S52A1_HUMAN
ID S52A1_HUMAN Reviewed; 448 AA.
AC Q9NWF4; B5MEV1; B5MEV2; Q6P9E0; Q86UT0;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Solute carrier family 52, riboflavin transporter, member 1;
DE AltName: Full=Porcine endogenous retrovirus A receptor 2 {ECO:0000303|PubMed:12740431};
DE Short=PERV-A receptor 2 {ECO:0000303|PubMed:12740431};
DE Short=huPAR-2 {ECO:0000303|PubMed:12740431};
DE AltName: Full=Protein GPR172B;
DE AltName: Full=Riboflavin transporter 1;
DE Short=hRFT1;
GN Name=SLC52A1 {ECO:0000312|HGNC:HGNC:30225}; Synonyms=GPR172B, PAR2, RFT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION AS A VIRAL RECEPTOR
RP (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ARG-70, FUNCTION,
RP TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18632736; DOI=10.1152/ajpcell.00019.2008;
RA Yonezawa A., Masuda S., Katsura T., Inui K.;
RT "Identification and functional characterization of a novel human and rat
RT riboflavin transporter, RFT1.";
RL Am. J. Physiol. 295:C632-C641(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-70.
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-70.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-70 AND
RP VAL-271.
RC TISSUE=Placenta;
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).
RN [7]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20463145; DOI=10.3945/jn.110.122911;
RA Yao Y., Yonezawa A., Yoshimatsu H., Masuda S., Katsura T., Inui K.;
RT "Identification and comparative functional characterization of a new human
RT riboflavin transporter hRFT3 expressed in the brain.";
RL J. Nutr. 140:1220-1226(2010).
RN [8]
RP VARIANTS ARG-70; VAL-271 AND MET-296, CHARACTERIZATION OF VARIANTS ARG-70
RP AND MET-296, AND INVOLVEMENT IN RBFVD.
RX PubMed=21089064; DOI=10.1002/humu.21399;
RA Ho G., Yonezawa A., Masuda S., Inui K., Sim K.G., Carpenter K., Olsen R.K.,
RA Mitchell J.J., Rhead W.J., Peters G., Christodoulou J.;
RT "Maternal riboflavin deficiency, resulting in transient neonatal-onset
RT glutaric aciduria Type 2, is caused by a microdeletion in the riboflavin
RT transporter gene GPR172B.";
RL Hum. Mutat. 32:E1976-E1984(2011).
RN [9]
RP VARIANT VAL-386.
RX PubMed=28190456; DOI=10.1016/j.ajhg.2017.01.024;
RA Wiessner M., Roos A., Munn C.J., Viswanathan R., Whyte T., Cox D.,
RA Schoser B., Sewry C., Roper H., Phadke R., Marini Bettolo C., Barresi R.,
RA Charlton R., Boennemann C.G., Abath Neto O., Reed U.C., Zanoteli E.,
RA Araujo Martins Moreno C., Ertl-Wagner B., Stucka R., De Goede C.,
RA Borges da Silva T., Hathazi D., Dell'Aica M., Zahedi R.P., Thiele S.,
RA Mueller J., Kingston H., Mueller S., Curtis E., Walter M.C., Strom T.M.,
RA Straub V., Bushby K., Muntoni F., Swan L.E., Lochmueller H., Senderek J.;
RT "Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause
RT Congenital muscular dystrophy with cataracts and mild cognitive
RT impairment.";
RL Am. J. Hum. Genet. 100:523-536(2017).
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 (PubMed:18632736, PubMed:20463145). Humans
CC are unable to synthesize vitamin B2/riboflavin and must obtain it via
CC intestinal absorption (PubMed:20463145). {ECO:0000269|PubMed:18632736,
CC ECO:0000269|PubMed:20463145, ECO:0000303|PubMed:20463145}.
CC -!- FUNCTION: (Microbial infection) May function as a cell receptor to
CC retroviral envelopes similar to the porcine endogenous retrovirus
CC (PERV-A). {ECO:0000305|PubMed:12740431}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC ChEBI:CHEBI:57986; Evidence={ECO:0000269|PubMed:18632736,
CC ECO:0000269|PubMed:20463145};
CC -!- ACTIVITY REGULATION: The activity is strongly inhibited by riboflavin
CC analogs, such as lumiflavin (PubMed:18632736, PubMed:20463145). Weakly
CC inhibited by flavin adenine dinucleotide (FAD) (PubMed:18632736,
CC PubMed:20463145). {ECO:0000269|PubMed:18632736,
CC ECO:0000269|PubMed:20463145}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.38 uM for riboflavin {ECO:0000269|PubMed:20463145};
CC -!- INTERACTION:
CC Q9NWF4; Q13520: AQP6; NbExp=3; IntAct=EBI-12904614, EBI-13059134;
CC Q9NWF4; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12904614, EBI-6942903;
CC Q9NWF4; P48165: GJA8; NbExp=3; IntAct=EBI-12904614, EBI-17458373;
CC Q9NWF4; P38484: IFNGR2; NbExp=3; IntAct=EBI-12904614, EBI-3905457;
CC Q9NWF4; Q16585: SGCB; NbExp=3; IntAct=EBI-12904614, EBI-5663627;
CC Q9NWF4; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-12904614, EBI-18037857;
CC Q9NWF4; P30825: SLC7A1; NbExp=3; IntAct=EBI-12904614, EBI-4289564;
CC Q9NWF4; Q7Z7N9: TMEM179B; NbExp=3; IntAct=EBI-12904614, EBI-11724423;
CC Q9NWF4; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-12904614, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12740431,
CC ECO:0000269|PubMed:18632736, ECO:0000269|PubMed:20463145}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NWF4-1; Sequence=Displayed;
CC Name=2; Synonyms=RFT1sv;
CC IsoId=Q9NWF4-2; Sequence=VSP_039888, VSP_039889;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the testis,
CC placenta and small intestine. Expressed at lower level in other
CC tissues. {ECO:0000269|PubMed:12740431, ECO:0000269|PubMed:18632736,
CC ECO:0000269|PubMed:20463145}.
CC -!- DISEASE: Riboflavin deficiency (RBFVD) [MIM:615026]: A disorder caused
CC by a primary defect in riboflavin metabolism, or by dietary riboflavin
CC deficiency. Riboflavin deficiency during pregnancy results in
CC hypoglycemia, metabolic acidosis, dicarboxylic aciduria and elevated
CC plasma acylcarnitine levels in the newborn. Treatment with oral
CC riboflavin results in complete resolution of the clinical and
CC biochemical findings. {ECO:0000269|PubMed:21089064}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC {ECO:0000305}.
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DR EMBL; AY070775; AAL59883.1; -; mRNA.
DR EMBL; AB362533; BAG71128.1; -; mRNA.
DR EMBL; AB362534; BAG71129.1; -; mRNA.
DR EMBL; AK000922; BAA91427.1; -; mRNA.
DR EMBL; AC012146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90363.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90364.1; -; Genomic_DNA.
DR EMBL; BC060810; AAH60810.1; -; mRNA.
DR EMBL; BC092473; AAH92473.1; -; mRNA.
DR CCDS; CCDS11066.1; -. [Q9NWF4-1]
DR RefSeq; NP_001098047.1; NM_001104577.1. [Q9NWF4-1]
DR RefSeq; NP_060456.3; NM_017986.3. [Q9NWF4-1]
DR RefSeq; XP_011522253.1; XM_011523951.1. [Q9NWF4-1]
DR AlphaFoldDB; Q9NWF4; -.
DR BioGRID; 120383; 9.
DR IntAct; Q9NWF4; 9.
DR STRING; 9606.ENSP00000399979; -.
DR TCDB; 2.A.125.1.1; the eukaryotic riboflavin transporter (e-rft) family.
DR GlyGen; Q9NWF4; 1 site.
DR iPTMnet; Q9NWF4; -.
DR PhosphoSitePlus; Q9NWF4; -.
DR BioMuta; SLC52A1; -.
DR DMDM; 308153487; -.
DR jPOST; Q9NWF4; -.
DR MassIVE; Q9NWF4; -.
DR PaxDb; Q9NWF4; -.
DR PeptideAtlas; Q9NWF4; -.
DR PRIDE; Q9NWF4; -.
DR ProteomicsDB; 82931; -. [Q9NWF4-2]
DR Antibodypedia; 23586; 184 antibodies from 23 providers.
DR DNASU; 55065; -.
DR Ensembl; ENST00000254853.10; ENSP00000254853.5; ENSG00000132517.15. [Q9NWF4-1]
DR Ensembl; ENST00000424747.1; ENSP00000399979.1; ENSG00000132517.15. [Q9NWF4-1]
DR GeneID; 55065; -.
DR KEGG; hsa:55065; -.
DR MANE-Select; ENST00000254853.10; ENSP00000254853.5; NM_017986.4; NP_060456.3.
DR UCSC; uc002gao.5; human. [Q9NWF4-1]
DR CTD; 55065; -.
DR DisGeNET; 55065; -.
DR GeneCards; SLC52A1; -.
DR GeneReviews; SLC52A1; -.
DR HGNC; HGNC:30225; SLC52A1.
DR HPA; ENSG00000132517; Group enriched (intestine, placenta, skin).
DR MalaCards; SLC52A1; -.
DR MIM; 607883; gene.
DR MIM; 615026; phenotype.
DR neXtProt; NX_Q9NWF4; -.
DR OpenTargets; ENSG00000132517; -.
DR Orphanet; 411712; Maternal riboflavin deficiency.
DR PharmGKB; PA134991217; -.
DR VEuPathDB; HostDB:ENSG00000132517; -.
DR eggNOG; KOG4255; Eukaryota.
DR GeneTree; ENSGT00390000003774; -.
DR HOGENOM; CLU_034789_1_0_1; -.
DR InParanoid; Q9NWF4; -.
DR OMA; WCGISIQ; -.
DR OrthoDB; 757564at2759; -.
DR PhylomeDB; Q9NWF4; -.
DR TreeFam; TF314820; -.
DR PathwayCommons; Q9NWF4; -.
DR Reactome; R-HSA-196843; Vitamin B2 (riboflavin) metabolism.
DR SignaLink; Q9NWF4; -.
DR BioGRID-ORCS; 55065; 13 hits in 1065 CRISPR screens.
DR GenomeRNAi; 55065; -.
DR Pharos; Q9NWF4; Tbio.
DR PRO; PR:Q9NWF4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NWF4; protein.
DR Bgee; ENSG00000132517; Expressed in duodenum and 77 other tissues.
DR ExpressionAtlas; Q9NWF4; baseline and differential.
DR Genevisible; Q9NWF4; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006771; P:riboflavin metabolic process; TAS:Reactome.
DR GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB.
DR InterPro; IPR009357; Riboflavin_transptr.
DR PANTHER; PTHR12929; PTHR12929; 1.
DR Pfam; PF06237; DUF1011; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein;
KW Host cell receptor for virus entry; Membrane; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..448
FT /note="Solute carrier family 52, riboflavin transporter,
FT member 1"
FT /id="PRO_0000042632"
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 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
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 225..267
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 45..167
FT /note="WSLPSYLSVVVALGNLGLLVVTLWRQLAPGKGEQVPIQVVQVLSVVGTALLA
FT PLWHHVAPVAGQLHSVAFLTLALVLAMACCTSNVTFLPFLSHLPPPFLRSFFLGQGLSA
FT LLPCVLALVQGV -> EWEGGTGKRGAGMPRKVACGSSLSLSHCAPDMASFLPCRLEPP
FT LIPLCGCGAGKPGSAGGDPVEAAGPGQGRAGPHPGGTGAECSGHSPAGPSVAPRGPSGR
FT AAPLCGLPNSGLGVGNGLLYL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18632736"
FT /id="VSP_039888"
FT VAR_SEQ 168..448
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18632736"
FT /id="VSP_039889"
FT VARIANT 70
FT /note="Q -> R (riboflavin transport is unaffected;
FT dbSNP:rs346822)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18632736,
FT ECO:0000269|PubMed:21089064, ECO:0000269|Ref.5"
FT /id="VAR_028361"
FT VARIANT 271
FT /note="A -> V (in dbSNP:rs346821)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:21089064"
FT /id="VAR_028362"
FT VARIANT 296
FT /note="V -> M (riboflavin transport is unaffected;
FT dbSNP:rs2304445)"
FT /evidence="ECO:0000269|PubMed:21089064"
FT /id="VAR_028363"
FT VARIANT 386
FT /note="L -> V (in dbSNP:rs187609896)"
FT /evidence="ECO:0000269|PubMed:28190456"
FT /id="VAR_079006"
SQ 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
