ID S52A2_HUMAN Reviewed; 445 AA. AC Q9HAB3; A8K6B6; D3DWL8; G1UCY1; Q86UT1; DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Solute carrier family 52, riboflavin transporter, member 2; DE AltName: Full=Porcine endogenous retrovirus A receptor 1 {ECO:0000303|PubMed:12740431}; DE Short=PERV-A receptor 1 {ECO:0000303|PubMed:12740431}; DE AltName: Full=Protein GPR172A; DE AltName: Full=Riboflavin transporter 3; DE Short=hRFT3; GN Name=SLC52A2; Synonyms=GPR172A, PAR1, RFT3; 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] RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION AS A VIRAL RP RECEPTOR (MICROBIAL INFECTION). RX PubMed=12740431; DOI=10.1073/pnas.1138025100; RA Ericsson T.A., Takeuchi Y., Templin C., Quinn G., Farhadian S.F., RA Wood J.C., Oldmixon B.A., Suling K.M., Ishii J.K., Kitagawa Y., RA Miyazawa T., Salomon D.R., Weiss R.A., Patience C.; RT "Identification of receptors for pig endogenous retrovirus."; RL Proc. Natl. Acad. Sci. U.S.A. 100:6759-6764(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo, 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=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [5] 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]. RC TISSUE=Skin; 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 FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17197387; DOI=10.1096/fj.06-6509com; RA Andriamampandry C., Taleb O., Kemmel V., Humbert J.P., Aunis D., Maitre M.; RT "Cloning and functional characterization of a gamma-hydroxybutyrate RT receptor identified in the human brain."; RL FASEB J. 21:885-895(2007). RN [8] RP FUNCTION AS A VIRAL RECEPTOR (MICROBIAL INFECTION). RX PubMed=19307586; DOI=10.1073/pnas.0809741106; RA Mazari P.M., Linder-Basso D., Sarangi A., Chang Y., Roth M.J.; RT "Single-round selection yields a unique retroviral envelope utilizing RT GPR172A as its host receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 106:5848-5853(2009). RN [9] RP VARIANT BVVLS2 ARG-306. RX PubMed=22740598; DOI=10.1093/brain/aws161; RA Johnson J.O., Gibbs J.R., Megarbane A., Urtizberea J.A., Hernandez D.G., RA Foley A.R., Arepalli S., Pandraud A., Simon-Sanchez J., Clayton P., RA Reilly M.M., Muntoni F., Abramzon Y., Houlden H., Singleton A.B.; RT "Exome sequencing reveals riboflavin transporter mutations as a cause of RT motor neuron disease."; RL Brain 135:2875-2882(2012). RN [10] RP VARIANTS BVVLS2 PRO-123 AND PRO-339, CHARACTERIZATION OF VARIANTS BVVLS2 RP PRO-123 AND PRO-339, FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=22864630; DOI=10.1007/s10545-012-9513-y; RA Haack T.B., Makowski C., Yao Y., Graf E., Hempel M., Wieland T., Tauer U., RA Ahting U., Mayr J.A., Freisinger P., Yoshimatsu H., Inui K., Strom T.M., RA Meitinger T., Yonezawa A., Prokisch H.; RT "Impaired riboflavin transport due to missense mutations in SLC52A2 causes RT Brown-Vialetto-Van Laere syndrome."; RL J. Inherit. Metab. Dis. 35:943-948(2012). RN [11] RP VARIANTS BVVLS2 PHE-52 AND SER-419, CHARACTERIZATION OF VARIANTS BVVLS2 RP PHE-52 AND SER-419, FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=23243084; DOI=10.1136/jmedgenet-2012-101204; RA Ciccolella M., Corti S., Catteruccia M., Petrini S., Tozzi G., Rizza T., RA Carrozzo R., Nizzardo M., Bordoni A., Ronchi D., D'Amico A., Rizzo C., RA Comi G.P., Bertini E.; RT "Riboflavin transporter 3 involvement in infantile Brown-Vialetto-Van Laere RT disease: two novel mutations."; RL J. Med. Genet. 50:104-107(2013). RN [12] RP VARIANTS BVVLS2 SER-31; ASP-284; CYS-305; ARG-306; PRO-312 AND PRO-339, RP CHARACTERIZATION OF VARIANTS BVVLS2 SER-31; ASP-284; CYS-305; ARG-306; RP PRO-312 AND PRO-339, FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR RP LOCATION. RX PubMed=24253200; DOI=10.1093/brain/awt315; RA Foley A.R., Menezes M.P., Pandraud A., Gonzalez M.A., Al-Odaib A., RA Abrams A.J., Sugano K., Yonezawa A., Manzur A.Y., Burns J., Hughes I., RA McCullagh B.G., Jungbluth H., Lim M.J., Lin J.P., Megarbane A., RA Urtizberea J.A., Shah A.H., Antony J., Webster R., Broomfield A., Ng J., RA Mathew A.A., O'Byrne J.J., Forman E., Scoto M., Prasad M., O'Brien K., RA Olpin S., Oppenheim M., Hargreaves I., Land J.M., Wang M.X., Carpenter K., RA Horvath R., Straub V., Lek M., Gold W., Farrell M.O., Brandner S., RA Phadke R., Matsubara K., McGarvey M.L., Scherer S.S., Baxter P.S., RA King M.D., Clayton P., Rahman S., Reilly M.M., Ouvrier R.A., RA Christodoulou J., Zuechner S., Muntoni F., Houlden H.; RT "Treatable childhood neuronopathy caused by mutations in riboflavin RT transporter RFVT2."; RL Brain 137:44-56(2014). RN [13] RP VARIANT BVVLS2 THR-141, CHARACTERIZATION OF VARIANT BVVLS2 THR-141, RP FUNCTION, 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:22864630, CC PubMed:23243084, PubMed:24253200, PubMed:27702554). Humans are unable CC to synthesize vitamin B2/riboflavin and must obtain it via intestinal CC absorption (PubMed:20463145). May also act as a receptor for 4- CC hydroxybutyrate (Probable). {ECO:0000269|PubMed:20463145, CC ECO:0000269|PubMed:22864630, ECO:0000269|PubMed:23243084, CC ECO:0000269|PubMed:24253200, ECO:0000269|PubMed:27702554, CC ECO:0000303|PubMed:20463145, ECO:0000305|PubMed:17197387}. CC -!- FUNCTION: (Microbial infection) In case of infection by retroviruses, CC acts as a cell receptor to retroviral envelopes similar to the porcine CC endogenous retrovirus (PERV-A). {ECO:0000269|PubMed:12740431, CC ECO:0000269|PubMed:19307586}. 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:22864630, ECO:0000269|PubMed:23243084, CC ECO:0000269|PubMed:24253200, ECO:0000269|PubMed:27702554}; CC -!- ACTIVITY REGULATION: Riboflavin transport is Na(+)-independent but CC moderately pH-sensitive (PubMed:20463145). Activity is strongly CC inhibited by riboflavin analogs, such as lumiflavin (PubMed:20463145). CC Weakly inhibited by flavin adenine dinucleotide (FAD) and flavin CC mononucleotide (FMN) (PubMed:20463145). {ECO:0000269|PubMed:20463145}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.33 uM for riboflavin {ECO:0000269|PubMed:20463145}; CC -!- INTERACTION: CC Q9HAB3; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10309896, EBI-396137; CC Q9HAB3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10309896, EBI-18304435; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17197387, CC ECO:0000269|PubMed:20463145, ECO:0000269|PubMed:24253200, CC ECO:0000269|PubMed:27702554}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Highly expressed in brain, fetal brain and salivary CC gland. Weakly expressed in other tissues. {ECO:0000269|PubMed:12740431, CC ECO:0000269|PubMed:20463145}. CC -!- DISEASE: Brown-Vialetto-Van Laere syndrome 2 (BVVLS2) [MIM:614707]: An CC autosomal recessive progressive neurologic disorder characterized by CC early childhood onset of sensorineural deafness, bulbar dysfunction, CC and severe diffuse muscle weakness and wasting resulting in respiratory CC insufficiency and loss of independent ambulation. Because it results CC from a defect in riboflavin metabolism, some patients may benefit from CC high-dose riboflavin supplementation. {ECO:0000269|PubMed:22740598, CC ECO:0000269|PubMed:22864630, ECO:0000269|PubMed:23243084, CC ECO:0000269|PubMed:24253200, ECO:0000269|PubMed:27702554}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the riboflavin transporter family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY070774; AAL59882.1; -; mRNA. DR EMBL; AB522904; BAK79010.1; -; mRNA. DR EMBL; AK021918; BAB13936.1; -; mRNA. DR EMBL; AK027888; BAB55433.1; -; mRNA. DR EMBL; AK291581; BAF84270.1; -; mRNA. DR EMBL; AF205589; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471162; EAW82115.1; -; Genomic_DNA. DR EMBL; CH471162; EAW82116.1; -; Genomic_DNA. DR EMBL; BC002917; AAH02917.1; -; mRNA. DR CCDS; CCDS6423.1; -. DR RefSeq; NP_001240744.1; NM_001253815.1. DR RefSeq; NP_001240745.1; NM_001253816.1. DR RefSeq; NP_078807.1; NM_024531.4. DR RefSeq; XP_006716721.1; XM_006716658.2. DR RefSeq; XP_006716722.1; XM_006716659.2. DR RefSeq; XP_006716723.1; XM_006716660.2. DR RefSeq; XP_016869308.1; XM_017013819.1. DR RefSeq; XP_016869309.1; XM_017013820.1. DR AlphaFoldDB; Q9HAB3; -. DR BioGRID; 122725; 15. DR IntAct; Q9HAB3; 6. DR MINT; Q9HAB3; -. DR STRING; 9606.ENSP00000496184; -. DR DrugBank; DB01440; gamma-Hydroxybutyric acid. DR DrugBank; DB09072; Sodium oxybate. DR TCDB; 2.A.125.1.3; the eukaryotic riboflavin transporter (e-rft) family. DR GlyCosmos; Q9HAB3; 1 site, 2 glycans. DR GlyGen; Q9HAB3; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; Q9HAB3; -. DR PhosphoSitePlus; Q9HAB3; -. DR SwissPalm; Q9HAB3; -. DR BioMuta; SLC52A2; -. DR DMDM; 74734171; -. DR EPD; Q9HAB3; -. DR jPOST; Q9HAB3; -. DR MassIVE; Q9HAB3; -. DR PaxDb; 9606-ENSP00000436768; -. DR PeptideAtlas; Q9HAB3; -. DR ProteomicsDB; 81389; -. DR Pumba; Q9HAB3; -. DR Antibodypedia; 67476; 115 antibodies from 18 providers. DR DNASU; 79581; -. DR Ensembl; ENST00000329994.7; ENSP00000333638.2; ENSG00000185803.12. DR Ensembl; ENST00000402965.5; ENSP00000385961.1; ENSG00000185803.12. DR Ensembl; ENST00000527078.6; ENSP00000434728.1; ENSG00000185803.12. DR Ensembl; ENST00000530047.5; ENSP00000435820.1; ENSG00000185803.12. DR Ensembl; ENST00000532815.2; ENSP00000501933.1; ENSG00000185803.12. DR Ensembl; ENST00000533662.2; ENSP00000502274.1; ENSG00000185803.12. DR Ensembl; ENST00000534725.6; ENSP00000431965.2; ENSG00000185803.12. DR Ensembl; ENST00000643944.2; ENSP00000496184.2; ENSG00000185803.12. DR Ensembl; ENST00000674870.1; ENSP00000502406.1; ENSG00000185803.12. DR Ensembl; ENST00000675121.1; ENSP00000501993.1; ENSG00000185803.12. DR Ensembl; ENST00000675280.1; ENSP00000502796.1; ENSG00000185803.12. DR Ensembl; ENST00000675292.1; ENSP00000502652.1; ENSG00000185803.12. DR Ensembl; ENST00000675888.1; ENSP00000502294.1; ENSG00000185803.12. DR Ensembl; ENST00000710449.1; ENSP00000518278.1; ENSG00000285112.5. DR Ensembl; ENST00000710451.1; ENSP00000518280.1; ENSG00000285112.5. DR Ensembl; ENST00000710453.1; ENSP00000518281.1; ENSG00000285112.5. DR Ensembl; ENST00000710454.1; ENSP00000518282.1; ENSG00000285112.5. DR Ensembl; ENST00000710455.1; ENSP00000518283.1; ENSG00000285112.5. DR Ensembl; ENST00000710456.1; ENSP00000518284.1; ENSG00000285112.5. DR Ensembl; ENST00000710458.1; ENSP00000518286.1; ENSG00000285112.5. DR Ensembl; ENST00000710459.1; ENSP00000518287.1; ENSG00000285112.5. DR Ensembl; ENST00000710461.1; ENSP00000518289.1; ENSG00000285112.5. DR Ensembl; ENST00000710462.1; ENSP00000518290.1; ENSG00000285112.5. DR Ensembl; ENST00000710465.1; ENSP00000518293.1; ENSG00000285112.5. DR Ensembl; ENST00000710466.1; ENSP00000518294.1; ENSG00000285112.5. DR Ensembl; ENST00000710468.1; ENSP00000518296.1; ENSG00000285112.5. DR GeneID; 79581; -. DR KEGG; hsa:79581; -. DR MANE-Select; ENST00000643944.2; ENSP00000496184.2; NM_001363118.2; NP_001350047.1. DR UCSC; uc003zcc.4; human. DR AGR; HGNC:30224; -. DR CTD; 79581; -. DR DisGeNET; 79581; -. DR GeneCards; SLC52A2; -. DR GeneReviews; SLC52A2; -. DR HGNC; HGNC:30224; SLC52A2. DR HPA; ENSG00000185803; Low tissue specificity. DR MalaCards; SLC52A2; -. DR MIM; 607882; gene. DR MIM; 614707; phenotype. DR neXtProt; NX_Q9HAB3; -. DR OpenTargets; ENSG00000185803; -. DR Orphanet; 572543; RFVT2-related riboflavin transporter deficiency. DR PharmGKB; PA134982935; -. DR VEuPathDB; HostDB:ENSG00000185803; -. DR eggNOG; KOG4255; Eukaryota. DR GeneTree; ENSGT00390000003774; -. DR HOGENOM; CLU_034789_1_0_1; -. DR InParanoid; Q9HAB3; -. DR OMA; RVAIHCI; -. DR OrthoDB; 5477759at2759; -. DR PhylomeDB; Q9HAB3; -. DR TreeFam; TF314820; -. DR PathwayCommons; Q9HAB3; -. DR Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism. DR SignaLink; Q9HAB3; -. DR BioGRID-ORCS; 79581; 36 hits in 1157 CRISPR screens. DR ChiTaRS; SLC52A2; human. DR GenomeRNAi; 79581; -. DR Pharos; Q9HAB3; Tbio. DR PRO; PR:Q9HAB3; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9HAB3; Protein. DR Bgee; ENSG00000185803; Expressed in mucosa of transverse colon and 95 other cell types or tissues. DR ExpressionAtlas; Q9HAB3; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0062124; F:4-hydroxybutyrate receptor activity; IDA:UniProtKB. DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0072388; P:flavin adenine dinucleotide biosynthetic process; IEA:Ensembl. DR GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome. DR GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB. DR InterPro; IPR009357; Riboflavin_transptr. DR PANTHER; PTHR12929; SOLUTE CARRIER FAMILY 52; 1. DR PANTHER; PTHR12929:SF1; SOLUTE CARRIER FAMILY 52, RIBOFLAVIN TRANSPORTER, MEMBER 2; 1. DR Pfam; PF06237; SLC52_ribofla_tr; 1. DR Genevisible; Q9HAB3; HS. PE 1: Evidence at protein level; KW Cell membrane; Deafness; Disease variant; KW Host cell receptor for virus entry; Membrane; Receptor; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..445 FT /note="Solute carrier family 52, riboflavin transporter, FT member 2" FT /id="PRO_0000042631" FT TRANSMEM 14..34 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 47..67 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 86..106 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 112..132 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 147..167 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 196..216 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 277..297 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 312..332 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 339..359 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 366..386 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 404..424 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 228..264 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 31 FT /note="W -> S (in BVVLS2; strong decrease in riboflavin FT transport; no effect on localization to plasma membrane; no FT effect on protein abundance; dbSNP:rs797045199)" FT /evidence="ECO:0000269|PubMed:24253200" FT /id="VAR_077433" FT VARIANT 52 FT /note="S -> F (in BVVLS2; decreased riboflavin transport; FT dbSNP:rs397514657)" FT /evidence="ECO:0000269|PubMed:23243084" FT /id="VAR_077434" FT VARIANT 123 FT /note="L -> P (in BVVLS2; strongly decreased riboflavin FT transport; dbSNP:rs397514538)" FT /evidence="ECO:0000269|PubMed:22864630" FT /id="VAR_077435" FT VARIANT 141 FT /note="P -> T (in BVVLS2; decreased riboflavin transport; FT no effect on localization to plasma membrane; FT dbSNP:rs377740960)" FT /evidence="ECO:0000269|PubMed:27702554" FT /id="VAR_077436" FT VARIANT 284 FT /note="A -> D (in BVVLS2; loss of riboflavin transport; FT loss of localization to plasma membrane; no effect on FT protein abundance; dbSNP:rs398123067)" FT /evidence="ECO:0000269|PubMed:24253200" FT /id="VAR_077437" FT VARIANT 305 FT /note="Y -> C (in BVVLS2; decreased riboflavin transport; FT decreased localization to plasma membrane; no effect on FT protein abundance; dbSNP:rs398123068)" FT /evidence="ECO:0000269|PubMed:24253200" FT /id="VAR_077438" FT VARIANT 306 FT /note="G -> R (in BVVLS2; decreased riboflavin transport; FT decreased localization to plasma membrane; no effect on FT protein abundance; dbSNP:rs398124641)" FT /evidence="ECO:0000269|PubMed:22740598, FT ECO:0000269|PubMed:24253200" FT /id="VAR_068694" FT VARIANT 312 FT /note="L -> P (in BVVLS2; decreased riboflavin transport; FT decreased localization to plasma membrane; no effect on FT protein abundance; dbSNP:rs754320812)" FT /evidence="ECO:0000269|PubMed:24253200" FT /id="VAR_077439" FT VARIANT 339 FT /note="L -> P (in BVVLS2; loss of riboflavin transport; FT loss of localization to plasma membrane; no effect on FT protein abundance; dbSNP:rs148234606)" FT /evidence="ECO:0000269|PubMed:22864630, FT ECO:0000269|PubMed:24253200" FT /id="VAR_077440" FT VARIANT 419 FT /note="G -> S (in BVVLS2; decreased riboflavin transport; FT dbSNP:rs397514658)" FT /evidence="ECO:0000269|PubMed:23243084" FT /id="VAR_077441" FT CONFLICT 341 FT /note="G -> S (in Ref. 1; AAL59882)" FT /evidence="ECO:0000305" SQ SEQUENCE 445 AA; 45777 MW; B61421B956E44F84 CRC64; MAAPTPARPV LTHLLVALFG MGSWAAVNGI WVELPVVVKE LPEGWSLPSY VSVLVALGNL GLLVVTLWRR LAPGKDEQVP IRVVQVLGMV GTALLASLWH HVAPVAGQLH SVAFLALAFV LALACCASNV TFLPFLSHLP PRFLRSFFLG QGLSALLPCV LALVQGVGRL ECPPAPINGT PGPPLDFLER FPASTFFWAL TALLVASAAA FQGLLLLLPP PPSVPTGELG SGLQVGAPGA EEEVEESSPL QEPPSQAAGT TPGPDPKAYQ LLSARSACLL GLLAATNALT NGVLPAVQSF SCLPYGRLAY HLAVVLGSAA NPLACFLAMG VLCRSLAGLG GLSLLGVFCG GYLMALAVLS PCPPLVGTSA GVVLVVLSWV LCLGVFSYVK VAASSLLHGG GRPALLAAGV AIQVGSLLGA VAMFPPTSIY HVFHSRKDCA DPCDS //