S52A2_MOUSE
ID S52A2_MOUSE Reviewed; 450 AA.
AC Q9D8F3; Q8CCV8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Solute carrier family 52, riboflavin transporter, member 2;
DE AltName: Full=Porcine endogenous retrovirus A receptor 2 homolog;
DE Short=PERV-A receptor 2 homolog;
DE AltName: Full=Protein GPR172B;
DE AltName: Full=Riboflavin transporter 1;
DE Short=mRFT1;
GN Name=Slc52a2; Synonyms=Gpr172b, Rft1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Small intestine, and Testis;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; 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).
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. May also act as a receptor for 4-
CC hydroxybutyrate. {ECO:0000250|UniProtKB:Q9HAB3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC ChEBI:CHEBI:57986; Evidence={ECO:0000250|UniProtKB:Q9HAB3};
CC -!- ACTIVITY REGULATION: Riboflavin transport is Na(+)-independent but
CC moderately pH-sensitive (By similarity). Activity is strongly inhibited
CC by riboflavin analogs, such as lumiflavin (By similarity). Weakly
CC inhibited by flavin adenine dinucleotide (FAD) and flavin
CC mononucleotide (FMN) (By similarity). {ECO:0000250|UniProtKB:Q9HAB3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HAB3};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D8F3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8F3-2; Sequence=VSP_015940, VSP_015941;
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
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DR EMBL; AK008081; BAB25447.1; -; mRNA.
DR EMBL; AK029579; BAC26522.1; -; mRNA.
DR EMBL; AK032015; BAC27648.1; -; mRNA.
DR EMBL; AK080449; BAC37920.1; -; mRNA.
DR EMBL; AK142597; BAE25123.1; -; mRNA.
DR EMBL; AK152335; BAE31133.1; -; mRNA.
DR EMBL; AK161447; BAE36401.1; -; mRNA.
DR EMBL; BC016264; AAH16264.1; -; mRNA.
DR CCDS; CCDS27575.1; -. [Q9D8F3-1]
DR RefSeq; NP_083919.1; NM_029643.3. [Q9D8F3-1]
DR RefSeq; XP_006521214.1; XM_006521151.3. [Q9D8F3-1]
DR AlphaFoldDB; Q9D8F3; -.
DR IntAct; Q9D8F3; 1.
DR STRING; 10090.ENSMUSP00000023220; -.
DR GlyGen; Q9D8F3; 1 site.
DR iPTMnet; Q9D8F3; -.
DR PhosphoSitePlus; Q9D8F3; -.
DR EPD; Q9D8F3; -.
DR PaxDb; Q9D8F3; -.
DR PeptideAtlas; Q9D8F3; -.
DR PRIDE; Q9D8F3; -.
DR ProteomicsDB; 260910; -. [Q9D8F3-1]
DR ProteomicsDB; 260911; -. [Q9D8F3-2]
DR DNASU; 52710; -.
DR Ensembl; ENSMUST00000023220; ENSMUSP00000023220; ENSMUSG00000022560. [Q9D8F3-1]
DR GeneID; 52710; -.
DR KEGG; mmu:52710; -.
DR UCSC; uc007wkt.1; mouse. [Q9D8F3-2]
DR UCSC; uc007wku.1; mouse. [Q9D8F3-1]
DR CTD; 79581; -.
DR MGI; MGI:1289288; Slc52a2.
DR VEuPathDB; HostDB:ENSMUSG00000022560; -.
DR eggNOG; KOG4255; Eukaryota.
DR GeneTree; ENSGT00390000003774; -.
DR HOGENOM; CLU_034789_1_0_1; -.
DR InParanoid; Q9D8F3; -.
DR OMA; WCGISIQ; -.
DR OrthoDB; 757564at2759; -.
DR PhylomeDB; Q9D8F3; -.
DR TreeFam; TF314820; -.
DR Reactome; R-MMU-196843; Vitamin B2 (riboflavin) metabolism.
DR BioGRID-ORCS; 52710; 9 hits in 77 CRISPR screens.
DR ChiTaRS; Slc52a2; mouse.
DR PRO; PR:Q9D8F3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9D8F3; protein.
DR Bgee; ENSMUSG00000022560; Expressed in external carotid artery and 249 other tissues.
DR Genevisible; Q9D8F3; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0062124; F:4-hydroxybutyrate receptor activity; ISS:UniProtKB.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0032218; P:riboflavin transport; ISS:UniProtKB.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929; PTHR12929; 1.
DR Pfam; PF06237; DUF1011; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..450
FT /note="Solute carrier family 52, riboflavin transporter,
FT member 2"
FT /id="PRO_0000042633"
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 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 227..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 340..351
FT /note="SLAGLCGLSLLG -> CSRTPKPPWGRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015940"
FT VAR_SEQ 352..450
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015941"
SQ SEQUENCE 450 AA; 46864 MW; 7A2CCCCCDD337791 CRC64;
MAAPPLGRLV LTHLLVALFG MGSWAAVNGI WVELPVVVKE LPEGWSLPSY LSVLVALGNL
GLLLVTLWRR LARGKGEQVP IRVVQGLGIV GTGLLASLWN HVAPVAGKPY SVAFLTLAFV
LALACCASNV TFLPFLSHLP PPFLRSFFLG QGLSALLPCV LALGQGVGRL ECLHVPANRT
TGPPIEVSPI NFPERFSATT FFWVLTALLG TSAAAFQGLL LLLPSPTSEP TTGTGLRVET
PGTEEEEEEE EASPLQEPPG QVAGIVSSPD PKAHQLFSSR SACLLGLLAI TNALTNGVLP
AVQSFSCLPY GRLAYHLAVV LGSCANPLAC FLAMAVLCRS LAGLCGLSLL GMLLGSYLMT
LAALSPCPPL VGTSAGVVLV VLSWVLCAGT FSYIKVAISS MLHSGGRPAL LAAGVAIQVG
SLLGAVAMFP PTSIYRVFRS GKDCVDQCGL
