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 27-MAR-2024, entry version 152. 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}; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9NWF4; 1 site, No reported glycans. 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; 9606-ENSP00000399979; -. DR PeptideAtlas; Q9NWF4; -. DR Antibodypedia; 23586; 211 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 AGR; HGNC:30225; -. 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; LLTRICH; -. DR OrthoDB; 5477759at2759; -. 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; 15 hits in 1143 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 78 other cell types or tissues. DR ExpressionAtlas; Q9NWF4; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. 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; SOLUTE CARRIER FAMILY 52; 1. DR PANTHER; PTHR12929:SF20; SOLUTE CARRIER FAMILY 52, RIBOFLAVIN TRANSPORTER, MEMBER 1; 1. DR Pfam; PF06237; SLC52_ribofla_tr; 1. DR Genevisible; Q9NWF4; HS. 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 //