S52A3_RAT
ID S52A3_RAT Reviewed; 463 AA.
AC Q4FZU9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Solute carrier family 52, riboflavin transporter, member 3;
DE AltName: Full=Riboflavin transporter 2;
DE Short=rRFT2;
GN Name=Slc52a3; Synonyms=Rft2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19122205; DOI=10.1093/jb/mvn181;
RA Yamamoto S., Inoue K., Ohta K.Y., Fukatsu R., Maeda J.Y., Yoshida Y.,
RA Yuasa H.;
RT "Identification and functional characterization of rat riboflavin
RT transporter 2.";
RL J. Biochem. 145:437-443(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-269, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 uM for riboflavin {ECO:0000269|PubMed:19122205};
CC Vmax=11 pmol/min/mg enzyme {ECO:0000269|PubMed:19122205};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19122205};
CC Multi-pass membrane protein {ECO:0000269|PubMed:19122205}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in small intestine. Highly
CC expressed in jejunum and ileum. Also expressed in testis and at lower
CC level in lung, kidney, stomach and colon.
CC {ECO:0000269|PubMed:19122205}.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
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DR EMBL; BC099097; AAH99097.1; -; mRNA.
DR RefSeq; NP_001032275.1; NM_001037198.1.
DR AlphaFoldDB; Q4FZU9; -.
DR STRING; 10116.ENSRNOP00000006828; -.
DR GlyGen; Q4FZU9; 1 site.
DR iPTMnet; Q4FZU9; -.
DR PhosphoSitePlus; Q4FZU9; -.
DR PaxDb; Q4FZU9; -.
DR GeneID; 311536; -.
DR KEGG; rno:311536; -.
DR UCSC; RGD:1304644; rat.
DR CTD; 113278; -.
DR RGD; 1304644; Slc52a3.
DR eggNOG; KOG4255; Eukaryota.
DR InParanoid; Q4FZU9; -.
DR PhylomeDB; Q4FZU9; -.
DR Reactome; R-RNO-196843; Vitamin B2 (riboflavin) metabolism.
DR PRO; PR:Q4FZU9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISO:RGD.
DR GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929; PTHR12929; 1.
DR Pfam; PF06237; DUF1011; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..463
FT /note="Solute carrier family 52, riboflavin transporter,
FT member 3"
FT /id="PRO_0000399792"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..37
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..105
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..214
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..329
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..390
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..463
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 463 AA; 50130 MW; 3D513AD8339D4B15 CRC64;
MAFLTHLLVC VFGMGSWVAI NGLWVELPLL VTKLPEGWYL PSYLTVVIQL ANTGPLLVTL
MHRFRPGCLS EVPVIFLILC VGTTACILLA FLWSMTSWIQ GRQHSVAFIV LTFFLALVDC
TSSVTFLPFM SQLPTYYLTT FFIGEGLSGL LPALVALVQG SGITTCVNVT ETPGTTLNPV
TTMETSITQR TLSPSLTPLT WHLESRYLAP RFSPLLFFLL LSFLMGCCLV AFFLLQRQPW
GRQGSIEDLL HSQVTLHSIK PRDTEDTGSV GAPVSSPGKG SVEVSVASLR PAQLAFIYSV
VAFVNALTNG VLPSVQTYSC LPYGPVAYHL SATLSSVASP LACFLPIFLP NRSLLFLGVL
TVLGTGFGTY NMAMAAMSPC PILQGHWGGE VLIVLSWMLF VACLSYVKVM LGVILRDRSR
SALLWCGAAV QLGSLIGALL MFPLVNVLKL FSSADYCSLD CSA
