WECA_ECOLI
ID WECA_ECOLI Reviewed; 367 AA.
AC P0AC78; P24235; P76751; Q2M892; Q9F8C8;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000305};
DE EC=2.7.8.33 {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000269|PubMed:17237164, ECO:0000269|PubMed:9134438};
DE AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000303|PubMed:1730666};
DE AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000255|HAMAP-Rule:MF_02030};
GN Name=wecA {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000303|PubMed:10629198};
GN Synonyms=rfe {ECO:0000303|PubMed:1722555}; OrderedLocusNames=b3784, JW3758;
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=1722555; DOI=10.1111/j.1365-2958.1991.tb00809.x;
RA Ohta M., Ina K., Kusuzaki K., Kido N., Arakawa Y., Kato N.;
RT "Cloning and expression of the rfe-rff gene cluster of Escherichia coli.";
RL Mol. Microbiol. 5:1853-1862(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN ECA BIOSYNTHESIS, AND
RP PATHWAY.
RC STRAIN=K12, and O8:K27;
RX PubMed=1730666; DOI=10.1016/s0021-9258(18)48347-0;
RA Meier-Dieter U., Barr K., Starman R., Hatch L., Rick P.D.;
RT "Nucleotide sequence of the Escherichia coli rfe gene involved in the
RT synthesis of enterobacterial common antigen. Molecular cloning of the rfe-
RT rff gene cluster.";
RL J. Biol. Chem. 267:746-753(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MB2884;
RX PubMed=11024259; DOI=10.1111/j.1574-6968.2000.tb09335.x;
RA Anderson M.S., Eveland S.S., Price N.P.J.;
RT "Conserved cytoplasmic motifs that distinguish sub-groups of the polyprenol
RT phosphate:N-acetylhexosamine-1-phosphate transferase family.";
RL FEMS Microbiol. Lett. 191:169-175(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [5]
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 [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=9134438; DOI=10.1093/glycob/7.2.315;
RA Rush J.S., Rick P.D., Waechter C.J.;
RT "Polyisoprenyl phosphate specificity of UDP-GlcNAc:undecaprenyl phosphate
RT N-acetylglucosaminyl 1-P transferase from E.coli.";
RL Glycobiology 7:315-322(1997).
RN [8]
RP IDENTIFICATION OF START CODON.
RX PubMed=10629198; DOI=10.1128/jb.182.2.498-503.2000;
RA Amer A.O., Valvano M.A.;
RT "The N-terminal region of the Escherichia coli WecA (Rfe) protein,
RT containing three predicted transmembrane helices, is required for function
RT but not for membrane insertion.";
RL J. Bacteriol. 182:498-503(2000).
RN [9]
RP FUNCTION IN LPS O-ANTIGEN BIOSYNTHESIS, SUBCELLULAR LOCATION, PATHWAY, AND
RP MUTAGENESIS OF ARG-265; HIS-279 AND 279-HIS--HIS-282.
RX PubMed=11700352; DOI=10.1099/00221287-147-11-3015;
RA Amer A.O., Valvano M.A.;
RT "Conserved amino acid residues found in a predicted cytosolic domain of the
RT lipopolysaccharide biosynthetic protein WecA are implicated in the
RT recognition of UDP-N-acetylglucosamine.";
RL Microbiology 147:3015-3025(2001).
RN [10]
RP MUTAGENESIS OF ASP-35; 90-ASP-ASP-91; ASP-94; ASP-156; 156-ASP--ASP-159;
RP ASP-159 AND ASP-276.
RX PubMed=11832520; DOI=10.1099/00221287-148-2-571;
RA Amer A.O., Valvano M.A.;
RT "Conserved aspartic acids are essential for the enzymic activity of the
RT WecA protein initiating the biosynthesis of O-specific lipopolysaccharide
RT and enterobacterial common antigen in Escherichia coli.";
RL Microbiology 148:571-582(2002).
RN [11]
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 [12]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF ASP-90; ASP-91; ASP-156
RP AND ASP-159.
RX PubMed=17237164; DOI=10.1128/jb.01905-06;
RA Lehrer J., Vigeant K.A., Tatar L.D., Valvano M.A.;
RT "Functional characterization and membrane topology of Escherichia coli
RT WecA, a sugar-phosphate transferase initiating the biosynthesis of
RT enterobacterial common antigen and O-antigen lipopolysaccharide.";
RL J. Bacteriol. 189:2618-2628(2007).
CC -!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from
CC UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P),
CC yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). It is the
CC first lipid-linked intermediate involved in enterobacterial common
CC antigen (ECA) synthesis, and an acceptor for the addition of subsequent
CC sugars to complete the biosynthesis of O-antigen lipopolysaccharide
CC (LPS) in many E.coli O types. The apparent affinity of WecA for the
CC polyisoprenyl phosphate substrates increases with the polyisoprenyl
CC chain length. WecA is unable to utilize dolichyl phosphate (Dol-P).
CC {ECO:0000269|PubMed:11700352, ECO:0000269|PubMed:17237164,
CC ECO:0000269|PubMed:1730666, ECO:0000269|PubMed:9134438}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-
CC undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:28090,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392,
CC ChEBI:CHEBI:62959; EC=2.7.8.33; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02030, ECO:0000269|PubMed:17237164,
CC ECO:0000269|PubMed:9134438};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02030,
CC ECO:0000269|PubMed:17237164};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02030,
CC ECO:0000269|PubMed:17237164};
CC -!- ACTIVITY REGULATION: Inhibited by tunicamycin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.6 uM for UDP-GlcNAc {ECO:0000269|PubMed:9134438};
CC KM=0.12 uM for UDP-GlcNAc (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:17237164};
CC KM=0.19 uM for UDP-GlcNAc (in the presence of Mn(2+))
CC {ECO:0000269|PubMed:17237164};
CC KM=1.7 mM for Mg(2+) {ECO:0000269|PubMed:17237164};
CC KM=0.3 mM for Mn(2+) {ECO:0000269|PubMed:17237164};
CC Vmax=57 pmol/min/mg enzyme (in the presence of Mg(2+))
CC {ECO:0000269|PubMed:17237164};
CC Vmax=56 pmol/min/mg enzyme (in the presence of Mn(2+))
CC {ECO:0000269|PubMed:17237164};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030,
CC ECO:0000269|PubMed:11700352}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; enterobacterial common
CC antigen biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02030,
CC ECO:0000269|PubMed:1730666}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02030, ECO:0000269|PubMed:11700352,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:17237164}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_02030}. Note=Localizes to
CC discrete regions in the plasma membrane. {ECO:0000269|PubMed:17237164}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02030, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24526.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB20842.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S75640; AAB20842.1; ALT_INIT; Genomic_DNA.
DR EMBL; M76129; AAA24526.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF248031; AAG26342.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67584.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76789.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77514.1; -; Genomic_DNA.
DR PIR; C65182; C65182.
DR RefSeq; NP_418231.1; NC_000913.3.
DR RefSeq; WP_001050960.1; NZ_STEB01000021.1.
DR AlphaFoldDB; P0AC78; -.
DR SMR; P0AC78; -.
DR BioGRID; 4263322; 318.
DR DIP; DIP-48083N; -.
DR IntAct; P0AC78; 1.
DR STRING; 511145.b3784; -.
DR TCDB; 9.B.146.1.7; the putative undecaprenyl-phosphate n-acetylglucosaminyl transferase (murg) family.
DR PaxDb; P0AC78; -.
DR PRIDE; P0AC78; -.
DR DNASU; 948789; -.
DR EnsemblBacteria; AAC76789; AAC76789; b3784.
DR EnsemblBacteria; BAE77514; BAE77514; BAE77514.
DR GeneID; 66672313; -.
DR GeneID; 948789; -.
DR KEGG; ecj:JW3758; -.
DR KEGG; eco:b3784; -.
DR PATRIC; fig|511145.12.peg.3900; -.
DR EchoBASE; EB0833; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_1_0_6; -.
DR InParanoid; P0AC78; -.
DR OMA; MCLGFLP; -.
DR PhylomeDB; P0AC78; -.
DR BioCyc; EcoCyc:GLCNACPTRANS-MON; -.
DR BioCyc; MetaCyc:GLCNACPTRANS-MON; -.
DR BRENDA; 2.7.8.33; 2026.
DR BRENDA; 2.7.8.35; 2026.
DR UniPathway; UPA00281; -.
DR UniPathway; UPA00566; -.
DR PRO; PR:P0AC78; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IDA:EcoliWiki.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IDA:UniProtKB.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IMP:EcoCyc.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02030; WecA_Gammaproteo; 1.
DR InterPro; IPR012750; ECA_WecA-rel.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR PANTHER; PTHR22926; PTHR22926; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR TIGRFAMs; TIGR02380; ECA_wecA; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Magnesium; Manganese; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..367
FT /note="Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-
FT phosphate transferase"
FT /id="PRO_0000108941"
FT TOPO_DOM 1..2
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..68
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17237164"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..131
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17237164"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..186
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..241
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:17237164"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..317
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:17237164"
FT SITE 90
FT /note="Important in orienting the substrate"
FT /evidence="ECO:0000305|PubMed:11832520,
FT ECO:0000305|PubMed:17237164"
FT SITE 91
FT /note="Important in orienting the substrate; probably
FT interacts with magnesium or manganese"
FT /evidence="ECO:0000305|PubMed:11832520,
FT ECO:0000305|PubMed:17237164"
FT SITE 156
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000305|PubMed:11832520,
FT ECO:0000305|PubMed:17237164"
FT SITE 159
FT /note="Could be required for catalysis"
FT /evidence="ECO:0000305|PubMed:11832520,
FT ECO:0000305|PubMed:17237164"
FT MUTAGEN 35
FT /note="D->G: Decrease in activity; both in vivo and in
FT vitro."
FT /evidence="ECO:0000269|PubMed:11832520"
FT MUTAGEN 90..91
FT /note="DD->EE,GG: Loss of activity in vivo. Decrease in
FT activity in vitro. No change in binding to tunicamycin."
FT /evidence="ECO:0000269|PubMed:11832520"
FT MUTAGEN 90
FT /note="D->E,N: Reduces slightly the velocity and shows a
FT small increase of the affinity for the transferase."
FT /evidence="ECO:0000269|PubMed:17237164"
FT MUTAGEN 91
FT /note="D->N: Reduces slightly the velocity and shows a
FT small increase of the affinity for the transferase."
FT /evidence="ECO:0000269|PubMed:17237164"
FT MUTAGEN 94
FT /note="D->G: No loss in activity; both in vivo and in
FT vitro."
FT /evidence="ECO:0000269|PubMed:11832520"
FT MUTAGEN 156
FT /note="D->E,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11832520,
FT ECO:0000269|PubMed:17237164"
FT MUTAGEN 156
FT /note="D->E: Loss of activity; both in vivo and in vitro;
FT when associated with E-159."
FT /evidence="ECO:0000269|PubMed:11832520,
FT ECO:0000269|PubMed:17237164"
FT MUTAGEN 156
FT /note="D->G: Loss of activity; both in vivo and in vitro.
FT No binding to tunicamycin; when associated with G-159."
FT /evidence="ECO:0000269|PubMed:11832520,
FT ECO:0000269|PubMed:17237164"
FT MUTAGEN 159
FT /note="D->E,N: The activity is detectable but drastically
FT reduced."
FT /evidence="ECO:0000269|PubMed:11832520,
FT ECO:0000269|PubMed:17237164"
FT MUTAGEN 159
FT /note="D->E: Loss of activity; both in vivo and in vitro;
FT when associated with E-156."
FT /evidence="ECO:0000269|PubMed:11832520,
FT ECO:0000269|PubMed:17237164"
FT MUTAGEN 159
FT /note="D->G: Loss of activity; both in vivo and in vitro.
FT No binding to tunicamycin; when associated with G-156."
FT /evidence="ECO:0000269|PubMed:11832520,
FT ECO:0000269|PubMed:17237164"
FT MUTAGEN 265
FT /note="R->K: Decrease in activity. Reduces binding to
FT tunicamycin."
FT /evidence="ECO:0000269|PubMed:11700352"
FT MUTAGEN 276
FT /note="D->G: No loss of activity; both in vivo and in
FT vitro."
FT /evidence="ECO:0000269|PubMed:11832520"
FT MUTAGEN 279..282
FT /note="HIHH->GGGG: Loss of activity. No binding to
FT tunicamycin."
FT /evidence="ECO:0000269|PubMed:11700352"
FT MUTAGEN 279
FT /note="H->S: Loss of activity. No binding to tunicamycin."
FT /evidence="ECO:0000269|PubMed:11700352"
FT CONFLICT 8
FT /note="T -> I (in Ref. 1; AAB20842)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> V (in Ref. 1; AAB20842)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="K -> N (in Ref. 3; AAG26342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 40957 MW; 6EB11CC80C6B9CC8 CRC64;
MNLLTVSTDL ISIFLFTTLF LFFARKVAKK VGLVDKPNFR KRHQGLIPLV GGISVYAGIC
FTFGIVDYYI PHASLYLACA GVLVFIGALD DRFDISVKIR ATIQAAVGIV MMVFGKLYLS
SLGYIFGSWE MVLGPFGYFL TLFAVWAAIN AFNMVDGIDG LLGGLSCVSF AAIGMILWFD
GQTSLAIWCF AMIAAILPYI MLNLGILGRR YKVFMGDAGS TLIGFTVIWI LLETTQGKTH
PISPVTALWI IAIPLMDMVA IMYRRLRKGM SPFSPDRQHI HHLIMRAGFT SRQAFVLITL
AAALLASIGV LAEYSHFVPE WVMLVLFLLA FFLYGYCIKR AWKVARFIKR VKRRLRRNRG
GSPNLTK
