GTR8_MOUSE
ID GTR8_MOUSE Reviewed; 477 AA.
AC Q9JIF3; Q5BKP8; Q9JJP4; Q9JJZ0;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 8 {ECO:0000305};
DE AltName: Full=Glucose transporter type 8 {ECO:0000303|PubMed:10821868};
DE Short=GLUT-8 {ECO:0000303|PubMed:10821868};
DE AltName: Full=Glucose transporter type X1 {ECO:0000303|PubMed:10671487};
GN Name=Slc2a8 {ECO:0000312|MGI:MGI:1860103};
GN Synonyms=Glut8 {ECO:0000303|PubMed:10821868},
GN GlutX1 {ECO:0000303|PubMed:10671487};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10671487; DOI=10.1074/jbc.275.7.4607;
RA Ibberson M.R., Uldry M.A., Thorens B.;
RT "GLUTX1, a novel mammalian glucose transporter expressed in the central
RT nervous system and insulin-sensitive tissues.";
RL J. Biol. Chem. 275:4607-4612(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Testis;
RX PubMed=10821868; DOI=10.1074/jbc.275.21.16275;
RA Doege H., Schuermann A., Bahrenberg G., Brauers A., Joost H.-G.;
RT "GLUT8, a novel member of the sugar transport facilitator family with
RT glucose transport activity.";
RL J. Biol. Chem. 275:16275-16280(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=129; TISSUE=Embryonic carcinoma;
RX PubMed=10860996; DOI=10.1073/pnas.97.13.7313;
RA Carayannopoulos M.O., Chi M.M.-Y., Cui Y., Pingsterhaus J.M.,
RA McKnight R.A., Mueckler M., Devaskar S.U., Moley K.H.;
RT "GLUT8 is a glucose transporter responsible for insulin-stimulated glucose
RT uptake in the blastocyst.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7313-7318(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=129/Ola; TISSUE=Spleen;
RX PubMed=11689004; DOI=10.1006/bbrc.2001.5866;
RA Scheepers A., Doege H., Joost H.-G., Schuermann A.;
RT "Mouse GLUT8: genomic organization and regulation of expression in 3T3-L1
RT adipocytes by glucose.";
RL Biochem. Biophys. Res. Commun. 288:969-974(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [9]
RP INTERACTION WITH AP2B1, AND MUTAGENESIS OF 12-LEU-LEU-13.
RX PubMed=16723738; DOI=10.1242/jcs.02943;
RA Schmidt U., Briese S., Leicht K., Schuermann A., Joost H.-G., Al-Hasani H.;
RT "Endocytosis of the glucose transporter GLUT8 is mediated by interaction of
RT a dileucine motif with the beta2-adaptin subunit of the AP-2 adaptor
RT complex.";
RL J. Cell Sci. 119:2321-2331(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23396969; DOI=10.1074/jbc.m112.436790;
RA Corpe C.P., Eck P., Wang J., Al-Hasani H., Levine M.;
RT "Intestinal dehydroascorbic acid (DHA) transport mediated by the
RT facilitative sugar transporters, GLUT2 and GLUT8.";
RL J. Biol. Chem. 288:9092-9101(2013).
CC -!- FUNCTION: Insulin-regulated facilitative hexose transporter that
CC mediates the transport of glucose and fructose (PubMed:10821868,
CC PubMed:10860996, PubMed:23396969). Also able to mediate the transport
CC of dehydroascorbate (PubMed:23396969). {ECO:0000269|PubMed:10821868,
CC ECO:0000269|PubMed:10860996, ECO:0000269|PubMed:23396969}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:23396969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372,
CC ChEBI:CHEBI:37721; Evidence={ECO:0000269|PubMed:23396969};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-dehydroascorbate(out) = L-dehydroascorbate(in);
CC Xref=Rhea:RHEA:60380, ChEBI:CHEBI:58539;
CC Evidence={ECO:0000269|PubMed:23396969};
CC -!- ACTIVITY REGULATION: Inhibited by cytochalasin B.
CC {ECO:0000269|PubMed:10821868}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.33 mM for dehydroascorbate {ECO:0000269|PubMed:23396969};
CC -!- SUBUNIT: Interacts with AP2B1 (PubMed:16723738). Also able to mediate
CC the transport of dehydroascorbate (PubMed:23396969).
CC {ECO:0000269|PubMed:16723738, ECO:0000269|PubMed:23396969}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10860996};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9JJZ1}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Principally intracellular. May move between
CC intracellular vesicles and the plasma membrane. The dileucine
CC internalization motif is critical for intracellular sequestration.
CC {ECO:0000250|UniProtKB:Q9JJZ1}.
CC -!- TISSUE SPECIFICITY: Highest level of expression in placenta and testis.
CC Highly expressed in adult and pubertal testis, but not prepubertal
CC testis. Lower levels of expression in brain, liver, heart, kidney, fat
CC and skeletal muscle. {ECO:0000269|PubMed:10860996}.
CC -!- DEVELOPMENTAL STAGE: High expression in blastocysts.
CC {ECO:0000269|PubMed:10860996}.
CC -!- INDUCTION: Inhibited under glucose deprivation.
CC {ECO:0000269|PubMed:11689004}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ245936; CAB75719.1; -; mRNA.
DR EMBL; Y17802; CAB89815.1; -; mRNA.
DR EMBL; AF232061; AAF78366.1; -; mRNA.
DR EMBL; AJ413951; CAC88690.1; -; Genomic_DNA.
DR EMBL; AY856043; AAX51785.1; -; mRNA.
DR EMBL; AK081806; BAC38338.1; -; mRNA.
DR EMBL; AK170319; BAE41714.1; -; mRNA.
DR EMBL; AL731852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08590.1; -; Genomic_DNA.
DR EMBL; BC090993; AAH90993.1; -; mRNA.
DR CCDS; CCDS15937.1; -.
DR RefSeq; NP_062361.1; NM_019488.4.
DR AlphaFoldDB; Q9JIF3; -.
DR SMR; Q9JIF3; -.
DR IntAct; Q9JIF3; 7.
DR MINT; Q9JIF3; -.
DR STRING; 10090.ENSMUSP00000028129; -.
DR TCDB; 2.A.1.1.46; the major facilitator superfamily (mfs).
DR GlyGen; Q9JIF3; 1 site.
DR PhosphoSitePlus; Q9JIF3; -.
DR EPD; Q9JIF3; -.
DR MaxQB; Q9JIF3; -.
DR PaxDb; Q9JIF3; -.
DR PRIDE; Q9JIF3; -.
DR ProteomicsDB; 271350; -.
DR Antibodypedia; 1986; 136 antibodies from 27 providers.
DR DNASU; 56017; -.
DR Ensembl; ENSMUST00000028129; ENSMUSP00000028129; ENSMUSG00000026791.
DR GeneID; 56017; -.
DR KEGG; mmu:56017; -.
DR UCSC; uc008jhf.1; mouse.
DR CTD; 29988; -.
DR MGI; MGI:1860103; Slc2a8.
DR VEuPathDB; HostDB:ENSMUSG00000026791; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000158795; -.
DR InParanoid; Q9JIF3; -.
DR OMA; WNCILAF; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q9JIF3; -.
DR TreeFam; TF325324; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 56017; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slc2a8; mouse.
DR PRO; PR:Q9JIF3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9JIF3; protein.
DR Bgee; ENSMUSG00000026791; Expressed in spermatocyte and 194 other tissues.
DR ExpressionAtlas; Q9JIF3; baseline and differential.
DR Genevisible; Q9JIF3; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0033300; F:dehydroascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005353; F:fructose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015284; F:fructose uniporter activity; ISO:MGI.
DR GO; GO:0005354; F:galactose transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005536; F:glucose binding; IDA:MGI.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070837; P:dehydroascorbic acid transport; IDA:UniProtKB.
DR GO; GO:0015755; P:fructose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015757; P:galactose transmembrane transport; ISO:MGI.
DR GO; GO:0006006; P:glucose metabolic process; TAS:MGI.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IDA:MGI.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..477
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 8"
FT /id="PRO_0000050376"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..70
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..438
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 12..13
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000269|PubMed:16723738"
FT BINDING 162
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 268..269
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 274
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 394
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 12..13
FT /note="LL->AA: Abolishes interaction with AP2B1."
FT /evidence="ECO:0000269|PubMed:16723738"
FT CONFLICT 39
FT /note="S -> N (in Ref. 1; CAB75719)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="A -> S (in Ref. 1; CAB75719 and 3; AAF78366)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="S -> N (in Ref. 1; CAB75719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 51508 MW; 59A985B52FADF478 CRC64;
MSPEDPQETQ PLLRPPEART PRGRRVFLAS FAAALGPLSF GFALGYSSPA IPSLRRTAPP
ALRLGDNAAS WFGAVVTLGA AAGGILGGWL LDRAGRKLSL LLCTVPFVTG FAVITAARDV
WMLLGGRLLT GLACGVASLV APVYISEIAY PAVRGLLGSC VQLMVVTGIL LAYVAGWVLE
WRWLAVLGCV PPTLMLLLMC YMPETPRFLL TQHQYQEAMA ALRFLWGSEE GWEEPPVGAE
HQGFQLALLR RPGIYKPLII GISLMVFQQL SGVNAIMFYA NSIFEEAKFK DSSLASVTVG
IIQVLFTAVA ALIMDRAGRR LLLALSGVIM VFSMSAFGTY FKLTQSLPSN SSHVGLVPIA
AEPVDVQVGL AWLAVGSMCL FIAGFAVGWG PIPWLLMSEI FPLHVKGVAT GICVLTNWFM
AFLVTKEFSS VMEMLRPYGA FWLTAAFCAL SVLFTLTVVP ETKGRTLEQV TAHFEGR
