ID   S52A2_PAPHA             Reviewed;         448 AA.
AC   Q863Y8;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Solute carrier family 52, riboflavin transporter, member 2;
DE   AltName: Full=Porcine endogenous retrovirus A receptor 2;
DE            Short=PERV-A receptor 2;
DE   AltName: Full=Protein GPR172B;
DE   AltName: Full=Riboflavin transporter 1;
DE            Short=RFT1;
GN   Name=SLC52A2; Synonyms=GPR172B, PAR2, RFT1;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION AS A VIRAL RECEPTOR.
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).
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   -!- 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   -!- 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   -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC       {ECO:0000305}.
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DR   EMBL; AY070776; AAL59884.1; -; mRNA.
DR   AlphaFoldDB; Q863Y8; -.
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:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Host cell receptor for virus entry; Membrane;
KW   Receptor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..448
FT                   /note="Solute carrier family 52, riboflavin transporter,
FT                   member 2"
FT                   /id="PRO_0000042634"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          228..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   448 AA;  46290 MW;  8BBC7FB8FE36B941 CRC64;
     MAAPTLGHLV LTHLLVALLG MGSWAAVNGI WVELPVVVKH LPEGWSLPSY LSVVVALGNL
     GLLVVTLWRR LAPGKGERVP IQVVQVLSVV GTALLAPLWH HVAPVAGQLH SVAFLTLALV
     LALACCTSNV TFLPFLSHLP PPFLRSFFLG QGLSALLPCV LALVQGVGRL ECSPAPTNGT
     SGPPLNFPER FPASTFYWAL TALLVTSAAA FQGLLLLLPS LPSVTTGGAG PELPLGSPGA
     EEEEKEEEEA LPLQEPPSQA AGTIPGPDPE AHQLFSAHGA FLLGLLAITS ALTNGVLPAV
     QSFSCLPYGR LAYHLAVVLG SAANPLACFL AMGVLCRSLA GLVGLSLLGM LFGAYLMVLA
     ILSPCPPLVG TTAGVVLVVL SWVLCLCVFS YVKVAASSLL HGGGRPALLA AGVAIQMGSL
     LGAGTMFPPT SIYHVFQSRK DCVDPCGP