S52A3_BOVIN
ID S52A3_BOVIN Reviewed; 467 AA.
AC Q5E9R1; Q3T066;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
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DR EMBL; BT020859; AAX08876.1; -; mRNA.
DR EMBL; BC102546; AAI02547.1; -; mRNA.
DR RefSeq; NP_001014864.1; NM_001014864.1.
DR RefSeq; XP_010809721.1; XM_010811419.2.
DR RefSeq; XP_010809722.1; XM_010811420.2.
DR RefSeq; XP_010809723.1; XM_010811421.2.
DR RefSeq; XP_015329621.1; XM_015474135.1.
DR AlphaFoldDB; Q5E9R1; -.
DR STRING; 9913.ENSBTAP00000005194; -.
DR PaxDb; Q5E9R1; -.
DR Ensembl; ENSBTAT00000005194; ENSBTAP00000005194; ENSBTAG00000003977.
DR Ensembl; ENSBTAT00000082893; ENSBTAP00000070838; ENSBTAG00000003977.
DR Ensembl; ENSBTAT00000084768; ENSBTAP00000057599; ENSBTAG00000003977.
DR GeneID; 507459; -.
DR KEGG; bta:507459; -.
DR CTD; 113278; -.
DR VEuPathDB; HostDB:ENSBTAG00000003977; -.
DR VGNC; VGNC:34902; SLC52A3.
DR eggNOG; KOG4255; Eukaryota.
DR GeneTree; ENSGT00390000003774; -.
DR HOGENOM; CLU_034789_1_0_1; -.
DR InParanoid; Q5E9R1; -.
DR OMA; NDGWTIH; -.
DR OrthoDB; 757564at2759; -.
DR TreeFam; TF314820; -.
DR Reactome; R-BTA-196843; Vitamin B2 (riboflavin) metabolism.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000003977; Expressed in spermatocyte and 38 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..467
FT /note="Solute carrier family 52, riboflavin transporter,
FT member 3"
FT /id="PRO_0000399791"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..43
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..105
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..220
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..333
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..394
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..467
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 266..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4FZU9"
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 CONFLICT 252
FT /note="I -> K (in Ref. 2; AAI02547)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="G -> W (in Ref. 2; AAI02547)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="L -> F (in Ref. 2; AAI02547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 50530 MW; 803F0756FEE6CC7D CRC64;
MAFLIHLLVC TFGMGSWVAI NGLWVELPLL VTELPEGWYL PSYLTVIIQL ANVGPLLVTL
LHHFRPGCLS EVAVVFTVLG VGTIACTLFA FLWNVTSWVL GSRHSIAFLV LTFFLALVDC
TSSVTFLPFM SRLPTYYLTT FFVGEGLSGL LPALVALAQG SGLTTCVNVT EISATTLSPE
TTRNMDSPQG ASSTLVSKLA GTAPSGIHLE SRYLPANFSP LVFFLLLSFM MACCFISFFF
LQRQPKRWEA SIEDLLTSQV TLNSIRPQEG KDLGPPEESG KAQDPPEEKT APQHLAHLTF
IYVLVAFVNA LTNGVLPSVQ TYSCLSYGPV AYHLSATLSS MASPLTCFLS IFLPNRSLPF
LGVLAVLGTS FGAYNMAMAV MSPCPFMQGH WGGEVLIVVS WVLFTGCLSY VKVMLGVILR
DHSRSALLWC GAAVQLGSLL GAVVMFPLVN VLRLFSSADF CSLQCSA
