DNA.
DR RefSeq; NP_001033515.2; NM_001038426.2.
DR AlphaFoldDB; Q3LFN0; -.
DR STRING; 6239.Y47D7A.16; -.
DR PaxDb; Q3LFN0; -.
DR EnsemblMetazoa; Y47D7A.16a.1; Y47D7A.16a.1; WBGene00044637.
DR GeneID; 3896860; -.
DR KEGG; cel:CELE_Y47D7A.16; -.
DR UCSC; Y47D7A.16; c. elegans.
DR CTD; 3896860; -.
DR WormBase; Y47D7A.16a; CE47043; WBGene00044637; rft-1.
DR eggNOG; KOG4255; Eukaryota.
DR GeneTree; ENSGT00390000003774; -.
DR HOGENOM; CLU_034789_1_0_1; -.
DR InParanoid; Q3LFN0; -.
DR OMA; WCGISIQ; -.
DR OrthoDB; 757564at2759; -.
DR PhylomeDB; Q3LFN0; -.
DR Reactome; R-CEL-196843; Vitamin B2 (riboflavin) metabolism.
DR PRO; PR:Q3LFN0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00044637; Expressed in adult organism and 2 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:CACAO.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:CACAO.
DR GO; GO:0032218; P:riboflavin transport; IBA:GO_Central.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929; PTHR12929; 1.
DR Pfam; PF06237; DUF1011; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..427
FT /note="Riboflavin transporter rft-1"
FT /id="PRO_0000442703"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..42
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..111
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..184
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..297
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..353
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..427
FT /note="Extracellular"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 47067 MW; 86097E48B3D7AC14 CRC64;
MKTFLFTFCL VAIFGSSSWI GTNSVWMELS LLTAKLPEGW NLPSYLSAIV QIACLGPLIY
SIIHKGIKMT IPTVPLIFIF MVLACICQLG LCFFWDDTGY IFGAIRSWPL YLLLFGLAIV
DAISSVLFLP FMAQFHPSFL NAYFVGMGLS ALIPSLLSLI QGTSNYWCDD NKTPHYYPPR
FSVSMFFLIN FFFTCAAVAA FLVLYKIGAH KNSSQVEPEP KHSIQIIQGD STTDVNEVNT
ESSFQETSSI PDSSSATGAR LAFLLLTTAL VNAQMNGIVT SVQSYATLVY SQNTYHYAVT
LSNVISPLAS YLQFFVKIRS LPILAFLTLC SSLTTAVIIY LAALSPNWIF NSETAGTIIS
IASSLIAAGL HSYLRVMFAA LLREGNQKES RLFWCGAFIQ IGSFTGSAIM FPLVNVWKLF
HSAPSCR
