S52A3_MOUSE
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 03-AUG-2022, entry version 137.
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 particulary
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 GlyGen; Q9D6X5; 2 sites.
DR iPTMnet; Q9D6X5; -.
DR PhosphoSitePlus; Q9D6X5; -.
DR MaxQB; Q9D6X5; -.
DR PaxDb; Q9D6X5; -.
DR PeptideAtlas; Q9D6X5; -.
DR PRIDE; Q9D6X5; -.
DR ProteomicsDB; 260799; -. [Q9D6X5-1]
DR Antibodypedia; 54121; 67 antibodies from 14 providers.
DR DNASU; 69698; -.
DR Ensembl; ENSMUST00000073228; ENSMUSP00000072961; ENSMUSG00000027463. [Q9D6X5-1]
DR Ensembl; ENSMUST00000109858; ENSMUSP00000105484; ENSMUSG00000027463. [Q9D6X5-2]
DR Ensembl; ENSMUST00000109859; ENSMUSP00000105485; ENSMUSG00000027463. [Q9D6X5-2]
DR Ensembl; ENSMUST00000109861; ENSMUSP00000105487; ENSMUSG00000027463. [Q9D6X5-1]
DR GeneID; 69698; -.
DR KEGG; mmu:69698; -.
DR UCSC; uc008neu.2; mouse. [Q9D6X5-1]
DR UCSC; uc012cga.1; mouse. [Q9D6X5-2]
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; NDGWTIH; -.
DR OrthoDB; 757564at2759; -.
DR PhylomeDB; Q9D6X5; -.
DR TreeFam; TF314820; -.
DR Reactome; R-MMU-196843; Vitamin B2 (riboflavin) metabolism.
DR BioGRID-ORCS; 69698; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q9D6X5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D6X5; protein.
DR Bgee; ENSMUSG00000027463; Expressed in intestinal villus and 139 other tissues.
DR Genevisible; Q9D6X5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA: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; PTHR12929; 1.
DR Pfam; PF06237; DUF1011; 1.
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
