PGM2_YEAST
ID PGM2_YEAST Reviewed; 569 AA.
AC P37012; D6VZS7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Phosphoglucomutase 2 {ECO:0000303|PubMed:5784209};
DE Short=PGM 2 {ECO:0000303|PubMed:5784209};
DE EC=5.4.2.2 {ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:23103740, ECO:0000269|PubMed:4992300};
DE AltName: Full=D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase {ECO:0000303|PubMed:14264884};
DE AltName: Full=Glucose phosphomutase 2;
GN Name=PGM2 {ECO:0000303|PubMed:5784209};
GN Synonyms=GA-5 {ECO:0000303|PubMed:13887540},
GN GAL5 {ECO:0000303|PubMed:2138705};
GN OrderedLocusNames=YMR105C {ECO:0000312|SGD:S000004711};
GN ORFNames=YM9718.04C;
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=8119301; DOI=10.1111/j.1432-1033.1994.tb18601.x;
RA Boles E., Liebetrau W., Hofmann M., Zimmermann F.K.;
RT "A family of hexosephosphate mutases in Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 220:83-96(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fu L., Bounelis P., Dey N., Browne B.L., Marchase R.B., Bedwell D.M.;
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 15-32 AND 265-275, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=8385141; DOI=10.1016/s0021-9258(18)53101-x;
RA Marchase R.B., Bounelis P., Brumley L.M., Dey N., Browne B., Auger D.,
RA Fritz T.A., Kulesza P., Bedwell D.M.;
RT "Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic
RT glycoprotein and the acceptor for a Glc-phosphotransferase.";
RL J. Biol. Chem. 268:8341-8349(1993).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=13887540; DOI=10.1016/0006-3002(61)90924-6;
RA Douglas H.C.;
RT "A mutation in Saccharomyces that affects phosphoglucomutase activity and
RT galactose utilization.";
RL Biochim. Biophys. Acta 52:209-211(1961).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=8050B;
RX PubMed=14264884; DOI=10.1016/0926-6569(64)90011-2;
RA Tsoi A., Douglas H.C.;
RT "The effect of mutation of two forms of phosphoglucomutase in
RT Saccharomyces.";
RL Biochim. Biophys. Acta 92:513-520(1964).
RN [9]
RP FUNCTION.
RX PubMed=5231755; DOI=10.1073/pnas.57.5.1482;
RA Joshi J.G., Hooper J., Kuwaki T., Sakurada T., Swanson J.R., Handler P.;
RT "Phosphoglucomutase. V. Multiple forms of phosphoglucomutase.";
RL Proc. Natl. Acad. Sci. U.S.A. 57:1482-1489(1967).
RN [10]
RP FUNCTION.
RX PubMed=5784209; DOI=10.1128/jb.98.2.532-535.1969;
RA Bevan P., Douglas H.C.;
RT "Genetic control of phosphoglucomutase variants in Saccharomyces
RT cerevisiae.";
RL J. Bacteriol. 98:532-535(1969).
RN [11]
RP CATALYTIC ACTIVITY.
RX PubMed=4992300; DOI=10.1093/oxfordjournals.jbchem.a129375;
RA Hirose M., Sugimoto E., Sasaki R., Chiaa H.;
RT "Crystallization and reaction mechanism of yeast phosphoglucomutase.";
RL J. Biochem. 68:449-457(1970).
RN [12]
RP COFACTOR.
RX PubMed=4628805; DOI=10.1016/0005-2744(72)90116-7;
RA Hirose M., Sugimoto E., Chiba H.;
RT "Studies on crystalline yeast phosphoglucomutase: the presence of intrinsic
RT zinc.";
RL Biochim. Biophys. Acta 289:137-146(1972).
RN [13]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=1100398; DOI=10.1111/j.1432-1033.1975.tb02282.x;
RA Daugherty J.P., Kraemer W.F., Joshi J.G.;
RT "Purification and properties of phosphoglucomutase from Fleischmann's
RT yeast.";
RL Eur. J. Biochem. 57:115-126(1975).
RN [14]
RP INDUCTION.
RX PubMed=2138705; DOI=10.1128/mcb.10.4.1415-1422.1990;
RA Oh D., Hopper J.E.;
RT "Transcription of a yeast phosphoglucomutase isozyme gene is galactose
RT inducible and glucose repressible.";
RL Mol. Cell. Biol. 10:1415-1422(1990).
RN [15]
RP GLYCOSYLATION.
RX PubMed=7929458; DOI=10.1016/s0021-9258(18)47136-0;
RA Dey N.B., Bounelis P., Fritz T.A., Bedwell D.M., Marchase R.B.;
RT "The glycosylation of phosphoglucomutase is modulated by carbon source and
RT heat shock in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:27143-27148(1994).
RN [16]
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 [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; THR-117 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [20]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23103740; DOI=10.1016/j.febslet.2012.09.042;
RA Walther T., Baylac A., Alkim C., Vax A., Cordier H., Francois J.M.;
RT "The PGM3 gene encodes the major phosphoribomutase in the yeast
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 586:4114-4118(2012).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Major phosphoglucomutase isozyme that catalyzes the
CC reversible interconversion of glucose 1-phosphate and glucose 6-
CC phosphate (PubMed:5784209). Constitutes about 80-90% of the
CC phosphoglucomutase activity in the cell (PubMed:14264884,
CC PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction
CC is an essential step in the energy metabolism of galactose since the
CC product of the galactose pathway enzymes in yeast is glucose 1-
CC phosphate. The reverse reaction is an essential step for biosynthesis
CC when carbon sources other than galactose are the energy source because
CC glucose 1-phosphate is the starting point for the synthesis of UDP-
CC glucose, which acts as a precursor for the synthesis of
CC oligosaccharides and trehalose (PubMed:14264884).
CC {ECO:0000269|PubMed:14264884, ECO:0000269|PubMed:5231755}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000269|PubMed:1100398,
CC ECO:0000269|PubMed:23103740, ECO:0000269|PubMed:4992300};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:4628805};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:4628805};
CC Note=Binds 1 magnesium ion per subunit. Can also use Zn(2+) as
CC cofactor. {ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:4628805};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.24 uM for alpha-D-glucose 1,6-diphosphate
CC {ECO:0000269|PubMed:1100398};
CC KM=23.4 uM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:1100398};
CC KM=26 uM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:23103740};
CC KM=530 uM for D-ribose 1-phosphate {ECO:0000269|PubMed:23103740};
CC Vmax=33.7 umol/min/mg enzyme for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:23103740};
CC Vmax=0.32 umol/min/mg enzyme for D-ribose 1-phosphate
CC {ECO:0000269|PubMed:23103740};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1100398}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8385141}.
CC -!- INDUCTION: Induced in response to galactose and severely repressed in
CC response to glucose. {ECO:0000269|PubMed:2138705}.
CC -!- PTM: O-glycosylated with mannose residues (By similarity). Substrate of
CC UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose
CC in a phosphodiester linkage to O-linked mannose (PubMed:8385141,
CC PubMed:7929458). {ECO:0000250|UniProtKB:P47244,
CC ECO:0000269|PubMed:7929458, ECO:0000269|PubMed:8385141}.
CC -!- DISRUPTION PHENOTYPE: Blocks galactose utilization, but does not impair
CC growth on glucose. {ECO:0000269|PubMed:14264884}.
CC -!- MISCELLANEOUS: Present with 3790 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; X74823; CAA52820.1; -; Genomic_DNA.
DR EMBL; U09499; AAA91282.1; -; Genomic_DNA.
DR EMBL; Z49702; CAA89741.1; -; Genomic_DNA.
DR EMBL; AY723853; AAU09770.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10001.1; -; Genomic_DNA.
DR PIR; S41200; S41200.
DR RefSeq; NP_013823.1; NM_001182605.1.
DR AlphaFoldDB; P37012; -.
DR SMR; P37012; -.
DR BioGRID; 35280; 126.
DR DIP; DIP-6499N; -.
DR IntAct; P37012; 28.
DR MINT; P37012; -.
DR STRING; 4932.YMR105C; -.
DR iPTMnet; P37012; -.
DR MaxQB; P37012; -.
DR PaxDb; P37012; -.
DR PRIDE; P37012; -.
DR EnsemblFungi; YMR105C_mRNA; YMR105C; YMR105C.
DR GeneID; 855131; -.
DR KEGG; sce:YMR105C; -.
DR SGD; S000004711; PGM2.
DR VEuPathDB; FungiDB:YMR105C; -.
DR eggNOG; KOG0625; Eukaryota.
DR GeneTree; ENSGT00940000173602; -.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; P37012; -.
DR OMA; DIYKIYA; -.
DR BioCyc; MetaCyc:YMR105C-MON; -.
DR BioCyc; YEAST:YMR105C-MON; -.
DR SABIO-RK; P37012; -.
DR PRO; PR:P37012; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P37012; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IMP:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:SGD.
DR GO; GO:0030003; P:cellular cation homeostasis; IMP:SGD.
DR GO; GO:0019388; P:galactose catabolic process; IMP:SGD.
DR GO; GO:0019255; P:glucose 1-phosphate metabolic process; IMP:SGD.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IGI:SGD.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005978; P:glycogen biosynthetic process; IGI:SGD.
DR GO; GO:0005992; P:trehalose biosynthetic process; IGI:SGD.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IGI:SGD.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573; PTHR22573; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Glucose metabolism; Glycoprotein; Isomerase; Magnesium; Metal-binding;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..569
FT /note="Phosphoglucomutase 2"
FT /id="PRO_0000147797"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 24
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 119
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 294
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 295
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 359
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 378
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 380
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 391
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 27
FT /note="T -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="D -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="S -> A (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 63089 MW; 45B78AFF8197645E CRC64;
MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE GSKGATLVVG
GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS HIMRTYEEKC TGGIILTASH
NPGGPENDMG IKYNLSNGGP APESVTNAIW EISKKLTSYK IIKDFPELDL GTIGKNKKYG
PLLVDIIDIT KDYVNFLKEI FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD
EFGLPADEVL QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG
YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH GLNCYEVPTG
WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW LNILAIYNKH HPENEASIKT
IQNEFWAKYG RTFFTRYDFE KVETEKANKI VDQLRAYVTK SGVVNSAFPA DESLKVTDCG
DFSYTDLDGS VSDHQGLYVK LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE
EYLKPIINSV IKFLNFKQVL GTEEPTVRT
