GGPPS_YEAST
ID GGPPS_YEAST Reviewed; 335 AA.
AC Q12051; D6W3U6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Geranylgeranyl pyrophosphate synthase BTS1 {ECO:0000303|PubMed:7665600};
DE Short=GGPP synthase;
DE Short=GGPPSase;
DE EC=2.5.1.-;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE AltName: Full=BET2 suppressor protein 1;
DE AltName: Full=Dimethylallyltranstransferase;
DE EC=2.5.1.1;
DE AltName: Full=Farnesyl diphosphate synthase;
DE AltName: Full=Farnesyltranstransferase;
DE EC=2.5.1.29;
DE AltName: Full=Geranylgeranyl diphosphate synthase;
DE AltName: Full=Geranyltranstransferase;
DE EC=2.5.1.10;
GN Name=BTS1; OrderedLocusNames=YPL069C;
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], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7665600; DOI=10.1074/jbc.270.37.21958;
RA Jiang Y., Proteau P., Poulter D., Ferro-Novick S.;
RT "BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 270:21793-21799(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=15296494; DOI=10.1111/j.1600-0854.2004.00213.x;
RA Shiflett S.L., Vaughn M.B., Huynh D., Kaplan J., McVey Ward D.;
RT "Bph1p, the Saccharomyces cerevisiae homologue of CHS1/beige, functions in
RT cell wall formation and protein sorting.";
RL Traffic 5:700-710(2004).
RN [7]
RP SUBUNIT, AND MUTAGENESIS OF GLU-7; LEU-8 AND ILE-9.
RX PubMed=19245203; DOI=10.1021/ja808699c;
RA Lo C.-H., Chang Y.-H., Wright J.D., Chen S.-H., Kan D., Lim C.,
RA Liang P.-H.;
RT "Combined experimental and theoretical study of long-range interactions
RT modulating dimerization and activity of yeast geranylgeranyl diphosphate
RT synthase.";
RL J. Am. Chem. Soc. 131:4051-4062(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP SUBUNIT.
RX PubMed=16554305; DOI=10.1074/jbc.m512886200;
RA Chang T.-H., Guo R.-T., Ko T.-P., Wang A.H.-J., Liang P.-H.;
RT "Crystal structure of type-III geranylgeranyl pyrophosphate synthase from
RT Saccharomyces cerevisiae and the mechanism of product chain length
RT determination.";
RL J. Biol. Chem. 281:14991-15000(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ISOPENTENYL
RP DIPHOSPHATE; FARNESYL DIPHOSPHATE AND MAGNESIUM, COFACTOR, AND SUBUNIT.
RX PubMed=17535895; DOI=10.1073/pnas.0702254104;
RA Guo R.-T., Cao R., Liang P.-H., Ko T.-P., Chang T.-H., Hudock M.P.,
RA Jeng W.-Y., Chen C.K.-M., Zhang Y., Song Y., Kuo C.-J., Yin F.,
RA Oldfield E., Wang A.H.-J.;
RT "Bisphosphonates target multiple sites in both cis- and trans-
RT prenyltransferases.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10022-10027(2007).
CC -!- FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto
CC DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane
CC attachment of YPT1 and SEC4. May be involved in vesicle trafficking and
CC protein sorting. {ECO:0000269|PubMed:15296494,
CC ECO:0000269|PubMed:7665600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-
CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:128769; EC=2.5.1.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate =
CC (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC Evidence={ECO:0000269|PubMed:7665600};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17535895};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:17535895};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 uM for farnesyl diphosphate;
CC KM=0.8 uM for isopentenyl diphosphate;
CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC diphosphate: step 1/1.
CC -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC isopentenyl diphosphate: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; U39205; AAB68296.1; -; Genomic_DNA.
DR EMBL; U31632; AAA83262.1; -; Genomic_DNA.
DR EMBL; AY692852; AAT92871.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11362.1; -; Genomic_DNA.
DR PIR; S60921; S60921.
DR RefSeq; NP_015256.1; NM_001183883.1.
DR PDB; 2DH4; X-ray; 1.98 A; A/B=1-335.
DR PDB; 2E8T; X-ray; 2.13 A; A/B=1-335.
DR PDB; 2E8U; X-ray; 2.08 A; A/B=1-335.
DR PDB; 2E8V; X-ray; 1.80 A; A/B=1-335.
DR PDB; 2E8W; X-ray; 2.35 A; A/B=1-335.
DR PDB; 2E8X; X-ray; 2.04 A; A/B=1-335.
DR PDB; 2E90; X-ray; 2.55 A; A/B=1-335.
DR PDB; 2E91; X-ray; 2.14 A; A/B=1-335.
DR PDB; 2E92; X-ray; 2.31 A; A/B=1-335.
DR PDB; 2E93; X-ray; 2.12 A; A/B=1-335.
DR PDB; 2E94; X-ray; 2.18 A; A/B=1-335.
DR PDB; 2E95; X-ray; 2.20 A; A/B=1-335.
DR PDB; 2Z4V; X-ray; 1.86 A; A/B=1-335.
DR PDB; 2Z4W; X-ray; 2.45 A; A/B=1-335.
DR PDB; 2Z4X; X-ray; 1.90 A; A/B=1-335.
DR PDB; 2Z4Y; X-ray; 2.10 A; A/B=1-335.
DR PDB; 2Z4Z; X-ray; 2.09 A; A/B=1-335.
DR PDB; 2Z50; X-ray; 2.01 A; A/B=1-335.
DR PDB; 2Z52; X-ray; 2.13 A; A/B=1-335.
DR PDB; 2Z78; X-ray; 2.10 A; A/B=1-335.
DR PDB; 2Z7H; X-ray; 2.08 A; A/B=1-335.
DR PDB; 2Z7I; X-ray; 2.10 A; A/B=1-335.
DR PDB; 2ZEU; X-ray; 2.00 A; A/B=1-335.
DR PDB; 2ZEV; X-ray; 2.23 A; A/B=1-335.
DR PDBsum; 2DH4; -.
DR PDBsum; 2E8T; -.
DR PDBsum; 2E8U; -.
DR PDBsum; 2E8V; -.
DR PDBsum; 2E8W; -.
DR PDBsum; 2E8X; -.
DR PDBsum; 2E90; -.
DR PDBsum; 2E91; -.
DR PDBsum; 2E92; -.
DR PDBsum; 2E93; -.
DR PDBsum; 2E94; -.
DR PDBsum; 2E95; -.
DR PDBsum; 2Z4V; -.
DR PDBsum; 2Z4W; -.
DR PDBsum; 2Z4X; -.
DR PDBsum; 2Z4Y; -.
DR PDBsum; 2Z4Z; -.
DR PDBsum; 2Z50; -.
DR PDBsum; 2Z52; -.
DR PDBsum; 2Z78; -.
DR PDBsum; 2Z7H; -.
DR PDBsum; 2Z7I; -.
DR PDBsum; 2ZEU; -.
DR PDBsum; 2ZEV; -.
DR AlphaFoldDB; Q12051; -.
DR SMR; Q12051; -.
DR BioGRID; 36110; 1026.
DR DIP; DIP-8889N; -.
DR IntAct; Q12051; 5.
DR STRING; 4932.YPL069C; -.
DR BindingDB; Q12051; -.
DR ChEMBL; CHEMBL1075251; -.
DR DrugCentral; Q12051; -.
DR MaxQB; Q12051; -.
DR PaxDb; Q12051; -.
DR PRIDE; Q12051; -.
DR EnsemblFungi; YPL069C_mRNA; YPL069C; YPL069C.
DR GeneID; 856036; -.
DR KEGG; sce:YPL069C; -.
DR SGD; S000005990; BTS1.
DR VEuPathDB; FungiDB:YPL069C; -.
DR eggNOG; KOG0777; Eukaryota.
DR GeneTree; ENSGT00940000153498; -.
DR HOGENOM; CLU_014015_6_0_1; -.
DR InParanoid; Q12051; -.
DR OMA; FYSKAFF; -.
DR BioCyc; MetaCyc:YPL069C-MON; -.
DR BioCyc; YEAST:YPL069C-MON; -.
DR BRENDA; 2.5.1.29; 984.
DR Reactome; R-SCE-191273; Cholesterol biosynthesis.
DR SABIO-RK; Q12051; -.
DR UniPathway; UPA00259; UER00368.
DR UniPathway; UPA00260; UER00369.
DR UniPathway; UPA00389; UER00564.
DR EvolutionaryTrace; Q12051; -.
DR PRO; PR:Q12051; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12051; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; IDA:SGD.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IDA:CACAO.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA:SGD.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carotenoid biosynthesis; Cytoplasm; Isoprene biosynthesis;
KW Magnesium; Metal-binding; Protein transport; Reference proteome;
KW Transferase; Transport.
FT CHAIN 1..335
FT /note="Geranylgeranyl pyrophosphate synthase BTS1"
FT /id="PRO_0000228139"
FT BINDING 36
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 39
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 68
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 79
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16554305,
FT ECO:0000269|PubMed:17535895"
FT BINDING 84
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 85
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 169
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 170
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 206
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 213
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT BINDING 223
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000305|PubMed:17535895"
FT BINDING 233
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000269|PubMed:17535895"
FT SITE 107
FT /note="Important for determining product chain length"
FT MUTAGEN 7
FT /note="E->G: No effect. Monomer; when associated with G-8."
FT /evidence="ECO:0000269|PubMed:19245203"
FT MUTAGEN 8
FT /note="L->G: Monomer and homodimer. Monomer; when
FT associated with G-7."
FT /evidence="ECO:0000269|PubMed:19245203"
FT MUTAGEN 9
FT /note="I->G: Mostly monomer. Exclusively monomer; when
FT associated with G-8. Reduces enzyme activity 1000-fold."
FT /evidence="ECO:0000269|PubMed:19245203"
FT MUTAGEN 107
FT /note="Y->A: Reduced affinity for isopentenyl diphosphate
FT (IPP)."
FT MUTAGEN 108
FT /note="F->A: Reduced affinity for isopentenyl diphosphate
FT (IPP)."
FT MUTAGEN 139
FT /note="H->A: Reduced affinity for isopentenyl diphosphate
FT (IPP)."
FT HELIX 1..9
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:2E8V"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2E8X"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 54..78
FT /evidence="ECO:0007829|PDB:2E8V"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 121..150
FT /evidence="ECO:0007829|PDB:2E8V"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2Z4V"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 171..184
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 195..215
FT /evidence="ECO:0007829|PDB:2E8V"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:2DH4"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 268..280
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 284..300
FT /evidence="ECO:0007829|PDB:2E8V"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:2Z4V"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:2Z4V"
SQ SEQUENCE 335 AA; 38651 MW; 4C7D6527FF29F157 CRC64;
MEAKIDELIN NDPVWSSQNE SLISKPYNHI LLKPGKNFRL NLIVQINRVM NLPKDQLAIV
SQIVELLHNS SLLIDDIEDN APLRRGQTTS HLIFGVPSTI NTANYMYFRA MQLVSQLTTK
EPLYHNLITI FNEELINLHR GQGLDIYWRD FLPEIIPTQE MYLNMVMNKT GGLFRLTLRL
MEALSPSSHH GHSLVPFINL LGIIYQIRDD YLNLKDFQMS SEKGFAEDIT EGKLSFPIVH
ALNFTKTKGQ TEQHNEILRI LLLRTSDKDI KLKLIQILEF DTNSLAYTKN FINQLVNMIK
NDNENKYLPD LASHSDTATN LHDELLYIID HLSEL
