S52A2_HUMAN
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 03-AUG-2022, entry version 152.
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}.
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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; 14.
DR IntAct; Q9HAB3; 6.
DR MINT; Q9HAB3; -.
DR STRING; 9606.ENSP00000436768; -.
DR DrugBank; DB01440; gamma-Hydroxybutyric acid.
DR TCDB; 2.A.125.1.3; the eukaryotic riboflavin transporter (e-rft) family.
DR GlyGen; Q9HAB3; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9HAB3; -.
DR PhosphoSitePlus; Q9HAB3; -.
DR BioMuta; SLC52A2; -.
DR DMDM; 74734171; -.
DR EPD; Q9HAB3; -.
DR jPOST; Q9HAB3; -.
DR MassIVE; Q9HAB3; -.
DR PaxDb; Q9HAB3; -.
DR PeptideAtlas; Q9HAB3; -.
DR PRIDE; Q9HAB3; -.
DR ProteomicsDB; 81389; -.
DR Antibodypedia; 67476; 94 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; ENST00000644059.3; ENSP00000494426.1; ENSG00000285112.4.
DR Ensembl; ENST00000644819.1; ENSP00000495046.1; ENSG00000285112.4.
DR Ensembl; ENST00000645040.1; ENSP00000495874.1; ENSG00000285112.4.
DR Ensembl; ENST00000645386.3; ENSP00000495049.1; ENSG00000285112.4.
DR Ensembl; ENST00000646034.1; ENSP00000495788.1; ENSG00000285112.4.
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 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 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; HVFHSRE; -.
DR OrthoDB; 757564at2759; -.
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; 35 hits in 1074 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 93 other tissues.
DR ExpressionAtlas; Q9HAB3; baseline and differential.
DR Genevisible; Q9HAB3; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
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:0006771; P:riboflavin metabolic process; TAS:Reactome.
DR GO; GO:0032218; P:riboflavin transport; IDA: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; 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
