NUPG_ECOLI
ID NUPG_ECOLI Reviewed; 418 AA.
AC P0AFF4; P09452; P76653; Q2M9M9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Nucleoside permease NupG {ECO:0000255|HAMAP-Rule:MF_02049, ECO:0000305};
DE AltName: Full=Nucleoside-transport system protein NupG {ECO:0000305};
GN Name=nupG {ECO:0000255|HAMAP-Rule:MF_02049, ECO:0000303|PubMed:374403};
GN OrderedLocusNames=b2964, JW2932;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=3311747; DOI=10.1111/j.1432-1033.1987.tb13431.x;
RA Westh Hansen S.E., Jensen N., Munch-Petersen A.;
RT "Studies on the sequence and structure of the Escherichia coli K-12 nupG
RT gene, encoding a nucleoside-transport system.";
RL Eur. J. Biochem. 168:385-391(1987).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=15513740; DOI=10.1080/09687860400003941;
RA Xie H., Patching S.G., Gallagher M.P., Litherland G.J., Brough A.R.,
RA Venter H., Yao S.Y., Ng A.M., Young J.D., Herbert R.B., Henderson P.J.,
RA Baldwin S.A.;
RT "Purification and properties of the Escherichia coli nucleoside transporter
RT NupG, a paradigm for a major facilitator transporter sub-family.";
RL Mol. Membr. Biol. 21:323-336(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=374403; DOI=10.1016/s0021-9258(18)50647-5;
RA Munch-Petersen A., Mygind B., Nicolaisen A., Pihl N.J.;
RT "Nucleoside transport in cells and membrane vesicles from Escherichia coli
RT K12.";
RL J. Biol. Chem. 254:3730-3737(1979).
RN [6]
RP FUNCTION.
RX PubMed=11466294; DOI=10.1128/jb.183.16.4900-4904.2001;
RA Noerholm M.H., Dandanell G.;
RT "Specificity and topology of the Escherichia coli xanthosine permease, a
RT representative of the NHS subfamily of the major facilitator superfamily.";
RL J. Bacteriol. 183:4900-4904(2001).
RN [7]
RP FUNCTION.
RX PubMed=15678184; DOI=10.1039/b414739a;
RA Patching S.G., Baldwin S.A., Baldwin A.D., Young J.D., Gallagher M.P.,
RA Henderson P.J., Herbert R.B.;
RT "The nucleoside transport proteins, NupC and NupG, from Escherichia coli:
RT specific structural motifs necessary for the binding of ligands.";
RL Org. Biomol. Chem. 3:462-470(2005).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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 [9] {ECO:0007744|PDB:7DL9, ECO:0007744|PDB:7DLA}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF WILD-TYPE AND MUTANT ALA-323,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF ARG-136; THR-140;
RP PHE-143; GLN-225; ASN-228; GLN-261; GLU-264; TYR-318; PHE-322 AND ASP-323.
RC STRAIN=K12masn;
RX PubMed=33640454; DOI=10.1016/j.jbc.2021.100479;
RA Wang C., Xiao Q., Duan H., Li J., Zhang J., Wang Q., Guo L., Hu J., Sun B.,
RA Deng D.;
RT "Molecular basis for substrate recognition by the bacterial nucleoside
RT transporter NupG.";
RL J. Biol. Chem. 296:100479-100479(2021).
CC -!- FUNCTION: Broad-specificity transporter of purine and pyrimidine
CC nucleosides (PubMed:374403, PubMed:15678184, PubMed:3311747,
CC PubMed:11466294, PubMed:15513740). Can transport adenosine, uridine,
CC thymidine, cytidine, deoxycytidine, guanosine and inosine
CC (PubMed:374403, PubMed:15678184, PubMed:3311747, PubMed:11466294,
CC PubMed:15513740). Can also transport xanthosine, but with a very low
CC affinity (PubMed:11466294). Transport is driven by a proton motive
CC force (PubMed:374403, PubMed:15513740). {ECO:0000269|PubMed:11466294,
CC ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:15678184,
CC ECO:0000269|PubMed:3311747, ECO:0000269|PubMed:374403}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(in) + H(+)(in) = adenosine(out) + H(+)(out);
CC Xref=Rhea:RHEA:29987, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335;
CC Evidence={ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:374403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + uridine(in) = H(+)(out) + uridine(out);
CC Xref=Rhea:RHEA:29951, ChEBI:CHEBI:15378, ChEBI:CHEBI:16704;
CC Evidence={ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:374403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + thymidine(in) = H(+)(out) + thymidine(out);
CC Xref=Rhea:RHEA:29955, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748;
CC Evidence={ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:374403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(in) + H(+)(in) = cytidine(out) + H(+)(out);
CC Xref=Rhea:RHEA:29983, ChEBI:CHEBI:15378, ChEBI:CHEBI:17562;
CC Evidence={ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:374403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine(in) + H(+)(in) = 2'-deoxycytidine(out) +
CC H(+)(out); Xref=Rhea:RHEA:29975, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15698; Evidence={ECO:0000269|PubMed:374403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(in) + H(+)(in) = guanosine(out) + H(+)(out);
CC Xref=Rhea:RHEA:70915, ChEBI:CHEBI:15378, ChEBI:CHEBI:16750;
CC Evidence={ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:374403};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + inosine(in) = H(+)(out) + inosine(out);
CC Xref=Rhea:RHEA:29963, ChEBI:CHEBI:15378, ChEBI:CHEBI:17596;
CC Evidence={ECO:0000269|PubMed:15513740};
CC -!- ACTIVITY REGULATION: Inhibited by the protonophore uncouplers 2,4-
CC dinitrophenol and carbonyl cyanide m-chlorophenylhydrazone (CCCP), and
CC by valinomycin (PubMed:15513740, PubMed:374403). Inhibited by the
CC nucleoside antibiotic showdomycin (PubMed:374403).
CC {ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:374403}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23.6 uM for uridine {ECO:0000269|PubMed:15513740};
CC KM=20.6 uM for adenosine {ECO:0000269|PubMed:15513740};
CC Vmax=67.2 nmol/min/mg enzyme with uridine as substrate
CC {ECO:0000269|PubMed:15513740};
CC Vmax=56.8 nmol/min/mg enzyme with adenosine as substrate
CC {ECO:0000269|PubMed:15513740};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02049, ECO:0000269|PubMed:15513740,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:3311747,
CC ECO:0000269|PubMed:33640454}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02049, ECO:0000269|PubMed:33640454}.
CC -!- INDUCTION: Transcriptionally regulated by CytR and DeoR.
CC {ECO:0000305|PubMed:3311747}.
CC -!- MISCELLANEOUS: Binding of nucleosides to NupG requires the presence of
CC hydroxyl groups at each of the C-3' and C-5' positions of ribose.
CC {ECO:0000269|PubMed:15678184}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Nucleoside:H(+) symporter (NHS) (TC 2.A.1.10) family.
CC {ECO:0000255|HAMAP-Rule:MF_02049, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69132.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X06174; CAA29541.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69132.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76001.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77027.1; -; Genomic_DNA.
DR RefSeq; NP_417439.4; NC_000913.3.
DR RefSeq; WP_001049791.1; NZ_STEB01000001.1.
DR PDB; 7DL9; X-ray; 3.00 A; A/B=1-418.
DR PDB; 7DLA; X-ray; 3.00 A; A=1-418.
DR PDBsum; 7DL9; -.
DR PDBsum; 7DLA; -.
DR AlphaFoldDB; P0AFF4; -.
DR SMR; P0AFF4; -.
DR BioGRID; 4262362; 113.
DR IntAct; P0AFF4; 1.
DR STRING; 511145.b2964; -.
DR TCDB; 2.A.1.10.1; the major facilitator superfamily (mfs).
DR jPOST; P0AFF4; -.
DR PaxDb; P0AFF4; -.
DR PRIDE; P0AFF4; -.
DR EnsemblBacteria; AAC76001; AAC76001; b2964.
DR EnsemblBacteria; BAE77027; BAE77027; BAE77027.
DR GeneID; 66673154; -.
DR GeneID; 946282; -.
DR KEGG; ecj:JW2932; -.
DR KEGG; eco:b2964; -.
DR PATRIC; fig|1411691.4.peg.3766; -.
DR EchoBASE; EB0658; -.
DR eggNOG; COG2211; Bacteria.
DR HOGENOM; CLU_013133_1_2_6; -.
DR InParanoid; P0AFF4; -.
DR OMA; FMMMTNG; -.
DR PhylomeDB; P0AFF4; -.
DR BioCyc; EcoCyc:NUPG-MON; -.
DR BioCyc; MetaCyc:NUPG-MON; -.
DR PRO; PR:P0AFF4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015212; F:cytidine transmembrane transporter activity; IMP:EcoliWiki.
DR GO; GO:0015506; F:nucleoside:proton symporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015214; F:pyrimidine nucleoside transmembrane transporter activity; IDA:EcoliWiki.
DR GO; GO:0015213; F:uridine transmembrane transporter activity; IDA:EcoliWiki.
DR GO; GO:0032238; P:adenosine transport; IMP:EcoliWiki.
DR GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR GO; GO:0015860; P:purine nucleoside transmembrane transport; IMP:EcoliWiki.
DR GO; GO:0015864; P:pyrimidine nucleoside transport; IDA:EcoliWiki.
DR GO; GO:0015862; P:uridine transport; IDA:EcoliWiki.
DR Gene3D; 1.20.1250.20; -; 2.
DR HAMAP; MF_02049; NupG; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004740; Nuc_H_symport.
DR InterPro; IPR033667; NupG.
DR Pfam; PF03825; Nuc_H_symport; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00889; 2A0110; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..418
FT /note="Nucleoside permease NupG"
FT /id="PRO_0000058005"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 5..29
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 30..36
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 59..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 89..91
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 114..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 157..158
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 179..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 210..236
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 237..247
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 269..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 281..300
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 301..305
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 327..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 347..369
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 370..379
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TRANSMEM 380..403
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:33640454,
FT ECO:0007744|PDB:7DL9"
FT TOPO_DOM 404..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:33640454, ECO:0007744|PDB:7DL9"
FT MUTAGEN 136
FT /note="R->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 140
FT /note="T->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 143
FT /note="F->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 225
FT /note="Q->A: No change in the binding affinity for
FT uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 228
FT /note="N->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 261
FT /note="Q->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 264
FT /note="E->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 318
FT /note="Y->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 322
FT /note="F->A: Abolishes the binding affinity for uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT MUTAGEN 323
FT /note="D->A: 20-fold increase in the binding affinity for
FT uridine."
FT /evidence="ECO:0000269|PubMed:33640454"
FT CONFLICT 3
FT /note="L -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:7DL9"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 37..64
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 128..153
FT /evidence="ECO:0007829|PDB:7DL9"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:7DLA"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:7DL9"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:7DLA"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 208..221
FT /evidence="ECO:0007829|PDB:7DL9"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 226..236
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:7DL9"
FT TURN 242..246
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 280..299
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 305..335
FT /evidence="ECO:0007829|PDB:7DL9"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 342..371
FT /evidence="ECO:0007829|PDB:7DL9"
FT HELIX 380..402
FT /evidence="ECO:0007829|PDB:7DL9"
SQ SEQUENCE 418 AA; 46389 MW; 01337ECEFC369266 CRC64;
MNLKLQLKIL SFLQFCLWGS WLTTLGSYMF VTLKFDGASI GAVYSSLGIA AVFMPALLGI
VADKWLSAKW VYAICHTIGA ITLFMAAQVT TPEAMFLVIL INSFAYMPTL GLINTISYYR
LQNAGMDIVT DFPPIRIWGT IGFIMAMWVV SLSGFELSHM QLYIGAALSA ILVLFTLTLP
HIPVAKQQAN QSWTTLLGLD AFALFKNKRM AIFFIFSMLL GAELQITNMF GNTFLHSFDK
DPMFASSFIV QHASIIMSIS QISETLFILT IPFFLSRYGI KNVMMISIVA WILRFALFAY
GDPTPFGTVL LVLSMIVYGC AFDFFNISGS VFVEKEVSPA IRASAQGMFL MMTNGFGCIL
GGIVSGKVVE MYTQNGITDW QTVWLIFAGY SVVLAFAFMA MFKYKHVRVP TGTQTVSH
