ID   BGL42_ARATH             Reviewed;         490 AA.
AC   Q9FIW4; Q2V330;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Beta-glucosidase 42 {ECO:0000303|PubMed:15604686};
DE            Short=AtBGLU42 {ECO:0000303|PubMed:15604686};
DE            EC=3.2.1.21 {ECO:0000269|PubMed:34965581};
DE   Flags: Precursor;
GN   Name=BGLU42 {ECO:0000303|PubMed:15604686};
GN   OrderedLocusNames=At5g36890 {ECO:0000312|Araport:AT5G36890};
GN   ORFNames=MLF18.1 {ECO:0000312|EMBL:BAB11630.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA   Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA   Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT   "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT   family 1.";
RL   Plant Mol. Biol. 55:343-367(2004).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY PSEUDOMONAS FLUORESCENS, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=25138267; DOI=10.1111/nph.12980;
RA   Zamioudis C., Hanson J., Pieterse C.M.J.;
RT   "beta-Glucosidase BGLU42 is a MYB72-dependent key regulator of
RT   rhizobacteria-induced systemic resistance and modulates iron deficiency
RT   responses in Arabidopsis roots.";
RL   New Phytol. 204:368-379(2014).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, MUTAGENESIS OF ARG-342,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Columbia;
RX   PubMed=34965581; DOI=10.1093/bbb/zbab200;
RA   Horikoshi S., Saburi W., Yu J., Matsuura H., Cairns J.R.K., Yao M.,
RA   Mori H.;
RT   "Substrate specificity of glycoside hydrolase family 1 beta-glucosidase
RT   AtBGlu42 from Arabidopsis thaliana and its molecular mechanism.";
RL   Biosci. Biotechnol. Biochem. 86:231-245(2022).
CC   -!- FUNCTION: Glucosidase that hydrolyzes scopolin and various beta-
CC       glucosides, cellooligosaccharides (mainly cellotriose) and
CC       laminarioligosaccharides (PubMed:34965581). Can use p-nitrophenyl-beta-
CC       glucosides (pNP beta-Glc) and p-nitrophenyl-beta-D-fucosides (pNP beta-
CC       D-Fuc) as substrates, and, to a lower extent, beta-galactosides, beta-
CC       mannosides and beta-xylosides (PubMed:34965581). Involved in the
CC       secretion of root-derived phenolics upon iron ions (Fe) depletion
CC       (PubMed:25138267). Promotes disease resistance toward B.cinerea,
CC       H.arabidopsidis and P.syringae pv. tomato DC3000 (PubMed:25138267).
CC       Required during rhizobacteria-mediated (e.g. P.fluorescens WCS417r)
CC       broad-spectrum induced systemic resistance (ISR) against several
CC       pathogens (PubMed:25138267). {ECO:0000269|PubMed:25138267,
CC       ECO:0000269|PubMed:34965581}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000269|PubMed:34965581};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.142 mM for pNP beta-D-glucopyranoside
CC         {ECO:0000269|PubMed:34965581};
CC         KM=0.158 mM for pNP beta-D-fucopyranoside
CC         {ECO:0000269|PubMed:34965581};
CC         KM=9.93 mM for pNP beta-D-galactopyranoside
CC         {ECO:0000269|PubMed:34965581};
CC         KM=0.29 mM for pNP beta-D-mannopyranoside
CC         {ECO:0000269|PubMed:34965581};
CC         KM=1.62 mM for pNP beta-D-xylopyranoside
CC         {ECO:0000269|PubMed:34965581};
CC         KM=0.0978 mM for pNP beta-D-cellobioside
CC         {ECO:0000269|PubMed:34965581};
CC         KM=0.0827 mM for 4-methylumbelliferyl beta-D-glucopyranoside
CC         {ECO:0000269|PubMed:34965581};
CC         KM=0.0981 mM for scopolin {ECO:0000269|PubMed:34965581};
CC         KM=0.0657 mM for helicin {ECO:0000269|PubMed:34965581};
CC         KM=4.07 mM for cellobiose {ECO:0000269|PubMed:34965581};
CC         KM=0.126 mM for cellotriose {ECO:0000269|PubMed:34965581};
CC         KM=0.231 mM for cellotetraose {ECO:0000269|PubMed:34965581};
CC         KM=0.283 mM for cellopentaose {ECO:0000269|PubMed:34965581};
CC         KM=0.314 mM for cellohexaose {ECO:0000269|PubMed:34965581};
CC         KM=0.117 mM for laminaribiose {ECO:0000269|PubMed:34965581};
CC         KM=0.636 mM for laminaritriose {ECO:0000269|PubMed:34965581};
CC         KM=0.864 mM for sophorose {ECO:0000269|PubMed:34965581};
CC         KM=16.9 mM for gentiobiose {ECO:0000269|PubMed:34965581};
CC         Note=kcat is 10.2 sec(-1) with pNP beta-D-glucopyranoside as
CC         substrate (PubMed:34965581). kcat is 12.9 sec(-1) with pNP
CC         beta-D-fucopyranoside as substrate (PubMed:34965581). kcat is 13.6
CC         sec(-1) with pNP beta-D-galactopyranoside as substrate
CC         (PubMed:34965581). kcat is 0.233 sec(-1) with pNP
CC         beta-D-mannopyranoside as substrate (PubMed:34965581). kcat is 0.464
CC         sec(-1) with pNP beta-D-xylopyranoside as substrate
CC         (PubMed:34965581). kcat is 9.4 sec(-1) with pNP beta-D-cellobioside
CC         as substrate (PubMed:34965581). kcat is 8.03 sec(-1) with
CC         4-methylumbelliferyl beta-D-glucopyranoside as substrate
CC         (PubMed:34965581). kcat is 10.2 sec(-1) with scopolin as substrate
CC         (PubMed:34965581). kcat is 10.5 sec(-1) with helicin as substrate
CC         (PubMed:34965581). kcat is 6.42 sec(-1) with cellobiose as substrate
CC         (PubMed:34965581). kcat is 10.8 sec(-1) with cellotriose as substrate
CC         (PubMed:34965581). kcat is 10.3 sec(-1) with cellotetraose as
CC         substrate (PubMed:34965581). kcat is 10.2 sec(-1) with cellopentaose
CC         as substrate (PubMed:34965581). kcat is 9.67 sec(-1) with
CC         cellohexaose as substrate (PubMed:34965581). kcat is 11.1 sec(-1)
CC         with laminaribiose as substrate (PubMed:34965581). kcat is 10.7
CC         sec(-1) with laminaritriose as substrate (PubMed:34965581). kcat is
CC         11.9 sec(-1) with sophorose as substrate (PubMed:34965581). kcat is
CC         0.543 sec(-1) with gentiobiose as substrate (PubMed:34965581).
CC         {ECO:0000269|PubMed:34965581};
CC       pH dependence:
CC         Optimum pH is 6.8. {ECO:0000269|PubMed:34965581};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:34965581};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FIW4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FIW4-2; Sequence=VSP_038498, VSP_038499;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels predominantly in root
CC       epidermal cells. {ECO:0000269|PubMed:25138267}.
CC   -!- INDUCTION: Accumulates upon rhizobacteria-mediated (e.g. P.fluorescens
CC       WCS417r) induced systemic resistance (ISR) in root trichoblasts and, to
CC       a lesser extent, in cortical cells. {ECO:0000269|PubMed:25138267}.
CC   -!- DISRUPTION PHENOTYPE: Reduced secretion of root-derived phenolics upon
CC       iron ions (Fe) depletion, thus leading to their accumulation in the
CC       root interior. Impaired P.fluorescens WCS417r-mediated broad-spectrum
CC       induced systemic resistance (ISR) against several pathogens.
CC       {ECO:0000269|PubMed:25138267}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; AB016877; BAB11630.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94122.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94123.1; -; Genomic_DNA.
DR   EMBL; BT010611; AAQ89633.1; -; mRNA.
DR   EMBL; AK175760; BAD43523.1; -; mRNA.
DR   RefSeq; NP_001031975.1; NM_001036898.2. [Q9FIW4-2]
DR   RefSeq; NP_198505.2; NM_123047.4. [Q9FIW4-1]
DR   PDB; 7F3A; X-ray; 1.70 A; A=1-490.
DR   PDBsum; 7F3A; -.
DR   AlphaFoldDB; Q9FIW4; -.
DR   SMR; Q9FIW4; -.
DR   BioGRID; 18907; 1.
DR   STRING; 3702.Q9FIW4; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   GlyCosmos; Q9FIW4; 1 site, No reported glycans.
DR   PaxDb; 3702-AT5G36890-1; -.
DR   ProteomicsDB; 240623; -. [Q9FIW4-1]
DR   EnsemblPlants; AT5G36890.1; AT5G36890.1; AT5G36890. [Q9FIW4-1]
DR   EnsemblPlants; AT5G36890.2; AT5G36890.2; AT5G36890. [Q9FIW4-2]
DR   GeneID; 833656; -.
DR   Gramene; AT5G36890.1; AT5G36890.1; AT5G36890. [Q9FIW4-1]
DR   Gramene; AT5G36890.2; AT5G36890.2; AT5G36890. [Q9FIW4-2]
DR   KEGG; ath:AT5G36890; -.
DR   Araport; AT5G36890; -.
DR   TAIR; AT5G36890; BGLU42.
DR   eggNOG; KOG0626; Eukaryota.
DR   InParanoid; Q9FIW4; -.
DR   OMA; HGSNDFY; -.
DR   OrthoDB; 3373839at2759; -.
DR   PhylomeDB; Q9FIW4; -.
DR   BioCyc; ARA:AT5G36890-MONOMER; -.
DR   PRO; PR:Q9FIW4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIW4; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   GO; GO:0009866; P:induced systemic resistance, ethylene mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0031349; P:positive regulation of defense response; IMP:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR   GO; GO:1990641; P:response to iron ion starvation; IMP:UniProtKB.
DR   GO; GO:0019748; P:secondary metabolic process; IMP:UniProtKB.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR017736; Glyco_hydro_1_beta-glucosidase.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR03356; BGL; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   Genevisible; Q9FIW4; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Glycoprotein; Glycosidase; Hydrolase;
KW   Plant defense; Reference proteome; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..490
FT                   /note="Beta-glucosidase 42"
FT                   /id="PRO_0000390315"
FT   ACT_SITE        183
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   ACT_SITE        388
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         35
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         137
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         182..183
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8GU20"
FT   BINDING         317
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         388
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SPP9"
FT   BINDING         437
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         444..445
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q8L7J2"
FT   BINDING         453
FT                   /ligand="a beta-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22798"
FT                   /evidence="ECO:0000250|UniProtKB:Q1XH05"
FT   SITE            342
FT                   /note="Important for substrate chain length specificity"
FT                   /evidence="ECO:0000269|PubMed:34965581"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         487
FT                   /note="G -> E (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038498"
FT   VAR_SEQ         488..490
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_038499"
FT   MUTAGEN         342
FT                   /note="R->A,Y: Highest preference on cellotetraose and
FT                   cellopentaose with increased affinities at subsite (+)3."
FT                   /evidence="ECO:0000269|PubMed:34965581"
FT   HELIX           1..11
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          26..30
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           49..54
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   TURN            66..70
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           72..86
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           97..100
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          106..108
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           111..126
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           142..148
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           156..171
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   TURN            172..174
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          177..182
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           184..192
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   TURN            205..207
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           208..230
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           232..235
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          238..244
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          247..253
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           255..268
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           270..278
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           283..289
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           290..292
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           298..306
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          310..315
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          319..324
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           333..336
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          340..343
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          351..355
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           366..378
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          384..388
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           401..405
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           408..427
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          431..437
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           445..450
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          455..459
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   TURN            460..464
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   STRAND          465..468
FT                   /evidence="ECO:0007829|PDB:7F3A"
FT   HELIX           470..480
FT                   /evidence="ECO:0007829|PDB:7F3A"
SQ   SEQUENCE   490 AA;  56077 MW;  50DED68FBF06D538 CRC64;
     MAQKLNLLNL AVPPVTHRSN FPSTFTFGVA TSAYQIEGGW NEGKKGPSIW DKFTHIEGKI
     LDGSNGDVAV DHYHRYKEDV DLIGQLGFGA YRFSISWSRI FPDGLGTEVN EEGIAFYNDL
     INTLLEKGIQ PYVTLYHWDL PSHLQEAIGG WTNRKIVDYF GLYADACFAN FGDRVKHWIT
     LNEPLQTSVN GHCIGIFAPG RNEKPLIEPY LVSHHQVLAH ATAVSIYRSK YKESQGGQIG
     LSVDCEWAEP NSEKPEDKVA ADRRIDFQLG WFLDPLFFGD YPASMRQKLG DNLPRFTPEE
     KEFMLQNSWD FLGLNHYTSR LISHVSNKEA ESNFYQAQEL ERIVELENGD LIGERAASDW
     LYAVPWGIRK TLNYMSKKYN HPPIFITENG MDDEDDGSAS IHDMLDDKRR VDYFKSYLAN
     VSQAIEDGVD IKGYFAWSLL DNFEWAQGYT KRFGLVYVDY KNGLTRHPKS SAYWFMKFLK
     GDEENKGKKE
//