S52AB_CAEEL
ID S52AB_CAEEL Reviewed; 476 AA.
AC G4SDH4; A0A168H3J9; G4SM24; Q95XZ2;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Riboflavin transporter rft-2 {ECO:0000312|EMBL:CCD69389.1};
DE AltName: Full=Solute carrier family 52, riboflavin transporter rft-2 {ECO:0000305};
GN Name=rft-2 {ECO:0000303|PubMed:23483992, ECO:0000312|WormBase:Y47D7A.14b};
GN ORFNames=Y47D7A.14 {ECO:0000312|WormBase:Y47D7A.14b};
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|EMBL:AFZ75250.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RA Salehi R., Fisher C.A., Bignell P.A., Old J.M.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION
RP 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).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=25963255; DOI=10.1007/s12038-015-9512-x;
RA Gandhimathi K., Karthi S., Manimaran P., Varalakshmi P., Ashokkumar B.;
RT "Riboflavin transporter-2 (rft-2) of Caenorhabditis elegans: Adaptive and
RT developmental regulation.";
RL J. Biosci. 40:257-268(2015).
CC -!- FUNCTION: Riboflavin transporter. {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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:Y47D7A.14b};
CC IsoId=G4SDH4-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y47D7A.14a};
CC IsoId=G4SDH4-2; Sequence=VSP_059271;
CC Name=c {ECO:0000312|WormBase:Y47D7A.14c};
CC IsoId=G4SDH4-3; Sequence=VSP_059270, VSP_059271;
CC -!- TISSUE SPECIFICITY: Expressed in intestine and pharynx.
CC {ECO:0000269|PubMed:23483992, ECO:0000269|PubMed:25963255}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults.
CC {ECO:0000269|PubMed:25963255}.
CC -!- INDUCTION: Down-regulated by high levels of riboflavin.
CC {ECO:0000269|PubMed:23483992, ECO:0000269|PubMed:25963255}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a severe reduction
CC in the number of laid eggs. {ECO:0000269|PubMed:23483992}.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
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DR EMBL; JX869968; AFZ75250.1; -; mRNA.
DR EMBL; BX284605; CCD69388.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD69389.1; -; Genomic_DNA.
DR EMBL; BX284605; SAP35550.1; -; Genomic_DNA.
DR RefSeq; NP_001256040.1; NM_001269111.1. [G4SDH4-2]
DR RefSeq; NP_001256041.1; NM_001269112.1. [G4SDH4-1]
DR RefSeq; NP_001317793.1; NM_001330869.1. [G4SDH4-3]
DR AlphaFoldDB; G4SDH4; -.
DR STRING; 6239.Y47D7A.14b; -.
DR PaxDb; G4SDH4; -.
DR EnsemblMetazoa; Y47D7A.14a.1; Y47D7A.14a.1; WBGene00021626. [G4SDH4-2]
DR EnsemblMetazoa; Y47D7A.14b.1; Y47D7A.14b.1; WBGene00021626. [G4SDH4-1]
DR EnsemblMetazoa; Y47D7A.14c.1; Y47D7A.14c.1; WBGene00021626. [G4SDH4-3]
DR GeneID; 178842; -.
DR KEGG; cel:CELE_Y47D7A.14; -.
DR UCSC; Y47D7A.14; c. elegans.
DR CTD; 178842; -.
DR WormBase; Y47D7A.14a; CE39189; WBGene00021626; rft-2. [G4SDH4-2]
DR WormBase; Y47D7A.14b; CE45087; WBGene00021626; rft-2. [G4SDH4-1]
DR WormBase; Y47D7A.14c; CE51669; WBGene00021626; rft-2. [G4SDH4-3]
DR eggNOG; KOG4255; Eukaryota.
DR GeneTree; ENSGT00390000003774; -.
DR InParanoid; G4SDH4; -.
DR OMA; NDGWTIH; -.
DR OrthoDB; 757564at2759; -.
DR PhylomeDB; G4SDH4; -.
DR Reactome; R-CEL-196843; Vitamin B2 (riboflavin) metabolism.
DR PRO; PR:G4SDH4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00021626; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; G4SDH4; baseline and differential.
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:0032218; P:riboflavin transport; IBA:GO_Central.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929; PTHR12929; 2.
DR Pfam; PF06237; DUF1011; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..476
FT /note="Riboflavin transporter rft-2"
FT /id="PRO_0000442704"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..75
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..140
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..306
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..366
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 388..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..437
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 215..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 2..124
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_059270"
FT VAR_SEQ 273..285
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_059271"
SQ SEQUENCE 476 AA; 51842 MW; 4098F321F568DA9C CRC64;
MGCSAATFIL VALFGSSSWM GTNSVWMQLP LLTSELPEQW NLPSYLAGVV QIACIVPLIY
TILHKGVKSF TIPTAPLIIA LLSLACCCQL GLSFFWSDYS EIFGAPRSWP LYSLLFGLAI
VNAMSNVLFM PFMAQFHPAY LNAYFVGMGL SSLAPSLLSL AQGTSMFKCD EKGVAERFPP
NFSVSIFFFV IFSFTCVALF AFIALYRSGA HTHFATPNKK EPNEGTPLKK DLNNTSSSRK
GDDEDESPIE IHETGAPAID AIVSELDVTF REELQKSFRD ANYLERSAMI NDDSEPHPVD
YITGVKFTFL LFTTALVNAQ MNGIITSVQS YAALPYSQAT YHFAVTLSNV VSPLSSFLPF
FISVRSIPVL AILTACSTAM TAFIVYLAAL SPNLIFNSVT IGSALSIGGS LIAAGLHSYL
RVVFASLLRE GHQSESRLFW CGVFIQIGSF IGSAVMFPLV NIAHLFTSAP QCKSIS
