MELB_ECOLI
ID MELB_ECOLI Reviewed; 473 AA.
AC P02921; Q2M6I4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Melibiose permease {ECO:0000303|PubMed:3316227};
DE AltName: Full=Melibiose carrier {ECO:0000303|PubMed:6323466};
DE AltName: Full=Melibiose transporter;
DE AltName: Full=Melibiose/cation symporter {ECO:0000305};
DE AltName: Full=Na+ (Li+)/melibiose symporter;
DE AltName: Full=Thiomethylgalactoside permease II;
GN Name=melB {ECO:0000303|PubMed:6323466}; Synonyms=mel-4;
GN OrderedLocusNames=b4120, JW4081;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6323466; DOI=10.1016/s0021-9258(17)43048-1;
RA Yazyu H., Shiota-Niiya S., Shimamoto T., Kanazawa H., Futai M.,
RA Tsuchiya T.;
RT "Nucleotide sequence of the melB gene and characteristics of deduced amino
RT acid sequence of the melibiose carrier in Escherichia coli.";
RL J. Biol. Chem. 259:4320-4326(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-8, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=7703254; DOI=10.1021/bi00013a033;
RA Pourcher T., Leclercq S., Brandolin G., Leblanc G.;
RT "Melibiose permease of Escherichia coli: large scale purification and
RT evidence that H+, Na+, and Li+ sugar symport is catalyzed by a single
RT polypeptide.";
RL Biochemistry 34:4412-4420(1995).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / W3133;
RX PubMed=45782; DOI=10.3109/09687687809063858;
RA Tsuchiya T., Wilson T.H.;
RT "Cation-sugar cotransport in the melibiose transport system of Escherichia
RT coli.";
RL Membr. Biochem. 2:63-79(1978).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3311166; DOI=10.1016/0005-2736(87)90368-3;
RA Wilson D.M., Wilson T.H.;
RT "Cation specificity for sugar substrates of the melibiose carrier in
RT Escherichia coli.";
RL Biochim. Biophys. Acta 904:191-200(1987).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=3316227; DOI=10.1016/s0021-9258(18)45463-4;
RA Bassilana M., Pourcher T., Leblanc G.;
RT "Facilitated diffusion properties of melibiose permease in Escherichia coli
RT membrane vesicles. Release of co-substrates is rate limiting for permease
RT cycling.";
RL J. Biol. Chem. 262:16865-16870(1987).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=2185831; DOI=10.1021/bi00462a020;
RA Roepe P.D., Kaback H.R.;
RT "Isolation and functional reconstitution of soluble melibiose permease from
RT Escherichia coli.";
RL Biochemistry 29:2572-2577(1990).
RN [10]
RP MUTAGENESIS OF ASP-59.
RX PubMed=1872836; DOI=10.1016/0006-291x(91)91016-6;
RA Pourcher T., Deckert M., Bassilana M., Leblanc G.;
RT "Melibiose permease of Escherichia coli: mutation of aspartic acid 55 in
RT putative helix II abolishes activation of sugar binding by Na+ ions.";
RL Biochem. Biophys. Res. Commun. 178:1176-1181(1991).
RN [11]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=1730719; DOI=10.1016/s0021-9258(18)46019-x;
RA Botfield M.C., Noguchi K., Tsuchiya T., Wilson T.H.;
RT "Membrane topology of the melibiose carrier of Escherichia coli.";
RL J. Biol. Chem. 267:1818-1822(1992).
RN [12]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8672452; DOI=10.1021/bi9527496;
RA Pourcher T., Bibi E., Kaback H.R., Leblanc G.;
RT "Membrane topology of the melibiose permease of Escherichia coli studied by
RT melB-phoA fusion analysis.";
RL Biochemistry 35:4161-4168(1996).
RN [13]
RP MUTAGENESIS OF LYS-18; ASP-19; ASP-35; ARG-52; ASP-55; ASP-59; ASP-124;
RP ARG-199 AND GLU-203.
RX PubMed=11444849; DOI=10.1006/bbrc.2001.5200;
RA Ding P.Z., Wilson T.H.;
RT "The effect of modifications of the charged residues in the transmembrane
RT helices on the transport activity of the melibiose carrier of Escherichia
RT coli.";
RL Biochem. Biophys. Res. Commun. 285:348-354(2001).
RN [14]
RP DOMAIN, AND CRYSTALLIZATION.
RX PubMed=12110569; DOI=10.1093/emboj/cdf378;
RA Hacksell I., Rigaud J.L., Purhonen P., Pourcher T., Hebert H., Leblanc G.;
RT "Projection structure at 8 A resolution of the melibiose permease, an Na-
RT sugar co-transporter from Escherichia coli.";
RL EMBO J. 21:3569-3574(2002).
RN [15]
RP DOMAIN, AND MUTAGENESIS OF LYS-138; ARG-139; ARG-141 AND ARG-149.
RX PubMed=12421811; DOI=10.1074/jbc.m210053200;
RA Abdel-Dayem M., Basquin C., Pourcher T., Cordat E., Leblanc G.;
RT "Cytoplasmic loop connecting helices IV and V of the melibiose permease
RT from Escherichia coli is involved in the process of Na+-coupled sugar
RT translocation.";
RL J. Biol. Chem. 278:1518-1524(2003).
RN [16]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [17]
RP DOMAIN, AND PROTEIN MODEL.
RX PubMed=19706416; DOI=10.1073/pnas.0905516106;
RA Yousef M.S., Guan L.;
RT "A 3D structure model of the melibiose permease of Escherichia coli
RT represents a distinctive fold for Na+ symporters.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15291-15296(2009).
RN [18]
RP MUTAGENESIS OF ASP-19; ASP-55; ASP-59 AND ASP-124, AND PROTEIN MODEL.
RX PubMed=21135207; DOI=10.1073/pnas.1008649107;
RA Granell M., Leon X., Leblanc G., Padros E., Lorenz-Fonfria V.A.;
RT "Structural insights into the activation mechanism of melibiose permease by
RT sodium binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22078-22083(2010).
CC -!- FUNCTION: Mediates the transport of melibiose and other galactosides by
CC a symport mechanism (PubMed:45782, PubMed:3311166, PubMed:3316227,
CC PubMed:2185831, PubMed:7703254). Can use sodium, lithium and protons as
CC coupling cations, depending on the sugar substrate and the cationic
CC environment (PubMed:45782, PubMed:3311166, PubMed:3316227,
CC PubMed:7703254). Alpha-galactosides (melibiose, raffinose, p-
CC nitrophenyl-alpha-galactoside or methyl-alpha-galactoside) are
CC cotransported with either Na(+) or H(+), whereas beta-galactosides
CC (lactose, L-arabinose-beta-D-galactoside, D-fructose-beta-D-
CC galactoside, methyl-beta-galactoside or p-nitrophenyl-beta-galactoside)
CC are cotransported with Na(+) or Li(+) but not H(+) (PubMed:45782,
CC PubMed:3311166). The monosaccharide D-galactose can use either Na(+) or
CC H(+) for cotransport whereas D-fucose, L-arabinose and D-galactosamine
CC can use only Na(+) (PubMed:3311166). {ECO:0000269|PubMed:2185831,
CC ECO:0000269|PubMed:3311166, ECO:0000269|PubMed:3316227,
CC ECO:0000269|PubMed:45782, ECO:0000269|PubMed:7703254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=melibiose(in) + Na(+)(in) = melibiose(out) + Na(+)(out);
CC Xref=Rhea:RHEA:28851, ChEBI:CHEBI:28053, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:3311166, ECO:0000269|PubMed:3316227,
CC ECO:0000269|PubMed:45782, ECO:0000269|PubMed:7703254};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Li(+)(in) + melibiose(in) = Li(+)(out) + melibiose(out);
CC Xref=Rhea:RHEA:28847, ChEBI:CHEBI:28053, ChEBI:CHEBI:49713;
CC Evidence={ECO:0000269|PubMed:3316227, ECO:0000269|PubMed:7703254};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + melibiose(in) = H(+)(out) + melibiose(out);
CC Xref=Rhea:RHEA:28855, ChEBI:CHEBI:15378, ChEBI:CHEBI:28053;
CC Evidence={ECO:0000269|PubMed:2185831, ECO:0000269|PubMed:3311166,
CC ECO:0000269|PubMed:3316227, ECO:0000269|PubMed:45782,
CC ECO:0000269|PubMed:7703254};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:2185831,
CC ECO:0000269|PubMed:7703254}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:1730719,
CC ECO:0000269|PubMed:7703254, ECO:0000269|PubMed:8672452}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:1730719,
CC ECO:0000269|PubMed:8672452}.
CC -!- DOMAIN: Consists of two pseudosymmetrical 6-helix bundles lining an
CC internal hydrophilic cavity, which faces the cytoplasmic side of the
CC membrane and probably contains the binding sites for both cosubstrates
CC (PubMed:12110569, PubMed:19706416). The cytoplasmic loop connecting the
CC membrane-spanning segments 4 and 5 is close to the sugar binding site
CC and may participate directly in cosubstrate translocation by MelB
CC (PubMed:12421811). The charged residue Arg-141 is probably involved in
CC the reaction of cosubstrate translocation or substrate release in the
CC inner compartment (PubMed:12421811). {ECO:0000269|PubMed:12110569,
CC ECO:0000269|PubMed:12421811, ECO:0000269|PubMed:19706416}.
CC -!- SIMILARITY: Belongs to the sodium:galactoside symporter (TC 2.A.2)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24148.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA97020.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE78122.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; K01991; AAA24148.1; ALT_INIT; Genomic_DNA.
DR EMBL; U14003; AAA97020.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77081.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78122.1; ALT_INIT; Genomic_DNA.
DR PIR; A03421; BDEC.
DR RefSeq; NP_418544.2; NC_000913.3.
DR RefSeq; WP_000028111.1; NZ_SSZK01000018.1.
DR AlphaFoldDB; P02921; -.
DR SMR; P02921; -.
DR BioGRID; 4263176; 14.
DR DIP; DIP-10180N; -.
DR IntAct; P02921; 1.
DR STRING; 511145.b4120; -.
DR PaxDb; P02921; -.
DR PRIDE; P02921; -.
DR EnsemblBacteria; AAC77081; AAC77081; b4120.
DR EnsemblBacteria; BAE78122; BAE78122; BAE78122.
DR GeneID; 948635; -.
DR KEGG; ecj:JW4081; -.
DR KEGG; eco:b4120; -.
DR PATRIC; fig|511145.12.peg.4251; -.
DR EchoBASE; EB0573; -.
DR eggNOG; COG2211; Bacteria.
DR HOGENOM; CLU_027408_0_3_6; -.
DR InParanoid; P02921; -.
DR PhylomeDB; P02921; -.
DR BioCyc; EcoCyc:MELB-MON; -.
DR BioCyc; MetaCyc:MELB-MON; -.
DR PRO; PR:P02921; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015487; F:melibiose:cation symporter activity; IDA:EcoCyc.
DR GO; GO:0043887; F:melibiose:sodium symporter activity; IDA:EcoCyc.
DR GO; GO:0015592; F:methylgalactoside transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015769; P:melibiose transport; IDA:EcoCyc.
DR GO; GO:0015765; P:methylgalactoside transport; IDA:EcoCyc.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR039672; MFS_2.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR001927; Na/Gal_symport.
DR InterPro; IPR018043; Na/Gal_symport_CS.
DR PANTHER; PTHR11328; PTHR11328; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00792; gph; 1.
DR PROSITE; PS00872; NA_GALACTOSIDE_SYMP; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing; Membrane;
KW Reference proteome; Sugar transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7703254"
FT CHAIN 2..473
FT /note="Melibiose permease"
FT /id="PRO_0000170752"
FT TOPO_DOM 2..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:1730719,
FT ECO:0000269|PubMed:8672452"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 38..39
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 61..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 99..105
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 127..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 172..183
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 205..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 254..266
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 288..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 318..325
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 347..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 400..407
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:8672452"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:8672452"
FT TOPO_DOM 429..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:1730719, ECO:0000269|PubMed:8672452"
FT SITE 141
FT /note="Important for activity"
FT /evidence="ECO:0000305|PubMed:12421811"
FT MUTAGEN 18
FT /note="K->C: Abolishes transporter activity."
FT /evidence="ECO:0000269|PubMed:11444849"
FT MUTAGEN 19
FT /note="D->C: Abolishes transporter activity. Can bind
FT Na(+). Large decrease in the affinity for melibiose in the
FT presence of H(+)."
FT /evidence="ECO:0000269|PubMed:11444849,
FT ECO:0000269|PubMed:21135207"
FT MUTAGEN 35
FT /note="D->C: Abolishes transporter activity."
FT /evidence="ECO:0000269|PubMed:11444849"
FT MUTAGEN 52
FT /note="R->C: Abolishes transporter activity."
FT /evidence="ECO:0000269|PubMed:11444849"
FT MUTAGEN 55
FT /note="D->C: Abolishes transporter activity. Chemical
FT restoration of the charge via the oxidation of the thiol to
FT the sulfinic and/or sulfonic acid results in partial
FT recovery of transporter activity. Does not bind Na(+).
FT Binds melibiose in the presence of H(+)."
FT /evidence="ECO:0000269|PubMed:11444849,
FT ECO:0000269|PubMed:21135207"
FT MUTAGEN 59
FT /note="D->C: Loses ability to catalyze Na(+) or H(+)-
FT coupled melibiose transport against a concentration
FT gradient. Does not bind Na(+). Binds melibiose in the
FT presence of H(+)."
FT /evidence="ECO:0000269|PubMed:11444849,
FT ECO:0000269|PubMed:1872836, ECO:0000269|PubMed:21135207"
FT MUTAGEN 124
FT /note="D->C: Abolishes transporter activity. Chemical
FT restoration of the charge via the oxidation of the thiol to
FT the sulfinic and/or sulfonic acid results in partial
FT recovery of transporter activity. Can bind Na(+), but
FT structural changes induced by Na(+) are less complete and
FT of smaller amplitude. Large decrease in the affinity for
FT melibiose in the presence of H(+)."
FT /evidence="ECO:0000269|PubMed:11444849,
FT ECO:0000269|PubMed:21135207"
FT MUTAGEN 138
FT /note="K->C: Can transport melibiose."
FT /evidence="ECO:0000269|PubMed:12421811"
FT MUTAGEN 139
FT /note="R->C: Can transport melibiose."
FT /evidence="ECO:0000269|PubMed:12421811"
FT MUTAGEN 141
FT /note="R->C,Q: Abolishes melibiose transport. Decreases
FT affinity for melibiose."
FT /evidence="ECO:0000269|PubMed:12421811"
FT MUTAGEN 141
FT /note="R->K: Retains ion-coupled melibiose transport."
FT /evidence="ECO:0000269|PubMed:12421811"
FT MUTAGEN 149
FT /note="R->C: Abolishes melibiose transport."
FT /evidence="ECO:0000269|PubMed:12421811"
FT MUTAGEN 149
FT /note="R->K,Q: Retains ion-coupled melibiose transport."
FT /evidence="ECO:0000269|PubMed:12421811"
FT MUTAGEN 199
FT /note="R->C: Does not affect transporter activity."
FT /evidence="ECO:0000269|PubMed:11444849"
FT MUTAGEN 203
FT /note="E->C: Does not affect transporter activity."
FT /evidence="ECO:0000269|PubMed:11444849"
SQ SEQUENCE 473 AA; 52636 MW; E05FAA436F4CA70C CRC64;
MSISMTTKLS YGFGAFGKDF AIGIVYMYLM YYYTDVVGLS VGLVGTLFLV ARIWDAINDP
IMGWIVNATR SRWGKFKPWI LIGTLANSVI LFLLFSAHLF EGTTQIVFVC VTYILWGMTY
TIMDIPFWSL VPTITLDKRE REQLVPYPRF FASLAGFVTA GVTLPFVNYV GGGDRGFGFQ
MFTLVLIAFF IVSTIITLRN VHEVFSSDNQ PSAEGSHLTL KAIVALIYKN DQLSCLLGMA
LAYNVASNII TGFAIYYFSY VIGDADLFPY YLSYAGAANL VTLVFFPRLV KSLSRRILWA
GASILPVLSC GVLLLMALMS YHNVVLIVIA GILLNVGTAL FWVLQVIMVA DIVDYGEYKL
HVRCESIAYS VQTMVVKGGS AFAAFFIAVV LGMIGYVPNV EQSTQALLGM QFIMIALPTL
FFMVTLILYF RFYRLNGDTL RRIQIHLLDK YRKVPPEPVH ADIPVGAVSD VKA
