SC5A2_HUMAN
ID SC5A2_HUMAN Reviewed; 672 AA.
AC P31639; A2RRD2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Sodium/glucose cotransporter 2;
DE Short=Na(+)/glucose cotransporter 2;
DE AltName: Full=Low affinity sodium-glucose cotransporter;
DE AltName: Full=Solute carrier family 5 member 2;
GN Name=SLC5A2 {ECO:0000303|PubMed:14614622};
GN Synonyms=SGLT2 {ECO:0000303|PubMed:14614622};
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).
RC TISSUE=Kidney;
RX PubMed=1415574; DOI=10.1152/ajprenal.1992.263.3.f459;
RA Wells R.G., Pajor A.M., Kanai Y., Turk E., Wright E.M., Hediger M.A.;
RT "Cloning of a human kidney cDNA with similarity to the sodium-glucose
RT cotransporter.";
RL Am. J. Physiol. 263:F459-F465(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=28592437; DOI=10.1152/ajprenal.00628.2016;
RA Coady M.J., Wallendorff B., Lapointe J.Y.;
RT "Characterization of the transport activity of SGLT2/MAP17, the renal low-
RT affinity Na+-glucose cotransporter.";
RL Am. J. Physiol. 313:F467-F474(2017).
RN [5]
RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=20980548; DOI=10.1152/ajpcell.00388.2010;
RA Hummel C.S., Lu C., Loo D.D., Hirayama B.A., Voss A.A., Wright E.M.;
RT "Glucose transport by human renal Na+/D-glucose cotransporters SGLT1 and
RT SGLT2.";
RL Am. J. Physiol. 300:C14-C21(2011).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.95 ANGSTROMS) IN COMPLEX WITH PDZK1IP1
RP AND EMPAGLIFLOZIN, FUNCTION, TRANSPORTER ACTIVITY, SUBUNIT, AND MUTAGENESIS
RP OF VAL-95; PHE-98; VAL-157; LEU-283 AND PHE-453.
RX PubMed=34880493; DOI=10.1038/s41586-021-04212-9;
RA Niu Y., Liu R., Guan C., Zhang Y., Chen Z., Hoerer S., Nar H., Chen L.;
RT "Structural basis of inhibition of the human SGLT2-MAP17 glucose
RT transporter.";
RL Nature 601:280-284(2022).
RN [7]
RP VARIANT GLYS SER-654.
RX PubMed=14614622; DOI=10.1007/s00439-003-1054-x;
RA Calado J., Soto K., Clemente C., Correia P., Rueff J.;
RT "Novel compound heterozygous mutations in SLC5A2 are responsible for
RT autosomal recessive renal glucosuria.";
RL Hum. Genet. 114:314-316(2004).
CC -!- FUNCTION: Electrogenic Na(+)-coupled sugar simporter that actively
CC transports D-glucose at the plasma membrane, with a Na(+) to sugar
CC coupling ratio of 1:1. Transporter activity is driven by a
CC transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump
CC (PubMed:20980548, PubMed:28592437, PubMed:34880493). Has a primary role
CC in D-glucose reabsorption from glomerular filtrate across the brush
CC border of the early proximal tubules of the kidney (By similarity).
CC {ECO:0000250|UniProtKB:Q923I7, ECO:0000269|PubMed:20980548,
CC ECO:0000269|PubMed:28592437, ECO:0000269|PubMed:34880493}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + Na(+)(out) = D-glucose(in) + Na(+)(in);
CC Xref=Rhea:RHEA:70571, ChEBI:CHEBI:4167, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:20980548, ECO:0000269|PubMed:28592437,
CC ECO:0000269|PubMed:34880493};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70572;
CC Evidence={ECO:0000305|PubMed:20980548, ECO:0000305|PubMed:28592437,
CC ECO:0000305|PubMed:34880493};
CC -!- ACTIVITY REGULATION: Inhibited by phlorizin. Inhibited by diabetic
CC drugs that lower blood sugar levels, including empagliflozin and
CC dapagliflozin. {ECO:0000269|PubMed:20980548,
CC ECO:0000269|PubMed:28592437}.
CC -!- SUBUNIT: Forms a heterodimer with PDZK1IP1; this interaction enhances
CC the transporter activity over a hundred-fold.
CC {ECO:0000269|PubMed:34880493}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q923I7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31639-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31639-2; Sequence=VSP_056333, VSP_056334;
CC -!- DISEASE: Renal glucosuria (GLYS) [MIM:233100]: A disorder characterized
CC by persistent isolated glucosuria, normal fasting serum glucose
CC concentration, decreased renal tubular resorption of glucose from the
CC urine, and absence of any other signs of tubular dysfunction.
CC {ECO:0000269|PubMed:14614622}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; M95549; AAA36608.1; -; mRNA.
DR EMBL; AC026471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131542; AAI31543.1; -; mRNA.
DR CCDS; CCDS10714.1; -. [P31639-1]
DR PIR; A56765; A56765.
DR RefSeq; NP_003032.1; NM_003041.3. [P31639-1]
DR PDB; 7VSI; EM; 2.95 A; A=1-672.
DR PDBsum; 7VSI; -.
DR AlphaFoldDB; P31639; -.
DR SMR; P31639; -.
DR BioGRID; 112415; 13.
DR IntAct; P31639; 4.
DR MINT; P31639; -.
DR STRING; 9606.ENSP00000327943; -.
DR BindingDB; P31639; -.
DR ChEMBL; CHEMBL3884; -.
DR DrugBank; DB08907; Canagliflozin.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB06292; Dapagliflozin.
DR DrugBank; DB09038; Empagliflozin.
DR DrugBank; DB11827; Ertugliflozin.
DR DrugCentral; P31639; -.
DR GuidetoPHARMACOLOGY; 916; -.
DR TCDB; 2.A.1.7.26; the major facilitator superfamily (mfs).
DR TCDB; 2.A.21.3.16; the solute:sodium symporter (sss) family.
DR CarbonylDB; P31639; -.
DR GlyGen; P31639; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P31639; -.
DR PhosphoSitePlus; P31639; -.
DR BioMuta; SLC5A2; -.
DR DMDM; 400337; -.
DR jPOST; P31639; -.
DR MassIVE; P31639; -.
DR PaxDb; P31639; -.
DR PeptideAtlas; P31639; -.
DR PRIDE; P31639; -.
DR ProteomicsDB; 461; -.
DR ProteomicsDB; 54795; -. [P31639-1]
DR Antibodypedia; 27902; 216 antibodies from 32 providers.
DR DNASU; 6524; -.
DR Ensembl; ENST00000330498.4; ENSP00000327943.3; ENSG00000140675.13. [P31639-1]
DR Ensembl; ENST00000419665.6; ENSP00000410601.2; ENSG00000140675.13. [P31639-2]
DR GeneID; 6524; -.
DR KEGG; hsa:6524; -.
DR MANE-Select; ENST00000330498.4; ENSP00000327943.3; NM_003041.4; NP_003032.1.
DR UCSC; uc002ecf.5; human. [P31639-1]
DR CTD; 6524; -.
DR DisGeNET; 6524; -.
DR GeneCards; SLC5A2; -.
DR HGNC; HGNC:11037; SLC5A2.
DR HPA; ENSG00000140675; Tissue enriched (kidney).
DR MalaCards; SLC5A2; -.
DR MIM; 182381; gene.
DR MIM; 233100; phenotype.
DR neXtProt; NX_P31639; -.
DR OpenTargets; ENSG00000140675; -.
DR Orphanet; 69076; Familial renal glucosuria.
DR PharmGKB; PA35902; -.
DR VEuPathDB; HostDB:ENSG00000140675; -.
DR eggNOG; KOG2349; Eukaryota.
DR GeneTree; ENSGT00940000160533; -.
DR HOGENOM; CLU_018808_9_0_1; -.
DR InParanoid; P31639; -.
DR OMA; LEYWMAV; -.
DR PhylomeDB; P31639; -.
DR TreeFam; TF352855; -.
DR PathwayCommons; P31639; -.
DR Reactome; R-HSA-189200; Cellular hexose transport.
DR Reactome; R-HSA-5658208; Defective SLC5A2 causes renal glucosuria (GLYS1).
DR SABIO-RK; P31639; -.
DR SignaLink; P31639; -.
DR SIGNOR; P31639; -.
DR BioGRID-ORCS; 6524; 6 hits in 1058 CRISPR screens.
DR ChiTaRS; SLC5A2; human.
DR GeneWiki; SLC5A2; -.
DR GenomeRNAi; 6524; -.
DR Pharos; P31639; Tclin.
DR PRO; PR:P31639; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P31639; protein.
DR Bgee; ENSG00000140675; Expressed in nephron tubule and 144 other tissues.
DR ExpressionAtlas; P31639; baseline and differential.
DR Genevisible; P31639; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015151; F:alpha-glucoside transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005412; F:glucose:sodium symporter activity; IDA:UniProtKB.
DR GO; GO:0005362; F:low-affinity glucose:sodium symporter activity; TAS:ProtInc.
DR GO; GO:0000017; P:alpha-glucoside transport; IDA:ARUK-UCL.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0098708; P:glucose import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0008645; P:hexose transmembrane transport; TAS:Reactome.
DR GO; GO:0035623; P:renal glucose absorption; ISS:UniProtKB.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR018212; Na/solute_symporter_CS.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disease variant;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..672
FT /note="Sodium/glucose cotransporter 2"
FT /id="PRO_0000105372"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..205
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..526
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 40
FT /note="Implicated in sodium coupling"
FT /evidence="ECO:0000250"
FT SITE 300
FT /note="Implicated in sodium coupling"
FT /evidence="ECO:0000250"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 378..458
FT /note="LRGLMLAVMLAALMSSLASIFNSSSTLFTMDIYTRLRPRAGDRELLLVGRLW
FT VVFIVVVSVAWLPVVQAAQGGQLFDYIQA -> RLLGTHRGPADGPGTPDSRVLLRLGQ
FT LCAALGVPSFPLRRALPLLRHCAVLLLWPPHPHGLPVHRAHPQKAPPPPGLQSPA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056333"
FT VAR_SEQ 459..672
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056334"
FT VARIANT 654
FT /note="N -> S (in GLYS; dbSNP:rs61742739)"
FT /evidence="ECO:0000269|PubMed:14614622"
FT /id="VAR_019310"
FT MUTAGEN 95
FT /note="V->A: Strong reduction in D-glucose transporter
FT activity. Confers partial resistance to empagliflozin
FT inhibition."
FT /evidence="ECO:0000269|PubMed:34880493"
FT MUTAGEN 98
FT /note="F->A: Slightly decreases D-glucose transporter
FT activity. Abolishes the binding to inhibitor,
FT empagliflozin."
FT /evidence="ECO:0000269|PubMed:34880493"
FT MUTAGEN 157
FT /note="V->A: Decreases D-glucose transporter activity."
FT /evidence="ECO:0000269|PubMed:34880493"
FT MUTAGEN 283
FT /note="L->M: Strong reduction in D-glucose transporter
FT activity. Confers partial resistance to empagliflozin
FT inhibition."
FT /evidence="ECO:0000269|PubMed:34880493"
FT MUTAGEN 453
FT /note="F->A: Slightly decreases D-glucose transporter
FT activity. Greatly reduces the binding to inhibitor,
FT empagliflozin."
FT /evidence="ECO:0000269|PubMed:34880493"
FT HELIX 23..47
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 137..153
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 175..223
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:7VSI"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7VSI"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:7VSI"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:7VSI"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:7VSI"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 276..292
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:7VSI"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 307..321
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 348..354
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 365..373
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 376..413
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 419..445
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 451..476
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 482..506
FT /evidence="ECO:0007829|PDB:7VSI"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 526..546
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 561..563
FT /evidence="ECO:0007829|PDB:7VSI"
FT HELIX 647..670
FT /evidence="ECO:0007829|PDB:7VSI"
SQ SEQUENCE 672 AA; 72897 MW; 233C65F1601B0337 CRC64;
MEEHTEAGSA PEMGAQKALI DNPADILVIA AYFLLVIGVG LWSMCRTNRG TVGGYFLAGR
SMVWWPVGAS LFASNIGSGH FVGLAGTGAA SGLAVAGFEW NALFVVLLLG WLFAPVYLTA
GVITMPQYLR KRFGGRRIRL YLSVLSLFLY IFTKISVDMF SGAVFIQQAL GWNIYASVIA
LLGITMIYTV TGGLAALMYT DTVQTFVILG GACILMGYAF HEVGGYSGLF DKYLGAATSL
TVSEDPAVGN ISSFCYRPRP DSYHLLRHPV TGDLPWPALL LGLTIVSGWY WCSDQVIVQR
CLAGKSLTHI KAGCILCGYL KLTPMFLMVM PGMISRILYP DEVACVVPEV CRRVCGTEVG
CSNIAYPRLV VKLMPNGLRG LMLAVMLAAL MSSLASIFNS SSTLFTMDIY TRLRPRAGDR
ELLLVGRLWV VFIVVVSVAW LPVVQAAQGG QLFDYIQAVS SYLAPPVSAV FVLALFVPRV
NEQGAFWGLI GGLLMGLARL IPEFSFGSGS CVQPSACPAF LCGVHYLYFA IVLFFCSGLL
TLTVSLCTAP IPRKHLHRLV FSLRHSKEER EDLDADEQQG SSLPVQNGCP ESAMEMNEPQ
APAPSLFRQC LLWFCGMSRG GVGSPPPLTQ EEAAAAARRL EDISEDPSWA RVVNLNALLM
MAVAVFLWGF YA
