S52A2_PIG
ID S52A2_PIG Reviewed; 446 AA.
AC Q863Y7;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Solute carrier family 52, riboflavin transporter, member 2;
DE AltName: Full=Endogenous retrovirus A receptor;
DE AltName: Full=Protein GPR172B;
DE AltName: Full=Riboflavin transporter 1;
GN Name=SLC52A2; Synonyms=GPR172B, RFT1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
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 porcine
CC endogenous retrovirus (PERV-A), acts as a cell receptor to retroviral
CC envelopes. {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; AY134475; AAM95457.1; -; mRNA.
DR RefSeq; NP_001004033.1; NM_001004033.1.
DR AlphaFoldDB; Q863Y7; -.
DR STRING; 9823.ENSSSCP00000006317; -.
DR PaxDb; Q863Y7; -.
DR GeneID; 445519; -.
DR KEGG; ssc:445519; -.
DR CTD; 79581; -.
DR eggNOG; KOG4255; Eukaryota.
DR InParanoid; Q863Y7; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..446
FT /note="Solute carrier family 52, riboflavin transporter,
FT member 2"
FT /id="PRO_0000042635"
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 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 228..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 45828 MW; C4DC41C711E274E0 CRC64;
MAAPTLARLV LTHLLVALFG MGSWAAINGI WVELPVVVKD LPEGWSLPSY LSVLVALGNL
GLLVVTLWRR LAPGKGERAP IQVVQALSVV GTALLAPLWQ HLTVMAGQVH SVAFLALTFV
LALACCASNV TYLPFLSRLP PPFLRSFFLG QGLSALLPCV LALGQGVGRL ECPPAPANGT
PGPPLDFPER FSASAFFGAL TALLVISAAA FQGLLLLLPS LVSIPTEGSG TGLRGGAPGV
EEEEEEEASP LQEPPSQAAG NTPSPDPAAH RLLSARGACL LGLLATTSAL TNGVLPAVQS
YSSLPYGRLA YHLAVVLGSA SNPLACFLAM GILCRSLAGL GGLSLLGTLF GAYLMALAIL
SPCPPLVGTS AGMVLVVVLW ALCLGVFSYV KVATSSLLHG GGPPALLAAG VAIQVGSLLG
AVTMFPPTSI YRVFQSRKDC VDPCEP
