SLC52A3
entrez
113278
canonical
uniprot
Q9NQ40
canonical
ensembl
ENSG00000101276
resolver
ensp
ENSP00000217254
resolver
ensp
ENSP00000494193
resolver
ensp
ENSP00000576549
resolver
ensp
ENSP00000607435
resolver
genesymbol
SLC52A3
resolver
genesymbol_syn
C20orf54
resolver
genesymbol_syn
RFT2
resolver
genesymbol_syn
RFVT3
resolver
hgnc
HGNC:16187
resolver
uniprot
A0A2I6BQ49
resolver
uniprot
A8K6P1
resolver
uniprot
K0A6P4
resolver
uniprot
Q5W1A0
resolver
uniprot
Q5W1A1
resolver
uniprot
Q8NCL7
resolver
uniprot
Q96GD5
resolver
uniprot_entry
S52A3_HUMAN
resolver
uniprot_sec
A0A2I6BQ49
resolver
uniprot_sec
A8K6P1
resolver
uniprot_sec
K0A6P4
resolver
uniprot_sec
Q5W1A0
resolver
uniprot_sec
Q5W1A1
resolver
uniprot_sec
Q8NCL7
resolver
uniprot_sec
Q96GD5
resolver
activity_regulation
ACTIVITY REGULATION: Activity is strongly inhibited by riboflavin analogs, such as lumiflavin, flavin mononucleotide (FMN), flavin adenine dinucleotide (FAD), by methylene blue, and to a lesser extent by amiloride. Riboflavin transport is Na(+)-independent at low pH but significantly reduced by Na(+) depletion under neutral pH conditions. {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:24264046}.
uniprot
proteins
amino_acid_sequence
MAFLMHLLVCVFGMGSWVTINGLWVELPLLVMELPEGWYLPSYLTVVIQLANIGPLLVTLLHHFRPSCLSEVPIIFTLLGVGTVTCIIFAFLWNMTSWVLDGHHSIAFLVLTFFLALVDCTSSVTFLPFMSRLPTYYLTTFFVGEGLSGLLPALVALAQGSGLTTCVNVTEISDSVPSPVPTRETDIAQGVPRALVSALPGMEAPLSHLESRYLPAHFSPLVFFLLLSIMMACCLVAFFVLQRQPRCWEASVEDLLNDQVTLHSIRPREENDLGPAGTVDSSQGQGYLEEKAAPCCPAHLAFIYTLVAFVNALTNGMLPSVQTYSCLSYGPVAYHLAATLSIVANPLASLVSMFLPNRSLLFLGVLSVLGTCFGGYNMAMAVMSPCPLLQGHWGGEVLIVASWVLFSGCLSYVKVMLGVVLRDLSRSALLWCGAAVQLGSLLGALLMFPLVNVLRLFSSADFCNLHCPA
uniprot
proteins
disease_involvement
DISEASE: Brown-Vialetto-Van Laere syndrome 1 (BVVLS1) [MIM:211530]: A rare neurologic disorder characterized by sensorineural hearing loss and a variety of cranial nerve palsies, which develop over a relatively short period of time in a previously healthy individual. Sensorineural hearing loss may precede the neurological signs. The course is invariably progressive, but the rate of decline is variable within and between families. With disease evolution, long tract signs, lower motor neuron signs, cerebellar ataxia and lower cranial nerve (III-VI) palsies develop, giving rise to a complex picture resembling amyotrophic lateral sclerosis. Diaphragmatic weakness and respiratory compromise are some of the most distressing features, leading to recurrent chest infections and respiratory failure, which are often the cause of patients' demise. {ECO:0000269|PubMed:20206331, ECO:0000269|PubMed:20920669, ECO:0000269|PubMed:21110228, ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:22633641, ECO:0000269|PubMed:22718020, ECO:0000269|PubMed:22824638, ECO:0000269|PubMed:27702554}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Fazio-Londe disease (FALOND) [MIM:211500]: A rare neurological disease characterized by progressive weakness of the muscles innervated by cranial nerves of the lower brain stem. It may present in childhood with severe neurological deterioration with hypotonia, respiratory insufficiency leading to premature death, or later in life with bulbar weakness which progresses to involve motor neurons throughout the neuroaxis. Clinical manifestations include dysarthria, dysphagia, facial weakness, tongue weakness, and fasciculations of the tongue and facial muscles. {ECO:0000269|PubMed:21110228}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism (PubMed:20463145, PubMed:22273710, PubMed:24264046, PubMed:27702554). Humans are unable to synthesize vitamin B2/riboflavin and must obtain it via intestinal absorption (PubMed:20463145). {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:24264046, ECO:0000269|PubMed:27702554, ECO:0000303|PubMed:20463145}.
uniprot
proteins
mass_dalton
50805
uniprot
proteins
mutagenesis
MUTAGEN 326; /note="C->A: No effect on cell surface localization."; /evidence="ECO:0000269|PubMed:21512156"; MUTAGEN 386; /note="C->A: Abolishes cell surface localization."; /evidence="ECO:0000269|PubMed:21512156"; MUTAGEN 455; /note="R->A: No effect on cell surface localization."; /evidence="ECO:0000269|PubMed:21512156"; MUTAGEN 463; /note="C->A: Abolishes cell surface localization."; /evidence="ECO:0000269|PubMed:21512156"; MUTAGEN 467; /note="C->A: Abolishes cell surface localization."; /evidence="ECO:0000269|PubMed:21512156
uniprot
proteins
protein_family
Riboflavin transporter family
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19122205
uniprot
proteins
pubmed
20206331
uniprot
proteins
pubmed
20463145
uniprot
proteins
pubmed
20920669
uniprot
proteins
pubmed
21110228
uniprot
proteins
pubmed
21512156
uniprot
proteins
pubmed
22273710
uniprot
proteins
pubmed
22633641
uniprot
proteins
pubmed
22718020
uniprot
proteins
pubmed
22824638
uniprot
proteins
pubmed
24264046
uniprot
proteins
pubmed
27702554
uniprot
proteins
pubmed
29428966
uniprot
proteins
sequence_length
469
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:21512156, ECO:0000269|PubMed:24264046}; Multi-pass membrane protein {ECO:0000269|PubMed:20463145}. Cell membrane {ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:27702554}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:29428966}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:29428966}; Multi-pass membrane protein. Cytoplasm {ECO:0000269|PubMed:29428966}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:29428966}.
uniprot
proteins
transmembrane_region
TRANSMEM 3..23; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 44..64; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 72..92; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 98..118; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 138..158; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 221..241; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 293..313; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 336..356; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 360..380; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 397..417; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 428..448; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins