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Protein

Solute carrier family 52, riboflavin transporter, member 3

Gene

SLC52A3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transporter for riboflavin, which must be obtained as a nutrient via intestinal absorption. Riboflavin transport is Na+-independent at low pH but significantly reduced by Na+ depletion under neutral pH conditions. 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.2 Publications

Kineticsi

  1. KM=0.98 µM for riboflavin1 Publication

    GO - Molecular functioni

    • riboflavin transporter activity Source: UniProtKB

    GO - Biological processi

    • cellular response to heat Source: Ensembl
    • riboflavin metabolic process Source: Reactome
    • riboflavin transport Source: UniProtKB
    • sensory perception of sound Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • vitamin metabolic process Source: Reactome
    • water-soluble vitamin metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_11070. Vitamin B2 (riboflavin) metabolism.

    Protein family/group databases

    TCDBi9.A.53.1.2. the eukaryotic riboflavin transporter (e-rft) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Solute carrier family 52, riboflavin transporter, member 3
    Alternative name(s):
    Riboflavin transporter 2
    Short name:
    hRFT2
    Gene namesi
    Name:SLC52A3
    Synonyms:C20orf54, RFT2, RFVT3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16187. SLC52A3.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 22CytoplasmicSequence Analysis
    Transmembranei3 – 2321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini24 – 4320ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei44 – 6421HelicalSequence AnalysisAdd
    BLAST
    Topological domaini65 – 717CytoplasmicSequence Analysis
    Transmembranei72 – 9221HelicalSequence AnalysisAdd
    BLAST
    Topological domaini93 – 975ExtracellularSequence Analysis
    Transmembranei98 – 11821HelicalSequence AnalysisAdd
    BLAST
    Topological domaini119 – 13719CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei138 – 15821HelicalSequence AnalysisAdd
    BLAST
    Topological domaini159 – 22062ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei221 – 24121HelicalSequence AnalysisAdd
    BLAST
    Topological domaini242 – 29251CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei293 – 31321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini314 – 33522ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei336 – 35621HelicalSequence AnalysisAdd
    BLAST
    Topological domaini357 – 3593CytoplasmicSequence Analysis
    Transmembranei360 – 38021HelicalSequence AnalysisAdd
    BLAST
    Topological domaini381 – 39616ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei397 – 41721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini418 – 42710CytoplasmicSequence Analysis
    Transmembranei428 – 44821HelicalSequence AnalysisAdd
    BLAST
    Topological domaini449 – 46921ExtracellularSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • apical plasma membrane Source: UniProtKB-SubCell
    • integral component of plasma membrane Source: UniProtKB
    • plasma membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Brown-Vialetto-Van Laere syndrome 1 (BVVLS1)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:211530
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361E → K in BVVLS1. 1 Publication
    VAR_063694
    Natural varianti132 – 1321R → W in BVVLS1. 1 Publication
    VAR_063695
    Natural varianti224 – 2241F → L in BVVLS1. 1 Publication
    VAR_063696
    Natural varianti413 – 4131V → A in BVVLS1; may cause a mild form of the disease. 1 Publication
    VAR_063700
    Natural varianti457 – 4571F → L in BVVLS1. 1 Publication
    VAR_063701
    Fazio-Londe disease (FALOND)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:211500

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi326 – 3261C → A: No effect on cell surface localization. 1 Publication
    Mutagenesisi386 – 3861C → A: Abolishes cell surface localization. 1 Publication
    Mutagenesisi455 – 4551R → A: No effect on cell surface localization. 1 Publication
    Mutagenesisi463 – 4631C → A: Abolishes cell surface localization. 1 Publication
    Mutagenesisi467 – 4671C → A: Abolishes cell surface localization. 1 Publication

    Keywords - Diseasei

    Deafness, Disease mutation

    Organism-specific databases

    MIMi211500. phenotype.
    211530. phenotype.
    Orphaneti97229. Riboflavin transporter deficiency.
    PharmGKBiPA25764.

    Polymorphism and mutation databases

    BioMutaiSLC52A3.
    DMDMi82654931.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 469469Solute carrier family 52, riboflavin transporter, member 3PRO_0000042636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi386 ↔ 4631 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ9NQ40.

    PTM databases

    PhosphoSiteiQ9NQ40.

    Expressioni

    Tissue specificityi

    Predominantly expressed in testis. Highly expressed in small intestine and prostate.1 Publication

    Gene expression databases

    BgeeiQ9NQ40.
    CleanExiHS_C20orf54.
    ExpressionAtlasiQ9NQ40. baseline and differential.
    GenevestigatoriQ9NQ40.

    Organism-specific databases

    HPAiHPA049391.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000217254.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NQ40.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the riboflavin transporter family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG326568.
    GeneTreeiENSGT00390000003774.
    HOGENOMiHOG000247012.
    HOVERGENiHBG051170.
    InParanoidiQ9NQ40.
    KOiK14620.
    OMAiWVLDGHH.
    OrthoDBiEOG7XDBFX.
    PhylomeDBiQ9NQ40.
    TreeFamiTF314820.

    Family and domain databases

    InterProiIPR009357. Endogenous_retrovirus_rcpt.
    [Graphical view]
    PANTHERiPTHR12929. PTHR12929. 1 hit.
    PfamiPF06237. DUF1011. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9NQ40-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MAFLMHLLVC VFGMGSWVTI NGLWVELPLL VMELPEGWYL PSYLTVVIQL
    60 70 80 90 100
    ANIGPLLVTL LHHFRPSCLS EVPIIFTLLG VGTVTCIIFA FLWNMTSWVL
    110 120 130 140 150
    DGHHSIAFLV LTFFLALVDC TSSVTFLPFM SRLPTYYLTT FFVGEGLSGL
    160 170 180 190 200
    LPALVALAQG SGLTTCVNVT EISDSVPSPV PTRETDIAQG VPRALVSALP
    210 220 230 240 250
    GMEAPLSHLE SRYLPAHFSP LVFFLLLSIM MACCLVAFFV LQRQPRCWEA
    260 270 280 290 300
    SVEDLLNDQV TLHSIRPREE NDLGPAGTVD SSQGQGYLEE KAAPCCPAHL
    310 320 330 340 350
    AFIYTLVAFV NALTNGMLPS VQTYSCLSYG PVAYHLAATL SIVANPLASL
    360 370 380 390 400
    VSMFLPNRSL LFLGVLSVLG TCFGGYNMAM AVMSPCPLLQ GHWGGEVLIV
    410 420 430 440 450
    ASWVLFSGCL SYVKVMLGVV LRDLSRSALL WCGAAVQLGS LLGALLMFPL
    460
    VNVLRLFSSA DFCNLHCPA
    Length:469
    Mass (Da):50,805
    Last modified:November 22, 2005 - v4
    Checksum:i239ED67348C93739
    GO
    Isoform 2 (identifier: Q9NQ40-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-415: ASWVLFSGCLSYVKV → SIRPVGLLPLRTPHP
         416-469: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:415
    Mass (Da):45,043
    Checksum:i8E072208A8998A56
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111V → D in BAF84395 (PubMed:14702039).Curated
    Sequence conflicti199 – 1991L → P in BAC11113 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361E → K in BVVLS1. 1 Publication
    VAR_063694
    Natural varianti74 – 741I → M.
    Corresponds to variant rs35655964 [ dbSNP | Ensembl ].
    VAR_053565
    Natural varianti132 – 1321R → W in BVVLS1. 1 Publication
    VAR_063695
    Natural varianti174 – 1741D → G.
    Corresponds to variant rs6054614 [ dbSNP | Ensembl ].
    VAR_053566
    Natural varianti224 – 2241F → L in BVVLS1. 1 Publication
    VAR_063696
    Natural varianti267 – 2671P → L.1 Publication
    Corresponds to variant rs3746804 [ dbSNP | Ensembl ].
    VAR_053567
    Natural varianti278 – 2781T → M.1 Publication
    Corresponds to variant rs3746803 [ dbSNP | Ensembl ].
    VAR_053568
    Natural varianti303 – 3031I → V.1 Publication
    Corresponds to variant rs3746802 [ dbSNP | Ensembl ].
    VAR_053569
    Natural varianti350 – 3501L → M May be a common polymorphism. 1 Publication
    Corresponds to variant rs76947760 [ dbSNP | Ensembl ].
    VAR_063698
    Natural varianti411 – 4111S → R.
    Corresponds to variant rs910857 [ dbSNP | Ensembl ].
    VAR_063699
    Natural varianti413 – 4131V → A in BVVLS1; may cause a mild form of the disease. 1 Publication
    VAR_063700
    Natural varianti457 – 4571F → L in BVVLS1. 1 Publication
    VAR_063701

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei401 – 41515ASWVL…SYVKV → SIRPVGLLPLRTPHP in isoform 2. 1 PublicationVSP_003814Add
    BLAST
    Alternative sequencei416 – 46954Missing in isoform 2. 1 PublicationVSP_003815Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK074650 mRNA. Translation: BAC11113.1.
    AK291706 mRNA. Translation: BAF84395.1.
    AL118502 Genomic DNA. Translation: CAH73077.2.
    AL118502 Genomic DNA. Translation: CAH73078.2.
    BC009750 mRNA. Translation: AAH09750.2.
    CCDSiCCDS13007.1. [Q9NQ40-1]
    RefSeqiNP_212134.3. NM_033409.3. [Q9NQ40-1]
    XP_005260712.1. XM_005260655.3. [Q9NQ40-1]
    UniGeneiHs.283865.

    Genome annotation databases

    EnsembliENST00000217254; ENSP00000217254; ENSG00000101276. [Q9NQ40-1]
    ENST00000381944; ENSP00000371370; ENSG00000101276. [Q9NQ40-2]
    GeneIDi113278.
    KEGGihsa:113278.
    UCSCiuc002wed.4. human. [Q9NQ40-1]
    uc002wee.2. human. [Q9NQ40-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AK074650 mRNA. Translation: BAC11113.1.
    AK291706 mRNA. Translation: BAF84395.1.
    AL118502 Genomic DNA. Translation: CAH73077.2.
    AL118502 Genomic DNA. Translation: CAH73078.2.
    BC009750 mRNA. Translation: AAH09750.2.
    CCDSiCCDS13007.1. [Q9NQ40-1]
    RefSeqiNP_212134.3. NM_033409.3. [Q9NQ40-1]
    XP_005260712.1. XM_005260655.3. [Q9NQ40-1]
    UniGeneiHs.283865.

    3D structure databases

    ProteinModelPortaliQ9NQ40.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000217254.

    Protein family/group databases

    TCDBi9.A.53.1.2. the eukaryotic riboflavin transporter (e-rft) family.

    PTM databases

    PhosphoSiteiQ9NQ40.

    Polymorphism and mutation databases

    BioMutaiSLC52A3.
    DMDMi82654931.

    Proteomic databases

    PRIDEiQ9NQ40.

    Protocols and materials databases

    DNASUi113278.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000217254; ENSP00000217254; ENSG00000101276. [Q9NQ40-1]
    ENST00000381944; ENSP00000371370; ENSG00000101276. [Q9NQ40-2]
    GeneIDi113278.
    KEGGihsa:113278.
    UCSCiuc002wed.4. human. [Q9NQ40-1]
    uc002wee.2. human. [Q9NQ40-2]

    Organism-specific databases

    CTDi113278.
    GeneCardsiGC20M000741.
    H-InvDBHIX0015557.
    HGNCiHGNC:16187. SLC52A3.
    HPAiHPA049391.
    MIMi211500. phenotype.
    211530. phenotype.
    613350. gene.
    neXtProtiNX_Q9NQ40.
    Orphaneti97229. Riboflavin transporter deficiency.
    PharmGKBiPA25764.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG326568.
    GeneTreeiENSGT00390000003774.
    HOGENOMiHOG000247012.
    HOVERGENiHBG051170.
    InParanoidiQ9NQ40.
    KOiK14620.
    OMAiWVLDGHH.
    OrthoDBiEOG7XDBFX.
    PhylomeDBiQ9NQ40.
    TreeFamiTF314820.

    Enzyme and pathway databases

    ReactomeiREACT_11070. Vitamin B2 (riboflavin) metabolism.

    Miscellaneous databases

    GeneWikiiC20orf54.
    GenomeRNAii113278.
    NextBioi78824.
    PROiQ9NQ40.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9NQ40.
    CleanExiHS_C20orf54.
    ExpressionAtlasiQ9NQ40. baseline and differential.
    GenevestigatoriQ9NQ40.

    Family and domain databases

    InterProiIPR009357. Endogenous_retrovirus_rcpt.
    [Graphical view]
    PANTHERiPTHR12929. PTHR12929. 1 hit.
    PfamiPF06237. DUF1011. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Mammary gland and Placenta.
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS LEU-267; MET-278 AND VAL-303.
      Tissue: Pancreas.
    4. "Identification and functional characterization of rat riboflavin transporter 2."
      Yamamoto S., Inoue K., Ohta K.Y., Fukatsu R., Maeda J.Y., Yoshida Y., Yuasa H.
      J. Biochem. 145:437-443(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    5. "Identification and comparative functional characterization of a new human riboflavin transporter hRFT3 expressed in the brain."
      Yao Y., Yonezawa A., Yoshimatsu H., Masuda S., Katsura T., Inui K.
      J. Nutr. 140:1220-1226(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Role of cysteine residues in cell surface expression of the human riboflavin transporter-2 (hRFT2) in intestinal epithelial cells."
      Subramanian V.S., Rapp L., Marchant J.S., Said H.M.
      Am. J. Physiol. 301:G100-G109(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TOPOLOGY, DISULFIDE BOND, MUTAGENESIS OF CYS-326; CYS-386; ARG-455; CYS-463 AND CYS-467.
    7. "Brown-Vialetto-Van Laere and Fazio Londe syndrome is associated with a riboflavin transporter defect mimicking mild MADD: a new inborn error of metabolism with potential treatment."
      Bosch A.M., Abeling N.G., Ijlst L., Knoester H., van der Pol W.L., Stroomer A.E., Wanders R.J., Visser G., Wijburg F.A., Duran M., Waterham H.R.
      J. Inherit. Metab. Dis. 34:159-164(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN FALOND.
    8. "Functional involvement of RFVT3/SLC52A3 in intestinal riboflavin absorption."
      Yoshimatsu H., Yonezawa A., Yao Y., Sugano K., Nakagawa S., Omura T., Matsubara K.
      Am. J. Physiol. 306:G102-G110(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Brown-Vialetto-Van Laere syndrome, a ponto-bulbar palsy with deafness, is caused by mutations in c20orf54."
      Green P., Wiseman M., Crow Y.J., Houlden H., Riphagen S., Lin J.P., Raymond F.L., Childs A.M., Sheridan E., Edwards S., Josifova D.J.
      Am. J. Hum. Genet. 86:485-489(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS BVVLS1 LYS-36; TRP-132; LEU-224; ALA-413 AND LEU-457, VARIANT MET-350.

    Entry informationi

    Entry nameiS52A3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQ40
    Secondary accession number(s): A8K6P1
    , Q5W1A0, Q5W1A1, Q8NCL7, Q96GD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 10, 2003
    Last sequence update: November 22, 2005
    Last modified: April 29, 2015
    This is version 115 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-5 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.