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Solute carrier family 52, riboflavin transporter, member 1 (Porcine endogenous retrovirus A receptor 2) (PERV-A receptor 2) (Protein GPR172B) (Riboflavin transporter 1) (hRFT1)

 S52A1_HUMAN             Reviewed;         448 AA.
Q9NWF4; B5MEV1; B5MEV2; Q6P9E0; Q86UT0;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
07-NOV-2018, entry version 122.
RecName: Full=Solute carrier family 52, riboflavin transporter, member 1;
AltName: Full=Porcine endogenous retrovirus A receptor 2;
Short=PERV-A receptor 2;
AltName: Full=Protein GPR172B;
AltName: Full=Riboflavin transporter 1;
Short=hRFT1;
Name=SLC52A1 {ECO:0000312|HGNC:HGNC:30225};
Synonyms=GPR172B, PAR2, RFT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
FUNCTION AS A VIRAL RECEPTOR.
PubMed=12740431; DOI=10.1073/pnas.1138025100;
Ericsson T.A., Takeuchi Y., Templin C., Quinn G., Farhadian S.F.,
Wood J.C., Oldmixon B.A., Suling K.M., Ishii J.K., Kitagawa Y.,
Miyazawa T., Salomon D.R., Weiss R.A., Patience C.;
"Identification of receptors for pig endogenous retrovirus.";
Proc. Natl. Acad. Sci. U.S.A. 100:6759-6764(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-70,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18632736; DOI=10.1152/ajpcell.00019.2008;
Yonezawa A., Masuda S., Katsura T., Inui K.;
"Identification and functional characterization of a novel human and
rat riboflavin transporter, RFT1.";
Am. J. Physiol. 295:C632-C641(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-70.
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-70.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ARG-70 AND VAL-271.
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=20463145; DOI=10.3945/jn.110.122911;
Yao Y., Yonezawa A., Yoshimatsu H., Masuda S., Katsura T., Inui K.;
"Identification and comparative functional characterization of a new
human riboflavin transporter hRFT3 expressed in the brain.";
J. Nutr. 140:1220-1226(2010).
[8]
VARIANTS ARG-70; VAL-271 AND MET-296, CHARACTERIZATION OF VARIANTS
ARG-70 AND MET-296, AND INVOLVEMENT IN RBFVD.
PubMed=21089064; DOI=10.1002/humu.21399;
Ho G., Yonezawa A., Masuda S., Inui K., Sim K.G., Carpenter K.,
Olsen R.K., Mitchell J.J., Rhead W.J., Peters G., Christodoulou J.;
"Maternal riboflavin deficiency, resulting in transient neonatal-onset
glutaric aciduria Type 2, is caused by a microdeletion in the
riboflavin transporter gene GPR172B.";
Hum. Mutat. 32:E1976-E1984(2011).
[9]
VARIANT VAL-386.
PubMed=28190456; DOI=10.1016/j.ajhg.2017.01.024;
Wiessner M., Roos A., Munn C.J., Viswanathan R., Whyte T., Cox D.,
Schoser B., Sewry C., Roper H., Phadke R., Marini Bettolo C.,
Barresi R., Charlton R., Boennemann C.G., Abath Neto O., Reed U.C.,
Zanoteli E., Araujo Martins Moreno C., Ertl-Wagner B., Stucka R.,
De Goede C., Borges da Silva T., Hathazi D., Dell'Aica M.,
Zahedi R.P., Thiele S., Mueller J., Kingston H., Mueller S.,
Curtis E., Walter M.C., Strom T.M., Straub V., Bushby K., Muntoni F.,
Swan L.E., Lochmueller H., Senderek J.;
"Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause
Congenital muscular dystrophy with cataracts and mild cognitive
impairment.";
Am. J. Hum. Genet. 100:523-536(2017).
-!- FUNCTION: Riboflavin transporter. Riboflavin transport is Na(+)-
independent but moderately pH-sensitive. Activity is strongly
inhibited by riboflavin analogs, such as lumiflavin. Weakly
inhibited by flavin adenine dinucleotide (FAD). In case of
infection by retroviruses, acts as a cell receptor to retroviral
envelopes similar to the porcine endogenous retrovirus (PERV-A).
{ECO:0000269|PubMed:12740431, ECO:0000269|PubMed:20463145}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.38 uM for riboflavin {ECO:0000269|PubMed:20463145};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18632736,
ECO:0000269|PubMed:20463145}; Multi-pass membrane protein
{ECO:0000269|PubMed:18632736, ECO:0000269|PubMed:20463145}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NWF4-1; Sequence=Displayed;
Name=2; Synonyms=RFT1sv;
IsoId=Q9NWF4-2; Sequence=VSP_039888, VSP_039889;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the
testis, placenta and small intestine. Expressed at lower level in
other tissues. {ECO:0000269|PubMed:12740431,
ECO:0000269|PubMed:18632736, ECO:0000269|PubMed:20463145}.
-!- DISEASE: Riboflavin deficiency (RBFVD) [MIM:615026]: A disorder
caused by a primary defect in riboflavin metabolism, or by dietary
riboflavin deficiency. Riboflavin deficiency during pregnancy
results in hypoglycemia, metabolic acidosis, dicarboxylic aciduria
and elevated plasma acylcarnitine levels in the newborn. Treatment
with oral riboflavin results in complete resolution of the
clinical and biochemical findings. {ECO:0000269|PubMed:21089064}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the riboflavin transporter family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY070775; AAL59883.1; -; mRNA.
EMBL; AB362533; BAG71128.1; -; mRNA.
EMBL; AB362534; BAG71129.1; -; mRNA.
EMBL; AK000922; BAA91427.1; -; mRNA.
EMBL; AC012146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW90363.1; -; Genomic_DNA.
EMBL; CH471108; EAW90364.1; -; Genomic_DNA.
EMBL; BC060810; AAH60810.1; -; mRNA.
EMBL; BC092473; AAH92473.1; -; mRNA.
CCDS; CCDS11066.1; -. [Q9NWF4-1]
RefSeq; NP_001098047.1; NM_001104577.1. [Q9NWF4-1]
RefSeq; NP_060456.3; NM_017986.3. [Q9NWF4-1]
RefSeq; XP_011522253.1; XM_011523951.1. [Q9NWF4-1]
UniGene; Hs.632247; -.
ProteinModelPortal; Q9NWF4; -.
IntAct; Q9NWF4; 8.
STRING; 9606.ENSP00000254853; -.
TCDB; 2.A.125.1.1; the eukaryotic riboflavin transporter (e-rft) family.
iPTMnet; Q9NWF4; -.
PhosphoSitePlus; Q9NWF4; -.
BioMuta; SLC52A1; -.
DMDM; 308153487; -.
PaxDb; Q9NWF4; -.
PeptideAtlas; Q9NWF4; -.
PRIDE; Q9NWF4; -.
ProteomicsDB; 82930; -.
ProteomicsDB; 82931; -. [Q9NWF4-2]
DNASU; 55065; -.
Ensembl; ENST00000254853; ENSP00000254853; ENSG00000132517. [Q9NWF4-1]
Ensembl; ENST00000424747; ENSP00000399979; ENSG00000132517. [Q9NWF4-1]
GeneID; 55065; -.
KEGG; hsa:55065; -.
UCSC; uc002gao.5; human. [Q9NWF4-1]
CTD; 55065; -.
DisGeNET; 55065; -.
EuPathDB; HostDB:ENSG00000132517.14; -.
GeneCards; SLC52A1; -.
H-InvDB; HIX0023130; -.
HGNC; HGNC:30225; SLC52A1.
HPA; CAB011449; -.
MalaCards; SLC52A1; -.
MIM; 607883; gene.
MIM; 615026; phenotype.
neXtProt; NX_Q9NWF4; -.
OpenTargets; ENSG00000132517; -.
Orphanet; 411712; Maternal riboflavin deficiency.
PharmGKB; PA134991217; -.
eggNOG; KOG4255; Eukaryota.
eggNOG; ENOG410YE1U; LUCA.
GeneTree; ENSGT00390000003774; -.
HOGENOM; HOG000247012; -.
HOVERGEN; HBG051170; -.
InParanoid; Q9NWF4; -.
KO; K22117; -.
OMA; SVNSLWV; -.
OrthoDB; EOG091G0BZA; -.
PhylomeDB; Q9NWF4; -.
TreeFam; TF314820; -.
Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
GenomeRNAi; 55065; -.
PRO; PR:Q9NWF4; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000132517; Expressed in 66 organ(s), highest expression level in placenta.
CleanEx; HS_GPR172B; -.
ExpressionAtlas; Q9NWF4; baseline and differential.
Genevisible; Q9NWF4; HS.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB.
InterPro; IPR009357; Riboflavin_transptr.
PANTHER; PTHR12929; PTHR12929; 1.
Pfam; PF06237; DUF1011; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Host cell receptor for virus entry; Membrane; Polymorphism; Receptor;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 448 Solute carrier family 52, riboflavin
transporter, member 1.
/FTId=PRO_0000042632.
TRANSMEM 14 34 Helical. {ECO:0000255}.
TRANSMEM 47 67 Helical. {ECO:0000255}.
TRANSMEM 79 99 Helical. {ECO:0000255}.
TRANSMEM 124 144 Helical. {ECO:0000255}.
TRANSMEM 147 167 Helical. {ECO:0000255}.
TRANSMEM 191 211 Helical. {ECO:0000255}.
TRANSMEM 280 300 Helical. {ECO:0000255}.
TRANSMEM 315 335 Helical. {ECO:0000255}.
TRANSMEM 342 362 Helical. {ECO:0000255}.
TRANSMEM 369 389 Helical. {ECO:0000255}.
TRANSMEM 407 427 Helical. {ECO:0000255}.
COMPBIAS 241 249 Poly-Glu.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 45 167 WSLPSYLSVVVALGNLGLLVVTLWRQLAPGKGEQVPIQVVQ
VLSVVGTALLAPLWHHVAPVAGQLHSVAFLTLALVLAMACC
TSNVTFLPFLSHLPPPFLRSFFLGQGLSALLPCVLALVQGV
-> EWEGGTGKRGAGMPRKVACGSSLSLSHCAPDMASFLPC
RLEPPLIPLCGCGAGKPGSAGGDPVEAAGPGQGRAGPHPGG
TGAECSGHSPAGPSVAPRGPSGRAAPLCGLPNSGLGVGNGL
LYL (in isoform 2).
{ECO:0000303|PubMed:18632736}.
/FTId=VSP_039888.
VAR_SEQ 168 448 Missing (in isoform 2).
{ECO:0000303|PubMed:18632736}.
/FTId=VSP_039889.
VARIANT 70 70 Q -> R (riboflavin transport is
unaffected; dbSNP:rs346822).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18632736,
ECO:0000269|PubMed:21089064,
ECO:0000269|Ref.5}.
/FTId=VAR_028361.
VARIANT 271 271 A -> V (in dbSNP:rs346821).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:21089064}.
/FTId=VAR_028362.
VARIANT 296 296 V -> M (riboflavin transport is
unaffected; dbSNP:rs2304445).
{ECO:0000269|PubMed:21089064}.
/FTId=VAR_028363.
VARIANT 386 386 L -> V (in dbSNP:rs187609896).
{ECO:0000269|PubMed:28190456}.
/FTId=VAR_079006.
SEQUENCE 448 AA; 46317 MW; B9D2EDEE75405668 CRC64;
MAAPTLGRLV LTHLLVALFG MGSWAAVNGI WVELPVVVKD LPEGWSLPSY LSVVVALGNL
GLLVVTLWRQ LAPGKGEQVP IQVVQVLSVV GTALLAPLWH HVAPVAGQLH SVAFLTLALV
LAMACCTSNV TFLPFLSHLP PPFLRSFFLG QGLSALLPCV LALVQGVGRL ECPPAPTNGT
SGPPLDFPER FPASTFFWAL TALLVTSAAA FRGLLLLLPS LPSVTTGGSG PELQLGSPGA
EEEEKEEEEA LPLQEPPSQA AGTIPGPDPE AHQLFSAHGA FLLGLMAFTS AVTNGVLPSV
QSFSCLPYGR LAYHLAVVLG SAANPLACFL AMGVLCRSLA GLVGLSLLGM LFGAYLMALA
ILSPCPPLVG TTAGVVLVVL SWVLCLCVFS YVKVAASSLL HGGGRPALLA AGVAIQVGSL
LGAGAMFPPT SIYHVFQSRK DCVDPCGP


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