S52A3_HUMAN
ID S52A3_HUMAN Reviewed; 469 AA.
AC Q9NQ40; A0A2I6BQ49; A8K6P1; K0A6P4; Q5W1A0; Q5W1A1; Q8NCL7; Q96GD5;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Solute carrier family 52, riboflavin transporter, member 3;
DE AltName: Full=Riboflavin transporter 2;
DE Short=hRFT2;
GN Name=SLC52A3; Synonyms=C20orf54, RFT2, RFVT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000312|EMBL:AUI80409.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION
RP (ISOFORMS 1 AND 2).
RX PubMed=29428966; DOI=10.1007/s00018-018-2757-4;
RA Long L., Pang X.X., Lei F., Zhang J.S., Wang W., Liao L.D., Xu X.E.,
RA He J.Z., Wu J.Y., Wu Z.Y., Wang L.D., Lin D.C., Li E.M., Xu L.Y.;
RT "SLC52A3 expression is activated by NF-kappaB p65/Rel-B and serves as a
RT prognostic biomarker in esophageal cancer.";
RL Cell. Mol. Life Sci. 75:2643-2661(2018).
RN [2] {ECO:0000312|EMBL:AFS68799.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Huang Z.G., Hong Q.N., Lun J.X., Lin W., Yang W., Deng Q.L., He Z.,
RA Lai Y.X., Xing J.M., Liu Y.Q.;
RT "Clone and bioinformatics analysis on the coding region of c20orf54 gene.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5] {ECO:0000312|EMBL:EAX10658.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-267;
RP MET-278 AND VAL-303.
RC TISSUE=Pancreas;
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 [7]
RP IDENTIFICATION.
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 [8]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20463145; DOI=10.3945/jn.110.122911;
RA Yao Y., Yonezawa A., Yoshimatsu H., Masuda S., Katsura T., Inui K.;
RT "Identification and comparative functional characterization of a new human
RT riboflavin transporter hRFT3 expressed in the brain.";
RL J. Nutr. 140:1220-1226(2010).
RN [9]
RP SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BOND, AND MUTAGENESIS OF CYS-326;
RP CYS-386; ARG-455; CYS-463 AND CYS-467.
RX PubMed=21512156; DOI=10.1152/ajpgi.00120.2011;
RA Subramanian V.S., Rapp L., Marchant J.S., Said H.M.;
RT "Role of cysteine residues in cell surface expression of the human
RT riboflavin transporter-2 (hRFT2) in intestinal epithelial cells.";
RL Am. J. Physiol. 301:G100-G109(2011).
RN [10]
RP INVOLVEMENT IN FALOND, INVOLVEMENT IN BVVLS1, AND VARIANT BVVLS1 ARG-17.
RX PubMed=21110228; DOI=10.1007/s10545-010-9242-z;
RA Bosch A.M., Abeling N.G., Ijlst L., Knoester H., van der Pol W.L.,
RA Stroomer A.E., Wanders R.J., Visser G., Wijburg F.A., Duran M.,
RA Waterham H.R.;
RT "Brown-Vialetto-Van Laere and Fazio Londe syndrome is associated with a
RT riboflavin transporter defect mimicking mild MADD: a new inborn error of
RT metabolism with potential treatment.";
RL J. Inherit. Metab. Dis. 34:159-164(2011).
RN [11]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24264046; DOI=10.1152/ajpgi.00349.2013;
RA Yoshimatsu H., Yonezawa A., Yao Y., Sugano K., Nakagawa S., Omura T.,
RA Matsubara K.;
RT "Functional involvement of RFVT3/SLC52A3 in intestinal riboflavin
RT absorption.";
RL Am. J. Physiol. 306:G102-G110(2014).
RN [12]
RP VARIANTS BVVLS1 LYS-36; TRP-132; LEU-224; ALA-413 AND LEU-457, AND VARIANT
RP MET-350.
RX PubMed=20206331; DOI=10.1016/j.ajhg.2010.02.006;
RA Green P., Wiseman M., Crow Y.J., Houlden H., Riphagen S., Lin J.P.,
RA Raymond F.L., Childs A.M., Sheridan E., Edwards S., Josifova D.J.;
RT "Brown-Vialetto-Van Laere syndrome, a ponto-bulbar palsy with deafness, is
RT caused by mutations in c20orf54.";
RL Am. J. Hum. Genet. 86:485-489(2010).
RN [13]
RP VARIANTS BVVLS1 THR-28 AND LYS-71.
RX PubMed=20920669; DOI=10.1016/j.ajhg.2010.05.021;
RA Johnson J.O., Gibbs J.R., Van Maldergem L., Houlden H., Singleton A.B.;
RT "Exome sequencing in Brown-Vialetto-van Laere syndrome.";
RL Am. J. Hum. Genet. 87:567-569(2010).
RN [14]
RP VARIANTS BVVLS1 SER-21; HIS-220; VAL-312 AND ASP-375.
RX PubMed=22718020; DOI=10.1038/jhg.2012.70;
RA Dezfouli M.A., Yadegari S., Nafissi S., Elahi E.;
RT "Four novel C20orf54 mutations identified in Brown-Vialetto-Van Laere
RT syndrome patients.";
RL J. Hum. Genet. 57:613-617(2012).
RN [15]
RP CHARACTERIZATION OF VARIANTS BVVLS1 ARG-17; THR-28; LYS-36; LYS-71 AND
RP TRP-132, CHARACTERIZATION OF VARIANT MET-350, FUNCTION, TRANSPORTER
RP ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22273710; DOI=10.1016/j.ymgme.2011.12.021;
RA Nabokina S.M., Subramanian V.S., Said H.M.;
RT "Effect of clinical mutations on functionality of the human riboflavin
RT transporter-2 (hRFT-2).";
RL Mol. Genet. Metab. 105:652-657(2012).
RN [16]
RP VARIANTS BVVLS1 ASP-58; TRP-266; SER-319 AND ALA-413, AND VARIANT VAL-303.
RX PubMed=22824638; DOI=10.1016/j.nmd.2012.05.007;
RA Ciccolella M., Catteruccia M., Benedetti S., Moroni I., Uziel G.,
RA Pantaleoni C., Chiapparini L., Bizzi A., D'Amico A., Fattori F.,
RA Salsano M.L., Pastore A., Tozzi G., Piemonte F., Bertini E.;
RT "Brown-Vialetto-van Laere and Fazio-Londe overlap syndromes: a clinical,
RT biochemical and genetic study.";
RL Neuromuscul. Disord. 22:1075-1082(2012).
RN [17]
RP VARIANT BVVLS1 VAL-330.
RX PubMed=22633641; DOI=10.1016/j.pediatrneurol.2012.03.008;
RA Koy A., Pillekamp F., Hoehn T., Waterham H., Klee D., Mayatepek E.,
RA Assmann B.;
RT "Brown-Vialetto-Van Laere syndrome: a riboflavin-unresponsive patient with
RT a novel mutation in the C20orf54 gene.";
RL Pediatr. Neurol. 46:407-409(2012).
RN [18]
RP VARIANT BVVLS1 SER-21, CHARACTERIZATION OF VARIANT BVVLS1 SER-21, FUNCTION,
RP TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=27702554; DOI=10.1016/j.cca.2016.09.022;
RA Udhayabanu T., Subramanian V.S., Teafatiller T., Gowda V.K., Raghavan V.S.,
RA Varalakshmi P., Said H.M., Ashokkumar B.;
RT "SLC52A2 [p.P141T] and SLC52A3 [p.N21S] causing Brown-Vialetto-Van Laere
RT syndrome in an Indian patient: First genetically proven case with mutations
RT in two riboflavin transporters.";
RL Clin. Chim. Acta 462:210-214(2016).
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 (PubMed:20463145, PubMed:22273710,
CC PubMed:24264046, PubMed:27702554). Humans are unable to synthesize
CC vitamin B2/riboflavin and must obtain it via intestinal absorption
CC (PubMed:20463145). {ECO:0000269|PubMed:20463145,
CC ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:24264046,
CC ECO:0000269|PubMed:27702554, ECO:0000303|PubMed:20463145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC ChEBI:CHEBI:57986; Evidence={ECO:0000269|PubMed:20463145,
CC ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:24264046,
CC ECO:0000269|PubMed:27702554};
CC -!- ACTIVITY REGULATION: Activity is strongly inhibited by riboflavin
CC analogs, such as lumiflavin, flavin mononucleotide (FMN), flavin
CC adenine dinucleotide (FAD), by methylene blue, and to a lesser extent
CC by amiloride. Riboflavin transport is Na(+)-independent at low pH but
CC significantly reduced by Na(+) depletion under neutral pH conditions.
CC {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:24264046}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.98 uM for riboflavin {ECO:0000269|PubMed:20463145};
CC -!- INTERACTION:
CC Q9NQ40; P54252: ATXN3; NbExp=3; IntAct=EBI-25845274, EBI-946046;
CC Q9NQ40; P50570-2: DNM2; NbExp=3; IntAct=EBI-25845274, EBI-10968534;
CC Q9NQ40; O14656-2: TOR1A; NbExp=3; IntAct=EBI-25845274, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:21512156,
CC ECO:0000269|PubMed:24264046}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20463145}. Cell membrane
CC {ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:27702554}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:29428966}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:29428966}; Multi-
CC pass membrane protein. Cytoplasm {ECO:0000269|PubMed:29428966}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:29428966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SLC52A3a {ECO:0000303|PubMed:29428966};
CC IsoId=Q9NQ40-1; Sequence=Displayed;
CC Name=2; Synonyms=SLC52A3b {ECO:0000303|PubMed:29428966};
CC IsoId=Q9NQ40-2; Sequence=VSP_003814, VSP_003815;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Highly expressed
CC in small intestine and prostate. {ECO:0000269|PubMed:20463145}.
CC -!- DISEASE: Brown-Vialetto-Van Laere syndrome 1 (BVVLS1) [MIM:211530]: A
CC rare neurologic disorder characterized by sensorineural hearing loss
CC and a variety of cranial nerve palsies, which develop over a relatively
CC short period of time in a previously healthy individual. Sensorineural
CC hearing loss may precede the neurological signs. The course is
CC invariably progressive, but the rate of decline is variable within and
CC between families. With disease evolution, long tract signs, lower motor
CC neuron signs, cerebellar ataxia and lower cranial nerve (III-VI)
CC palsies develop, giving rise to a complex picture resembling
CC amyotrophic lateral sclerosis. Diaphragmatic weakness and respiratory
CC compromise are some of the most distressing features, leading to
CC recurrent chest infections and respiratory failure, which are often the
CC cause of patients' demise. {ECO:0000269|PubMed:20206331,
CC ECO:0000269|PubMed:20920669, ECO:0000269|PubMed:21110228,
CC ECO:0000269|PubMed:22273710, ECO:0000269|PubMed:22633641,
CC ECO:0000269|PubMed:22718020, ECO:0000269|PubMed:22824638,
CC ECO:0000269|PubMed:27702554}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Fazio-Londe disease (FALOND) [MIM:211500]: A rare neurological
CC disease characterized by progressive weakness of the muscles innervated
CC by cranial nerves of the lower brain stem. It may present in childhood
CC with severe neurological deterioration with hypotonia, respiratory
CC insufficiency leading to premature death, or later in life with bulbar
CC weakness which progresses to involve motor neurons throughout the
CC neuroaxis. Clinical manifestations include dysarthria, dysphagia,
CC facial weakness, tongue weakness, and fasciculations of the tongue and
CC facial muscles. {ECO:0000269|PubMed:21110228}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
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DR EMBL; KY978478; AUI80409.1; -; mRNA.
DR EMBL; KY978479; AUI80410.1; -; mRNA.
DR EMBL; JX478249; AFS68799.1; -; mRNA.
DR EMBL; AK074650; BAC11113.1; -; mRNA.
DR EMBL; AK291706; BAF84395.1; -; mRNA.
DR EMBL; AL118502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10658.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10659.1; -; Genomic_DNA.
DR EMBL; BC009750; AAH09750.2; -; mRNA.
DR CCDS; CCDS13007.1; -. [Q9NQ40-1]
DR RefSeq; NP_212134.3; NM_033409.3. [Q9NQ40-1]
DR RefSeq; XP_005260712.1; XM_005260655.3.
DR RefSeq; XP_011527450.1; XM_011529148.1.
DR AlphaFoldDB; Q9NQ40; -.
DR BioGRID; 125241; 1.
DR IntAct; Q9NQ40; 3.
DR STRING; 9606.ENSP00000217254; -.
DR TCDB; 2.A.125.1.2; the eukaryotic riboflavin transporter (e-rft) family.
DR GlyGen; Q9NQ40; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQ40; -.
DR PhosphoSitePlus; Q9NQ40; -.
DR BioMuta; SLC52A3; -.
DR DMDM; 82654931; -.
DR MassIVE; Q9NQ40; -.
DR PaxDb; Q9NQ40; -.
DR PeptideAtlas; Q9NQ40; -.
DR PRIDE; Q9NQ40; -.
DR ProteomicsDB; 82078; -. [Q9NQ40-1]
DR ProteomicsDB; 82079; -. [Q9NQ40-2]
DR Antibodypedia; 54121; 67 antibodies from 14 providers.
DR DNASU; 113278; -.
DR Ensembl; ENST00000217254.11; ENSP00000217254.7; ENSG00000101276.18. [Q9NQ40-1]
DR Ensembl; ENST00000381944.5; ENSP00000371370.3; ENSG00000101276.18. [Q9NQ40-2]
DR Ensembl; ENST00000488495.3; ENSP00000494009.1; ENSG00000101276.18. [Q9NQ40-1]
DR Ensembl; ENST00000645534.1; ENSP00000494193.1; ENSG00000101276.18. [Q9NQ40-1]
DR GeneID; 113278; -.
DR KEGG; hsa:113278; -.
DR MANE-Select; ENST00000645534.1; ENSP00000494193.1; NM_033409.4; NP_212134.3.
DR UCSC; uc002wed.5; human. [Q9NQ40-1]
DR CTD; 113278; -.
DR DisGeNET; 113278; -.
DR GeneCards; SLC52A3; -.
DR GeneReviews; SLC52A3; -.
DR HGNC; HGNC:16187; SLC52A3.
DR HPA; ENSG00000101276; Tissue enhanced (intestine, testis).
DR MalaCards; SLC52A3; -.
DR MIM; 211500; phenotype.
DR MIM; 211530; phenotype.
DR MIM; 613350; gene.
DR neXtProt; NX_Q9NQ40; -.
DR OpenTargets; ENSG00000101276; -.
DR Orphanet; 572550; RFVT3-related riboflavin transporter deficiency.
DR PharmGKB; PA25764; -.
DR VEuPathDB; HostDB:ENSG00000101276; -.
DR eggNOG; KOG4255; Eukaryota.
DR GeneTree; ENSGT00390000003774; -.
DR HOGENOM; CLU_034789_1_0_1; -.
DR InParanoid; Q9NQ40; -.
DR OMA; NDGWTIH; -.
DR OrthoDB; 757564at2759; -.
DR PhylomeDB; Q9NQ40; -.
DR TreeFam; TF314820; -.
DR PathwayCommons; Q9NQ40; -.
DR Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
DR SignaLink; Q9NQ40; -.
DR BioGRID-ORCS; 113278; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; SLC52A3; human.
DR GeneWiki; C20orf54; -.
DR GenomeRNAi; 113278; -.
DR Pharos; Q9NQ40; Tbio.
DR PRO; PR:Q9NQ40; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NQ40; protein.
DR Bgee; ENSG00000101276; Expressed in right testis and 117 other tissues.
DR ExpressionAtlas; Q9NQ40; baseline and differential.
DR Genevisible; Q9NQ40; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
DR GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929; PTHR12929; 1.
DR Pfam; PF06237; DUF1011; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Deafness; Disease variant;
KW Disulfide bond; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..469
FT /note="Solute carrier family 52, riboflavin transporter,
FT member 3"
FT /id="PRO_0000042636"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU9"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 386..463
FT /evidence="ECO:0000305|PubMed:21512156"
FT VAR_SEQ 401..415
FT /note="ASWVLFSGCLSYVKV -> SIRPVGLLPLRTPHP (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:29428966,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_003814"
FT VAR_SEQ 416..469
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:29428966,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_003815"
FT VARIANT 17
FT /note="W -> R (in BVVLS1; loss of riboflavin transport; no
FT effect on localization to cell membrane; does not affect
FT protein abundance; dbSNP:rs797045190)"
FT /evidence="ECO:0000269|PubMed:21110228,
FT ECO:0000269|PubMed:22273710"
FT /id="VAR_077422"
FT VARIANT 21
FT /note="N -> S (in BVVLS1; loss of localization to cell
FT membrane; loss of riboflavin transport; dbSNP:rs199588390)"
FT /evidence="ECO:0000269|PubMed:22718020,
FT ECO:0000269|PubMed:27702554"
FT /id="VAR_077423"
FT VARIANT 28
FT /note="P -> T (in BVVLS1; loss of localization to cell
FT membrane; loss of riboflavin transport; does not affect
FT protein abundance; dbSNP:rs267606688)"
FT /evidence="ECO:0000269|PubMed:20920669,
FT ECO:0000269|PubMed:22273710"
FT /id="VAR_077424"
FT VARIANT 36
FT /note="E -> K (in BVVLS1; loss of localization to cell
FT membrane; loss of riboflavin transport; does not affect
FT protein abundance; dbSNP:rs267606686)"
FT /evidence="ECO:0000269|PubMed:20206331,
FT ECO:0000269|PubMed:22273710"
FT /id="VAR_063694"
FT VARIANT 58
FT /note="V -> D (in BVVLS1; dbSNP:rs797045192)"
FT /evidence="ECO:0000269|PubMed:22824638"
FT /id="VAR_077425"
FT VARIANT 71
FT /note="E -> K (in BVVLS1; loss of localization to cell
FT membrane; loss of riboflavin transport; does not affect
FT protein abundance; dbSNP:rs267606683)"
FT /evidence="ECO:0000269|PubMed:20920669,
FT ECO:0000269|PubMed:22273710"
FT /id="VAR_077426"
FT VARIANT 74
FT /note="I -> M (in dbSNP:rs35655964)"
FT /id="VAR_053565"
FT VARIANT 132
FT /note="R -> W (in BVVLS1; loss of localization to cell
FT membrane; loss of riboflavin transport; does not affect
FT protein abundance; dbSNP:rs267606684)"
FT /evidence="ECO:0000269|PubMed:20206331,
FT ECO:0000269|PubMed:22273710"
FT /id="VAR_063695"
FT VARIANT 174
FT /note="D -> G (in dbSNP:rs6054614)"
FT /id="VAR_053566"
FT VARIANT 220
FT /note="P -> H (in BVVLS1; unknown pathological
FT significance; dbSNP:rs797045194)"
FT /evidence="ECO:0000269|PubMed:22718020"
FT /id="VAR_077427"
FT VARIANT 224
FT /note="F -> L (in BVVLS1; dbSNP:rs267606685)"
FT /evidence="ECO:0000269|PubMed:20206331"
FT /id="VAR_063696"
FT VARIANT 266
FT /note="R -> W (in BVVLS1; unknown pathological
FT significance; dbSNP:rs370499474)"
FT /evidence="ECO:0000269|PubMed:22824638"
FT /id="VAR_077428"
FT VARIANT 267
FT /note="P -> L (in dbSNP:rs3746804)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_053567"
FT VARIANT 278
FT /note="T -> M (in dbSNP:rs3746803)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_053568"
FT VARIANT 303
FT /note="I -> V (in dbSNP:rs3746802)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:22824638"
FT /id="VAR_053569"
FT VARIANT 312
FT /note="A -> V (in BVVLS1; unknown pathological
FT significance; dbSNP:rs752218005)"
FT /evidence="ECO:0000269|PubMed:22718020"
FT /id="VAR_077429"
FT VARIANT 319
FT /note="P -> S (in BVVLS1; unknown pathological
FT significance; dbSNP:rs797045195)"
FT /evidence="ECO:0000269|PubMed:22824638"
FT /id="VAR_077430"
FT VARIANT 330
FT /note="G -> V (in BVVLS1; unknown pathological
FT significance; dbSNP:rs797045196)"
FT /evidence="ECO:0000269|PubMed:22633641"
FT /id="VAR_077431"
FT VARIANT 350
FT /note="L -> M (no effect on riboflavin transport; no effect
FT on localization to cell membrane; dbSNP:rs76947760)"
FT /evidence="ECO:0000269|PubMed:20206331,
FT ECO:0000269|PubMed:22273710"
FT /id="VAR_063698"
FT VARIANT 375
FT /note="G -> D (in BVVLS1; unknown pathological
FT significance; dbSNP:rs1219868273)"
FT /evidence="ECO:0000269|PubMed:22718020"
FT /id="VAR_077432"
FT VARIANT 411
FT /note="S -> R (in dbSNP:rs910857)"
FT /id="VAR_063699"
FT VARIANT 413
FT /note="V -> A (in BVVLS1; dbSNP:rs267606687)"
FT /evidence="ECO:0000269|PubMed:20206331,
FT ECO:0000269|PubMed:22824638"
FT /id="VAR_063700"
FT VARIANT 457
FT /note="F -> L (in BVVLS1; dbSNP:rs779750163)"
FT /evidence="ECO:0000269|PubMed:20206331"
FT /id="VAR_063701"
FT MUTAGEN 326
FT /note="C->A: No effect on cell surface localization."
FT /evidence="ECO:0000269|PubMed:21512156"
FT MUTAGEN 386
FT /note="C->A: Abolishes cell surface localization."
FT /evidence="ECO:0000269|PubMed:21512156"
FT MUTAGEN 455
FT /note="R->A: No effect on cell surface localization."
FT /evidence="ECO:0000269|PubMed:21512156"
FT MUTAGEN 463
FT /note="C->A: Abolishes cell surface localization."
FT /evidence="ECO:0000269|PubMed:21512156"
FT MUTAGEN 467
FT /note="C->A: Abolishes cell surface localization."
FT /evidence="ECO:0000269|PubMed:21512156"
FT CONFLICT 11
FT /note="V -> D (in Ref. 3; BAF84395)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="L -> P (in Ref. 3; BAC11113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 50805 MW; 239ED67348C93739 CRC64;
MAFLMHLLVC VFGMGSWVTI NGLWVELPLL VMELPEGWYL PSYLTVVIQL ANIGPLLVTL
LHHFRPSCLS EVPIIFTLLG VGTVTCIIFA FLWNMTSWVL DGHHSIAFLV LTFFLALVDC
TSSVTFLPFM SRLPTYYLTT FFVGEGLSGL LPALVALAQG SGLTTCVNVT EISDSVPSPV
PTRETDIAQG VPRALVSALP GMEAPLSHLE SRYLPAHFSP LVFFLLLSIM MACCLVAFFV
LQRQPRCWEA SVEDLLNDQV TLHSIRPREE NDLGPAGTVD SSQGQGYLEE KAAPCCPAHL
AFIYTLVAFV NALTNGMLPS VQTYSCLSYG PVAYHLAATL SIVANPLASL VSMFLPNRSL
LFLGVLSVLG TCFGGYNMAM AVMSPCPLLQ GHWGGEVLIV ASWVLFSGCL SYVKVMLGVV
LRDLSRSALL WCGAAVQLGS LLGALLMFPL VNVLRLFSSA DFCNLHCPA
