ID   S52A3_MOUSE             Reviewed;         460 AA.
AC   Q9D6X5; A2AQU3; Q3TDJ6; Q3U328; Q8CE36; Q91WB9;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Solute carrier family 52, riboflavin transporter, member 3;
DE   AltName: Full=Riboflavin transporter 2;
DE            Short=RFT2;
GN   Name=Slc52a3; Synonyms=Rft2, RFVT3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Salivary gland;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   TISSUE SPECIFICITY.
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).
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. {ECO:0000250|UniProtKB:Q9NQ40}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC         ChEBI:CHEBI:57986; Evidence={ECO:0000250|UniProtKB:Q9NQ40};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NQ40};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D6X5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D6X5-2; Sequence=VSP_003816, VSP_003817;
CC   -!- TISSUE SPECIFICITY: Within the small intestine, it is particularly
CC       expressed in the jujenum and the ileum. Almost negligible expression in
CC       the stomach, duodenum, and large intestine.
CC       {ECO:0000269|PubMed:24264046}.
CC   -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC       {ECO:0000305}.
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DR   EMBL; AK009850; BAB26542.1; -; mRNA.
DR   EMBL; AK029091; BAC26290.1; -; mRNA.
DR   EMBL; AK154970; BAE32962.1; -; mRNA.
DR   EMBL; AK170158; BAE41605.1; -; mRNA.
DR   EMBL; AL845161; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466551; EDL05945.1; -; Genomic_DNA.
DR   EMBL; BC016127; AAH16127.1; -; mRNA.
DR   CCDS; CCDS16876.1; -. [Q9D6X5-1]
DR   CCDS; CCDS50749.1; -. [Q9D6X5-2]
DR   RefSeq; NP_001158291.1; NM_001164819.1. [Q9D6X5-1]
DR   RefSeq; NP_001158292.1; NM_001164820.1. [Q9D6X5-2]
DR   RefSeq; NP_081448.2; NM_027172.3. [Q9D6X5-1]
DR   AlphaFoldDB; Q9D6X5; -.
DR   BioGRID; 213623; 1.
DR   IntAct; Q9D6X5; 1.
DR   MINT; Q9D6X5; -.
DR   STRING; 10090.ENSMUSP00000072961; -.
DR   GlyCosmos; Q9D6X5; 2 sites, No reported glycans.
DR   GlyGen; Q9D6X5; 2 sites.
DR   iPTMnet; Q9D6X5; -.
DR   PhosphoSitePlus; Q9D6X5; -.
DR   SwissPalm; Q9D6X5; -.
DR   MaxQB; Q9D6X5; -.
DR   PaxDb; 10090-ENSMUSP00000072961; -.
DR   PeptideAtlas; Q9D6X5; -.
DR   ProteomicsDB; 260799; -. [Q9D6X5-1]
DR   Antibodypedia; 54121; 104 antibodies from 15 providers.
DR   DNASU; 69698; -.
DR   Ensembl; ENSMUST00000073228.12; ENSMUSP00000072961.6; ENSMUSG00000027463.15. [Q9D6X5-1]
DR   Ensembl; ENSMUST00000109858.2; ENSMUSP00000105484.2; ENSMUSG00000027463.15. [Q9D6X5-2]
DR   Ensembl; ENSMUST00000109859.9; ENSMUSP00000105485.3; ENSMUSG00000027463.15. [Q9D6X5-2]
DR   Ensembl; ENSMUST00000109861.8; ENSMUSP00000105487.2; ENSMUSG00000027463.15. [Q9D6X5-1]
DR   GeneID; 69698; -.
DR   KEGG; mmu:69698; -.
DR   UCSC; uc008neu.2; mouse. [Q9D6X5-1]
DR   UCSC; uc012cga.1; mouse. [Q9D6X5-2]
DR   AGR; MGI:1916948; -.
DR   CTD; 113278; -.
DR   MGI; MGI:1916948; Slc52a3.
DR   VEuPathDB; HostDB:ENSMUSG00000027463; -.
DR   eggNOG; KOG4255; Eukaryota.
DR   GeneTree; ENSGT00390000003774; -.
DR   HOGENOM; CLU_1111093_0_0_1; -.
DR   InParanoid; Q9D6X5; -.
DR   OMA; CGAAAQM; -.
DR   OrthoDB; 5477759at2759; -.
DR   PhylomeDB; Q9D6X5; -.
DR   TreeFam; TF314820; -.
DR   Reactome; R-MMU-196843; Vitamin B2 (riboflavin) metabolism.
DR   BioGRID-ORCS; 69698; 2 hits in 76 CRISPR screens.
DR   PRO; PR:Q9D6X5; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9D6X5; Protein.
DR   Bgee; ENSMUSG00000027463; Expressed in intestinal villus and 141 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IMP:MGI.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; IMP:MGI.
DR   GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR   GO; GO:0072388; P:flavin adenine dinucleotide biosynthetic process; IMP:MGI.
DR   GO; GO:0006771; P:riboflavin metabolic process; IMP:MGI.
DR   GO; GO:0032218; P:riboflavin transport; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   InterPro; IPR009357; Riboflavin_transptr.
DR   PANTHER; PTHR12929; SOLUTE CARRIER FAMILY 52; 1.
DR   PANTHER; PTHR12929:SF4; SOLUTE CARRIER FAMILY 52, RIBOFLAVIN TRANSPORTER, MEMBER 3; 1.
DR   Pfam; PF06237; SLC52_ribofla_tr; 1.
DR   Genevisible; Q9D6X5; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..460
FT                   /note="Solute carrier family 52, riboflavin transporter,
FT                   member 3"
FT                   /id="PRO_0000042637"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..37
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..211
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        233..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        348..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..387
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        409..418
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        419..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        440..460
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4FZU9"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
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        377..454
FT                   /evidence="ECO:0000250|UniProtKB:Q9NQ40"
FT   VAR_SEQ         187..250
FT                   /note="GNLSPSLPSPSWHQESRYLAPRFSPLLFFLLLSFLTGCCLVAFFLLQRQPWG
FT                   RQGSIEDLLHSQ -> VAVIPGGAHSVGDRLWGLQYGHGCYEPLPCPAGSLGWRSPYRA
FT                   LLGAVCSLSQLCQGDAGCDLA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003816"
FT   VAR_SEQ         251..460
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003817"
FT   CONFLICT        81
FT                   /note="V -> L (in Ref. 1; BAE41605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="T -> N (in Ref. 1; BAB26542)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="S -> P (in Ref. 1; BAE41605)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="G -> C (in Ref. 1; BAB26542)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        286
FT                   /note="L -> I (in Ref. 1; BAE41605)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   460 AA;  49559 MW;  7F299163AD3C884E CRC64;
     MAFLTHLLVC VFGMGSWVAI NGLWVELPLL VTELPEAWYL PSYLTVVIQL ANIGPLLVTL
     MHRFRPGCLS EVPVIFLILC VGTAACILLA FLWNVTSWIQ GGQHSVAFIV LTFFLALVDC
     TSSVTFLPFM SQLPTYYLTT FFIGEGLSGL LPALVALVQG SGITTCVNVT ETPGTTLNTM
     ETPITQGNLS PSLPSPSWHQ ESRYLAPRFS PLLFFLLLSF LTGCCLVAFF LLQRQPWGRQ
     GSIEDLLHSQ VTLHSIRPRD TEDTSSLGAP VSSPGKGSVE ASVASLRPAQ LAFIYSVVAF
     VNALTNGVLP SVQTYSCLPY GPVAYHLSAT LSSVASPLAC FLPIFLPNRS LLFLGVLTVL
     GTGFGAYNMA MAAMSPCPVL QGHWGGEVLI VLSWVLFAAC LSYVKVMLGV ILRDRSRSAL
     LWCGAAVQLG SLIGALLMFP LVNVLKLFSS ADYCSLDCSV
//