ID GLFT2_MYCTU Reviewed; 637 AA. AC O53585; L0TFB5; DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 03-MAY-2023, entry version 112. DE RecName: Full=Galactofuranosyltransferase GlfT2 {ECO:0000305}; DE Short=GalTr 2 {ECO:0000305}; DE EC=2.4.1.288 {ECO:0000269|PubMed:18055597, ECO:0000269|PubMed:19571009, ECO:0000305|PubMed:16704275}; DE AltName: Full=Arabinogalactan galactosyltransferase 2 {ECO:0000305}; DE AltName: Full=Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase; DE AltName: Full=Polymerizing galactofuranosyltransferase GlfT2 {ECO:0000305}; GN Name=glfT2 {ECO:0000303|PubMed:18423586, ECO:0000312|EMBL:CCP46637.1}; GN Synonyms=glfT {ECO:0000303|PubMed:11304545, ECO:0000303|PubMed:16704275}; GN OrderedLocusNames=Rv3808c; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinomycetota; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., RA Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the complete RT genome sequence."; RL Nature 393:537-544(1998). RN [2] RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE. RX PubMed=10934214; DOI=10.1074/jbc.m006875200; RA Mikusova K., Yagi T., Stern R., McNeil M.R., Besra G.S., Crick D.C., RA Brennan P.J.; RT "Biosynthesis of the galactan component of the mycobacterial cell wall."; RL J. Biol. Chem. 275:33890-33897(2000). RN [3] RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE, SUBCELLULAR LOCATION, AND RP PATHWAY. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=11304545; DOI=10.1074/jbc.m102022200; RA Kremer L., Dover L.G., Morehouse C., Hitchin P., Everett M., Morris H.R., RA Dell A., Brennan P.J., McNeil M.R., Flaherty C., Duncan K., Besra G.S.; RT "Galactan biosynthesis in Mycobacterium tuberculosis. Identification of a RT bifunctional UDP-galactofuranosyltransferase."; RL J. Biol. Chem. 276:26430-26440(2001). RN [4] RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND PATHWAY. RX PubMed=16704275; DOI=10.1021/ja058254d; RA Rose N.L., Completo G.C., Lin S.J., McNeil M., Palcic M.M., Lowary T.L.; RT "Expression, purification, and characterization of a RT galactofuranosyltransferase involved in Mycobacterium tuberculosis RT arabinogalactan biosynthesis."; RL J. Am. Chem. Soc. 128:6721-6729(2006). RN [5] RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS]. RX PubMed=19099550; DOI=10.1186/1752-0509-2-109; RA Raman K., Yeturu K., Chandra N.; RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis RT through an interactome, reactome and genome-scale structural analysis."; RL BMC Syst. Biol. 2:109-109(2008). RN [6] RP FUNCTION AS A GALACTOFURANOSYLTRANSFERASE, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=18423586; DOI=10.1016/j.carres.2008.03.023; RA Rose N.L., Zheng R.B., Pearcey J., Zhou R., Completo G.C., Lowary T.L.; RT "Development of a coupled spectrophotometric assay for GlfT2, a RT bifunctional mycobacterial galactofuranosyltransferase."; RL Carbohydr. Res. 343:2130-2139(2008). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=18055597; DOI=10.1128/jb.01326-07; RA Belanova M., Dianiskova P., Brennan P.J., Completo G.C., Rose N.L., RA Lowary T.L., Mikusova K.; RT "Galactosyl transferases in mycobacterial cell wall synthesis."; RL J. Bacteriol. 190:1141-1145(2008). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND POLYMER LENGTH CONTROL. RC STRAIN=H37Rv; RX PubMed=19571009; DOI=10.1073/pnas.0901407106; RA May J.F., Splain R.A., Brotschi C., Kiessling L.L.; RT "A tethering mechanism for length control in a processive carbohydrate RT polymerization."; RL Proc. Natl. Acad. Sci. U.S.A. 106:11851-11856(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.m111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution RT mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEXES WITH UDP AND MANGANESE RP IONS, MUTAGENESIS OF GLU-300; ASP-371; ASP-372; TRP-399 AND HIS-413, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVE SITE, AND SUBUNIT. RX PubMed=22707726; DOI=10.1074/jbc.m112.347484; RA Wheatley R.W., Zheng R.B., Richards M.R., Lowary T.L., Ng K.K.; RT "Tetrameric structure of the GlfT2 galactofuranosyltransferase reveals a RT scaffold for the assembly of mycobacterial arabinogalactan."; RL J. Biol. Chem. 287:28132-28143(2012). CC -!- FUNCTION: Involved in the galactan polymerization of the CC arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan CC (mAGP) complex, an essential component of the mycobacteria cell wall. CC Thus, successively transfers approximately 28 galactofuranosyl (Galf) CC residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl- CC galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha- CC GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and CC 1->6 links, forming a galactan domain with approximately 30 CC galactofuranosyl residues. {ECO:0000269|PubMed:18055597, CC ECO:0000269|PubMed:19571009, ECO:0000305|PubMed:10934214, CC ECO:0000305|PubMed:11304545, ECO:0000305|PubMed:16704275, CC ECO:0000305|PubMed:18423586}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)- CC alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho- CC trans,octa-cis-decaprenol + 28 UDP-alpha-D-galactofuranose = [beta-D- CC galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D- CC galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L- CC rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho- CC trans,octa-cis-decaprenol + 28 H(+) + 28 UDP; Xref=Rhea:RHEA:34391, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66915, CC ChEBI:CHEBI:67210, ChEBI:CHEBI:67212; EC=2.4.1.288; CC Evidence={ECO:0000269|PubMed:18055597, ECO:0000269|PubMed:19571009, CC ECO:0000305|PubMed:16704275}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000305|PubMed:22707726}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000305|PubMed:22707726}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.38 mM for UDP-Galf {ECO:0000269|PubMed:18423586, CC ECO:0000269|PubMed:22707726}; CC KM=0.60 mM for beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf- CC octyl {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726}; CC KM=1.7 mM for beta-D-Galf-(1->5)-beta-D-Galf-octyl CC {ECO:0000269|PubMed:16704275}; CC KM=0.635 mM for beta-D-Galf-(1->6)-beta-D-Galf-octyl CC {ECO:0000269|PubMed:16704275}; CC KM=0.208 mM for beta-D-Galf-(1->5)-beta-D-Galf-(1->6)-beta-D-Galf- CC octyl {ECO:0000269|PubMed:16704275}; CC KM=0.204 mM for beta-D-Galf-(1->6)-beta-D-Galf-(1->5)-beta-D-Galf- CC octyl {ECO:0000269|PubMed:16704275}; CC Vmax=4.4 umol/min/mg enzyme for galtactose transfer on beta-D-Galf- CC (1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl CC {ECO:0000269|PubMed:16704275, ECO:0000269|PubMed:18423586}; CC Note=kcat is 430 min(-1) for galtactose transfer on beta-D-Galf- CC (1->5)-beta-D-Galf-(1->6)-beta-D-Galf-octyl. CC {ECO:0000269|PubMed:18423586, ECO:0000269|PubMed:22707726}; CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis. CC {ECO:0000305|PubMed:11304545, ECO:0000305|PubMed:16704275}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22707726}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11304545}. CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target. CC {ECO:0000305|PubMed:19099550}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL123456; CCP46637.1; -; Genomic_DNA. DR PIR; D70888; D70888. DR RefSeq; NP_218325.1; NC_000962.3. DR RefSeq; WP_003900761.1; NZ_NVQJ01000022.1. DR PDB; 4FIX; X-ray; 2.45 A; A/B=1-637. DR PDB; 4FIY; X-ray; 3.10 A; A/B=1-637. DR PDBsum; 4FIX; -. DR PDBsum; 4FIY; -. DR AlphaFoldDB; O53585; -. DR SMR; O53585; -. DR STRING; 83332.Rv3808c; -. DR BindingDB; O53585; -. DR ChEMBL; CHEMBL1075096; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR PaxDb; O53585; -. DR DNASU; 886136; -. DR GeneID; 886136; -. DR KEGG; mtu:Rv3808c; -. DR TubercuList; Rv3808c; -. DR eggNOG; COG1216; Bacteria. DR OMA; NGWWMCL; -. DR OrthoDB; 3225550at2; -. DR PhylomeDB; O53585; -. DR BioCyc; MetaCyc:G185E-8104-MON; -. DR BRENDA; 2.4.1.288; 3445. DR UniPathway; UPA00963; -. DR PRO; PR:O53585; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005829; C:cytosol; HDA:MTBBASE. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB. DR GO; GO:0035496; F:lipopolysaccharide-1,5-galactosyltransferase activity; IDA:MTBBASE. DR GO; GO:0008921; F:lipopolysaccharide-1,6-galactosyltransferase activity; IDA:MTBBASE. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IDA:UniProtKB. DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:MTBBASE. DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway. 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:0070592; P:cell wall polysaccharide biosynthetic process; IDA:MTBBASE. DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IDA:MTBBASE. DR GO; GO:0071769; P:mycolate cell wall layer assembly; IDA:MTBBASE. DR GO; GO:0052573; P:UDP-D-galactose metabolic process; IDA:MTBBASE. DR Gene3D; 3.90.550.60; -; 1. DR InterPro; IPR045699; GlfT2_C. DR InterPro; IPR040492; GlfT2_N. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR43179:SF9; GALACTOFURANOSYLTRANSFERASE GLFT2; 1. DR PANTHER; PTHR43179; RHAMNOSYLTRANSFERASE WBBL; 1. DR Pfam; PF19320; GlfT2_domain3; 1. DR Pfam; PF17994; Glft2_N; 1. DR Pfam; PF13641; Glyco_tranf_2_3; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cell wall biogenesis/degradation; KW Glycosyltransferase; Magnesium; Manganese; Membrane; Metal-binding; KW Reference proteome; Transferase. FT CHAIN 1..637 FT /note="Galactofuranosyltransferase GlfT2" FT /id="PRO_0000395356" FT ACT_SITE 372 FT /note="Proton acceptor" FT /evidence="ECO:0000305|PubMed:22707726" FT BINDING 171 FT /ligand="UDP-alpha-D-galactofuranose" FT /ligand_id="ChEBI:CHEBI:66915" FT /evidence="ECO:0000305|PubMed:22707726" FT BINDING 200 FT /ligand="UDP-alpha-D-galactofuranose" FT /ligand_id="ChEBI:CHEBI:66915" FT /evidence="ECO:0000305|PubMed:22707726" FT BINDING 229 FT /ligand="UDP-alpha-D-galactofuranose" FT /ligand_id="ChEBI:CHEBI:66915" FT /evidence="ECO:0000305|PubMed:22707726" FT BINDING 256 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:22707726" FT BINDING 256 FT /ligand="UDP-alpha-D-galactofuranose" FT /ligand_id="ChEBI:CHEBI:66915" FT /evidence="ECO:0000305|PubMed:22707726" FT BINDING 258 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:22707726" FT BINDING 396 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:22707726" FT MUTAGEN 300 FT /note="E->S: 1400-fold decrease in transferase activity. No FT effect on affinity for the substrate UDP-Galf." FT /evidence="ECO:0000269|PubMed:22707726" FT MUTAGEN 371 FT /note="D->S: Loss of transferase activity." FT /evidence="ECO:0000269|PubMed:22707726" FT MUTAGEN 372 FT /note="D->S: Loss of transferase activity." FT /evidence="ECO:0000269|PubMed:22707726" FT MUTAGEN 399 FT /note="W->S: 1200-fold decrease in transferase activity. No FT effect on affinity for the substrate UDP-Galf." FT /evidence="ECO:0000269|PubMed:22707726" FT MUTAGEN 413 FT /note="H->S: 1700-fold decrease in transferase activity. No FT effect on affinity for the substrate UDP-Galf." FT /evidence="ECO:0000269|PubMed:22707726" FT HELIX 3..7 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 8..11 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:4FIX" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 39..42 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:4FIX" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 65..71 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 75..94 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 100..110 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 116..124 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 133..141 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 143..151 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 172..182 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 186..189 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 205..207 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 211..218 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 222..226 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 231..246 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 250..255 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 257..261 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 264..275 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 281..288 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 300..303 FT /evidence="ECO:0007829|PDB:4FIX" FT TURN 304..307 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 308..311 FT /evidence="ECO:0007829|PDB:4FIX" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 354..360 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 367..370 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 371..381 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 386..396 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 399..402 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:4FIY" FT HELIX 409..424 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 429..431 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 432..448 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 452..466 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 469..474 FT /evidence="ECO:0007829|PDB:4FIX" FT TURN 475..478 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 479..487 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 491..493 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 494..497 FT /evidence="ECO:0007829|PDB:4FIY" FT HELIX 499..501 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 518..532 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 538..541 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 545..548 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 555..558 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 562..567 FT /evidence="ECO:0007829|PDB:4FIX" FT STRAND 574..578 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 581..611 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 613..617 FT /evidence="ECO:0007829|PDB:4FIX" FT HELIX 619..626 FT /evidence="ECO:0007829|PDB:4FIX" SQ SEQUENCE 637 AA; 71507 MW; D7C9AB28B5005B66 CRC64; MSELAASLLS RVILPRPGEP LDVRKLYLEE STTNARRAHA PTRTSLQIGA ESEVSFATYF NAFPASYWRR WTTCKSVVLR VQVTGAGRVD VYRTKATGAR IFVEGHDFTG TEDQPAAVET EVVLQPFEDG GWVWFDITTD TAVTLHSGGW YATSPAPGTA NIAVGIPTFN RPADCVNALR ELTADPLVDQ VIGAVIVPDQ GERKVRDHPD FPAAAARLGS RLSIHDQPNL GGSGGYSRVM YEALKNTDCQ QILFMDDDIR LEPDSILRVL AMHRFAKAPM LVGGQMLNLQ EPSHLHIMGE VVDRSIFMWT AAPHAEYDHD FAEYPLNDNN SRSKLLHRRI DVDYNGWWTC MIPRQVAEEL GQPLPLFIKW DDADYGLRAA EHGYPTVTLP GAAIWHMAWS DKDDAIDWQA YFHLRNRLVV AAMHWDGPKA QVIGLVRSHL KATLKHLACL EYSTVAIQNK AIDDFLAGPE HIFSILESAL PQVHRIRKSY PDAVVLPAAS ELPPPLHKNK AMKPPVNPLV IGYRLARGIM HNLTAANPQH HRRPEFNVPT QDARWFLLCT VDGATVTTAD GCGVVYRQRD RAKMFALLWQ SLRRQRQLLK RFEEMRRIYR DALPTLSSKQ KWETALLPAA NQEPEHG //