TPS1_YEAST
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 03-AUG-2022, entry version 207.
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; OrderedLocusNames=YBR126C;
GN 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};
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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; 499.
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; Q00764; -.
DR PRIDE; Q00764; -.
DR TopDownProteomics; Q00764; -.
DR EnsemblFungi; YBR126C_mRNA; YBR126C; YBR126C.
DR GeneID; 852423; -.
DR KEGG; sce:YBR126C; -.
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; YYGFSNR; -.
DR BioCyc; MetaCyc:YBR126C-MON; -.
DR BioCyc; YEAST:YBR126C-MON; -.
DR BRENDA; 2.4.1.15; 984.
DR SABIO-RK; Q00764; -.
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:0044262; P:cellular 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 InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 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
