ID TPS1_YEAST Reviewed; 495 AA. AC Q00764; D6VQC3; Q01801; Q05168; Q6J5J4; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit; DE EC=2.4.1.15 {ECO:0000269|PubMed:2546763}; DE AltName: Full=General glucose sensor subunit 1; DE AltName: Full=Glycogen metabolism control protein GLC6; DE AltName: Full=Trehalose synthase complex catalytic subunit TPS1; DE AltName: Full=Trehalose-6-phosphate synthase; DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase; GN Name=TPS1 {ECO:0000303|PubMed:8467996}; GN Synonyms=BYP1, CIF1, FDP1, GGS1, GLC6, TSS1; GN OrderedLocusNames=YBR126C; ORFNames=YBR0922; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2521486; DOI=10.1016/s0021-9258(18)94254-7; RA Nelson H., Mandiyan S., Nelson N.; RT "A conserved gene encoding the 57-kDa subunit of the yeast vacuolar H+- RT ATPase."; RL J. Biol. Chem. 264:1775-1778(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C13-ABYS86; RX PubMed=1425702; DOI=10.1111/j.1432-1033.1992.tb17368.x; RA Bell W., Klaassen P., Ohnacker M., Boller T., Herweijer M., Schoppink P., RA van der Zee P., Wiemken A.; RT "Characterization of the 56-kDa subunit of yeast trehalose-6-phosphate RT synthase and cloning of its gene reveal its identity with the product of RT CIF1, a regulator of carbon catabolite inactivation."; RL Eur. J. Biochem. 209:951-959(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8467996; DOI=10.1016/0378-1097(93)90348-6; RA McDougall J., Kaasen I., Stroem A.R.; RT "A yeast gene for trehalose-6-phosphate synthase and its complementation of RT an Escherichia coli otsA mutant."; RL FEMS Microbiol. Lett. 107:25-30(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C836; RX PubMed=1315471; DOI=10.1002/yea.320080304; RA Gonzales M.I., Stucka R., Blazquez M.A., Feldmann H., Gancedo C.; RT "Molecular cloning of CIF1, a yeast gene necessary for growth on glucose."; RL Yeast 8:183-192(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8355617; DOI=10.1111/j.1365-2958.1993.tb01638.x; RA van Aelst L., Hohmann S., Bulaya B., de Koning W., Sierkstra L., RA Neves M.J., Luyten K., Alijo R., Ramos J., Coccetti P., Martegani E., RA de Magalhaes-Rocha N.M., Brandao R.L., van Dijck P., Vanhalewyn M., RA Durnez P., Jans A.W.H., Thevelein J.M.; RT "Molecular cloning of a gene involved in glucose sensing in the yeast RT Saccharomyces cerevisiae."; RL Mol. Microbiol. 8:927-943(1993). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF HIS-223. RX PubMed=8150278; DOI=10.1093/genetics/136.2.485; RA Cannon J.F., Pringle J.R., Fiechter A., Khalil M.; RT "Characterization of glycogen-deficient glc mutants of Saccharomyces RT cerevisiae."; RL Genetics 136:485-503(1994). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8404905; DOI=10.1111/j.1432-1033.1993.tb18207.x; RA Vuorio O.E., Kalkkinen N., Londesborough J.; RT "Cloning of two related genes encoding the 56-kDa and 123-kDa subunits of RT trehalose synthase from the yeast Saccharomyces cerevisiae."; RL Eur. J. Biochem. 216:849-861(1993). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=AS2.1416; RX PubMed=11059292; RA Dong Z.Y., Duan Y.K., Chen H.M., Jin C., Zhang S.Z.; RT "cDNA cloning, sequence analysis of trehalose-6-phosphate synthase gene RT from Saccharomyces cerevisiae AS2.1416."; RL Sheng Wu Gong Cheng Xue Bao 16:408-410(2000). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=FHS, and WFB; RA Ma X., Guo Y., Zhang F., Yu H., Kuang J., Yao J., Li Z., He G.; RT "Research on the mechanism of osmotolerance and thermotolerance of yeast."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8091856; DOI=10.1002/yea.320100002; RA Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., RA Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., RA Herbert C.J.; RT "The sequence of 29.7 kb from the right arm of chromosome II reveals 13 RT complete open reading frames, of which ten correspond to new genes."; RL Yeast 10:S1-S11(1994). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [12] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 291-495. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7900426; DOI=10.1002/yea.320101014; RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.; RT "Analysis of a 70 kb region on the right arm of yeast chromosome II."; RL Yeast 10:1363-1381(1994). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=2546763; DOI=10.1111/j.1432-1033.1989.tb14870.x; RA Vandercammen A., Francois J., Hers H.-G.; RT "Characterization of trehalose-6-phosphate synthase and trehalose-6- RT phosphate phosphatase of Saccharomyces cerevisiae."; RL Eur. J. Biochem. 182:613-620(1989). RN [16] RP ACTIVITY REGULATION. RX PubMed=8404904; DOI=10.1111/j.1432-1033.1993.tb18206.x; RA Londesborough J., Vuorio O.E.; RT "Purification of trehalose synthase from baker's yeast. Its temperature- RT dependent activation by fructose 6-phosphate and inhibition by phosphate."; RL Eur. J. Biochem. 216:841-848(1993). RN [17] RP FUNCTION, AND INTERACTION WITH TPS2; TPS3 AND TSL1. RX PubMed=9194697; DOI=10.1046/j.1365-2958.1997.3861749.x; RA Reinders A., Buerckert N., Hohmann S., Thevelein J.M., Boller T., RA Wiemken A., De Virgilio C.; RT "Structural analysis of the subunits of the trehalose-6-phosphate RT synthase/phosphatase complex in Saccharomyces cerevisiae and their function RT during heat shock."; RL Mol. Microbiol. 24:687-695(1997). RN [18] RP SUBUNIT. RX PubMed=9837904; DOI=10.1074/jbc.273.50.33311; RA Bell W., Sun W., Hohmann S., Wera S., Reinders A., De Virgilio C., RA Wiemken A., Thevelein J.M.; RT "Composition and functional analysis of the Saccharomyces cerevisiae RT trehalose synthase complex."; RL J. Biol. Chem. 273:33311-33319(1998). RN [19] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [20] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Synthase catalytic subunit of the trehalose synthase complex CC that catalyzes the production of trehalose from glucose-6-phosphate and CC UDP-alpha-D-glucose in a two step process. Can function independently CC of the complex. {ECO:0000269|PubMed:2546763, CC ECO:0000269|PubMed:9194697}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha- CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429, CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15; CC Evidence={ECO:0000269|PubMed:2546763}; CC -!- ACTIVITY REGULATION: Activated by fructose 6-phosphate. Inorganic CC phosphate inhibits the synthase activity in the complex, but activates CC the synthase activity in the free monomeric form. CC {ECO:0000269|PubMed:8404904}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=3.5 mM for D-glucose 6-phosphate {ECO:0000269|PubMed:2546763}; CC KM=0.5 mM for UDP-alpha-D-glucose {ECO:0000269|PubMed:2546763}; CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}. CC -!- SUBUNIT: The trehalose synthase complex is composed of the two CC catalytic subunits TPS1 and TPS2 and at least one of the two regulatory CC subunits TPS3 or TSL1. {ECO:0000269|PubMed:9837904}. CC -!- INTERACTION: CC Q00764; P31688: TPS2; NbExp=7; IntAct=EBI-19430, EBI-19440; CC Q00764; P38426: TPS3; NbExp=5; IntAct=EBI-19430, EBI-19448; CC Q00764; P38427: TSL1; NbExp=6; IntAct=EBI-19430, EBI-19638; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- INDUCTION: Either partial repression by glucose or induction by CC galactose. Induced by heat shock. CC -!- MISCELLANEOUS: Present with 10900 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA66891.1; Type=Frameshift; Evidence={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; J04450; AAA66891.1; ALT_FRAME; Genomic_DNA. DR EMBL; X68214; CAA48296.1; -; mRNA. DR EMBL; X68496; CAA48510.1; -; Genomic_DNA. DR EMBL; X67499; CAA47834.1; -; Genomic_DNA. DR EMBL; X61275; CAA43580.1; -; Genomic_DNA. DR EMBL; L21999; AAA53672.1; -; Genomic_DNA. DR EMBL; X78993; CAA55627.1; ALT_SEQ; Genomic_DNA. DR EMBL; X75891; CAA53485.1; -; Genomic_DNA. DR EMBL; AF061037; AAC16974.1; -; mRNA. DR EMBL; AY598966; AAT27376.1; -; Genomic_DNA. DR EMBL; AY598964; AAT27374.1; -; Genomic_DNA. DR EMBL; Z35995; CAA85083.1; -; Genomic_DNA. DR EMBL; AY693147; AAT93166.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07243.1; -; Genomic_DNA. DR PIR; S34979; S34979. DR RefSeq; NP_009684.1; NM_001178474.1. DR AlphaFoldDB; Q00764; -. DR SMR; Q00764; -. DR BioGRID; 32827; 517. DR ComplexPortal; CPX-582; Trehalose-6-phosphate synthase/phosphatase complex, tps3 variant. DR ComplexPortal; CPX-583; Trehalose-6-phosphate synthase/phosphatase complex, tsl1 variant. DR DIP; DIP-744N; -. DR IntAct; Q00764; 39. DR MINT; Q00764; -. DR STRING; 4932.YBR126C; -. DR CAZy; GT20; Glycosyltransferase Family 20. DR CarbonylDB; Q00764; -. DR iPTMnet; Q00764; -. DR MaxQB; Q00764; -. DR PaxDb; 4932-YBR126C; -. DR PeptideAtlas; Q00764; -. DR TopDownProteomics; Q00764; -. DR EnsemblFungi; YBR126C_mRNA; YBR126C; YBR126C. DR GeneID; 852423; -. DR KEGG; sce:YBR126C; -. DR AGR; SGD:S000000330; -. DR SGD; S000000330; TPS1. DR VEuPathDB; FungiDB:YBR126C; -. DR eggNOG; KOG1050; Eukaryota. DR GeneTree; ENSGT00940000167933; -. DR HOGENOM; CLU_002351_7_2_1; -. DR InParanoid; Q00764; -. DR OMA; RTIWPLF; -. DR OrthoDB; 1023at2759; -. DR BioCyc; MetaCyc:YBR126C-MONOMER; -. DR BioCyc; YEAST:YBR126C-MONOMER; -. DR BRENDA; 2.4.1.15; 984. DR SABIO-RK; Q00764; -. DR BioGRID-ORCS; 852423; 8 hits in 10 CRISPR screens. DR PRO; PR:Q00764; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; Q00764; Protein. DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IMP:SGD. DR GO; GO:0004805; F:trehalose-phosphatase activity; IMP:SGD. DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:SGD. DR GO; GO:0071465; P:cellular response to desiccation; IMP:SGD. DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central. DR GO; GO:0005992; P:trehalose biosynthetic process; IDA:SGD. DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central. DR CDD; cd03788; GT20_TPS; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR001830; Glyco_trans_20. DR InterPro; IPR012766; Trehalose_OtsA. DR NCBIfam; TIGR02400; trehalose_OtsA; 1. DR PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1. DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1. DR Pfam; PF00982; Glyco_transf_20; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 1: Evidence at protein level; KW Cytoplasm; Direct protein sequencing; Glycosyltransferase; KW Reference proteome; Stress response; Transferase. FT CHAIN 1..495 FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP- FT forming] 56 kDa subunit" FT /id="PRO_0000122502" FT BINDING 102 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 156 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 293 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 293 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 298 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 298 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 331 FT /ligand="D-glucose 6-phosphate" FT /ligand_id="ChEBI:CHEBI:61548" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 370 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 370 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 392..400 FT /ligand="UDP-alpha-D-glucose" FT /ligand_id="ChEBI:CHEBI:58885" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT BINDING 396..400 FT /ligand="UDP" FT /ligand_id="ChEBI:CHEBI:58223" FT /evidence="ECO:0000250|UniProtKB:Q92410" FT MUTAGEN 223 FT /note="H->Y: In GLC6-1; low glycogen accumulation." FT /evidence="ECO:0000269|PubMed:8150278" FT CONFLICT 75 FT /note="K -> M (in Ref. 2; CAA48296)" FT /evidence="ECO:0000305" FT CONFLICT 101 FT /note="H -> L (in Ref. 2; CAA48296)" FT /evidence="ECO:0000305" FT CONFLICT 104 FT /note="G -> W (in Ref. 2; CAA48296)" FT /evidence="ECO:0000305" FT CONFLICT 129..130 FT /note="LA -> FG (in Ref. 4; CAA43580)" FT /evidence="ECO:0000305" FT CONFLICT 217 FT /note="T -> S (in Ref. 2; CAA48296)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="I -> L (in Ref. 2; CAA48296)" FT /evidence="ECO:0000305" SQ SEQUENCE 495 AA; 56148 MW; 47325A0FA3554E3D CRC64; MTTDNAKAQL TSSSGGNIIV VSNRLPVTIT KNSSTGQYEY AMSSGGLVTA LEGLKKTYTF KWFGWPGLEI PDDEKDQVRK DLLEKFNAVP IFLSDEIADL HYNGFSNSIL WPLFHYHPGE INFDENAWLA YNEANQTFTN EIAKTMNHND LIWVHDYHLM LVPEMLRVKI HEKQLQNVKV GWFLHTPFPS SEIYRILPVR QEILKGVLSC DLVGFHTYDY ARHFLSSVQR VLNVNTLPNG VEYQGRFVNV GAFPIGIDVD KFTDGLKKES VQKRIQQLKE TFKGCKIIVG VDRLDYIKGV PQKLHAMEVF LNEHPEWRGK VVLVQVAVPS RGDVEEYQYL RSVVNELVGR INGQFGTVEF VPIHFMHKSI PFEELISLYA VSDVCLVSST RDGMNLVSYE YIACQEEKKG SLILSEFTGA AQSLNGAIIV NPWNTDDLSD AINEALTLPD VKKEVNWEKL YKYISKYTSA FWGENFVHEL YSTSSSSTSS SATKN //