BGALA_ASPNC
ID BGALA_ASPNC Reviewed; 1007 AA.
AC A2QAN3;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Beta-galactosidase A {ECO:0000305};
DE Short=An-beta-gal {ECO:0000303|PubMed:28391618};
DE EC=3.2.1.23 {ECO:0000269|PubMed:28391618};
DE AltName: Full=Lactase A;
DE Flags: Precursor;
GN Name=lacA; ORFNames=An01g12150;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF WILD-TYPE AND MUTANT GLN-298 IN
RP COMPLEXES WITH ALLOLACTOSE; 3-GALACTOSYL-GLUCOSE; 6-GALACTOSYL-GALACTOSE;
RP 4-GALACTOSYL-LACTOSE AND 6-GALACTOSYL-LACTOSE, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MISCELLANEOUS, REGIONS, ACTIVE
RP SITE, GLYCOSYLATION AT ASN-156; ASN-402; ASN-478; ASN-522; ASN-622;
RP ASN-739; ASN-760; ASN-777 AND ASN-914, DISULFIDE BONDS, AND MUTAGENESIS OF
RP GLU-298; TYR-304; TYR-355; ASN-357 AND TRP-806.
RX PubMed=28391618; DOI=10.1111/febs.14083;
RA Rico-Diaz A., Ramirez-Escudero M., Vizoso-Vazquez A., Cerdan M.E.,
RA Becerra M., Sanz-Aparicio J.;
RT "Structural features of Aspergillus niger beta-galactosidase define its
RT activity against glycoside linkages.";
RL FEBS J. 284:1815-1829(2017).
CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC gangliosides, glycoproteins, and glycosaminoglycans.
CC {ECO:0000269|PubMed:28391618}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000269|PubMed:28391618};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=92.5 mM for lactose {ECO:0000269|PubMed:28391618};
CC Note=kcat is 214.9 sec(-1). {ECO:0000269|PubMed:28391618};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- MISCELLANEOUS: Mutants of this enzyme have improved
CC transgalactosylation activity and can be used for galacto-
CC oligosaccharides (GOS) production in vitro.
CC {ECO:0000269|PubMed:28391618}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR EMBL; AM269982; CAK44114.1; -; Genomic_DNA.
DR RefSeq; XP_001389622.1; XM_001389585.2.
DR PDB; 5IFP; X-ray; 1.71 A; A=1-1007.
DR PDB; 5IFT; X-ray; 2.45 A; A=1-1007.
DR PDB; 5IHR; X-ray; 2.40 A; A=1-1007.
DR PDB; 5JUV; X-ray; 2.27 A; A=1-1007.
DR PDB; 5MGC; X-ray; 2.30 A; A=1-1007.
DR PDB; 5MGD; X-ray; 2.15 A; A=1-1007.
DR PDBsum; 5IFP; -.
DR PDBsum; 5IFT; -.
DR PDBsum; 5IHR; -.
DR PDBsum; 5JUV; -.
DR PDBsum; 5MGC; -.
DR PDBsum; 5MGD; -.
DR AlphaFoldDB; A2QAN3; -.
DR SMR; A2QAN3; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR iPTMnet; A2QAN3; -.
DR PaxDb; A2QAN3; -.
DR EnsemblFungi; CAK44114; CAK44114; An01g12150.
DR GeneID; 4977988; -.
DR KEGG; ang:ANI_1_1636014; -.
DR VEuPathDB; FungiDB:An01g12150; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR Proteomes; UP000006706; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IMP:AspGD.
DR GO; GO:0005990; P:lactose catabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.20.10; -; 1.
DR Gene3D; 2.60.390.10; -; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421; PTHR23421; 1.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF13364; BetaGal_dom4_5; 2.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF117100; SSF117100; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1007
FT /note="Beta-galactosidase A"
FT /evidence="ECO:0000255"
FT /id="PRO_5000219458"
FT ACT_SITE 200
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:28391618"
FT ACT_SITE 298
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:28391618"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28391618,
FT ECO:0007744|PDB:5JUV"
FT BINDING 140..142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28391618,
FT ECO:0007744|PDB:5JUV"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28391618,
FT ECO:0007744|PDB:5JUV"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:28391618,
FT ECO:0007744|PDB:5JUV"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT CARBOHYD 805
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:28391618, ECO:0007744|PDB:5IFP"
FT DISULFID 205..206
FT /evidence="ECO:0000269|PubMed:28391618,
FT ECO:0007744|PDB:5IFP"
FT DISULFID 266..315
FT /evidence="ECO:0000269|PubMed:28391618,
FT ECO:0007744|PDB:5IFP"
FT MUTAGEN 298
FT /note="E->Q: Loss of hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:28391618"
FT MUTAGEN 304
FT /note="Y->A: Nearly complete loss of hydrolytic activity
FT against lactose compared to wild-type due to decreased
FT substrate affinity."
FT /evidence="ECO:0000269|PubMed:28391618"
FT MUTAGEN 304
FT /note="Y->F: Over 33% increase of hydrolytic activity
FT against lactose compared to wild-type. No effect on
FT hydrolytic activity compared to wild-type; when associated
FT with H-355 and G-357. 58% reduction in hydrolytic activity
FT compared to wild-type; when associated with H-355, G-357
FT and F-806."
FT /evidence="ECO:0000269|PubMed:28391618"
FT MUTAGEN 355
FT /note="Y->H: No effect on hydrolytic activity compared to
FT wild-type; when associated with F-304 and G-357. 58%
FT reduction in hydrolytic activity compared to wild-type;
FT when associated with F-304, G-357 and F-806."
FT /evidence="ECO:0000269|PubMed:28391618"
FT MUTAGEN 357
FT /note="N->G: No effect on hydrolytic activity compared to
FT wild-type; when associated with F-304 and H-355. 58%
FT reduction in hydrolytic activity compared to wild-type;
FT when associated with F-304, H-355 and F-806."
FT /evidence="ECO:0000269|PubMed:28391618"
FT MUTAGEN 806
FT /note="W->F: 43% loss of hydrolytic activity against
FT lactose compared to wild-type. 58% reduction in hydrolytic
FT activity compared to wild-type; when associated with F-304,
FT H-355 and G-357."
FT /evidence="ECO:0000269|PubMed:28391618"
FT MUTAGEN 806
FT /note="W->S: 90% loss of hydrolytic activity against
FT lactose compared to wild-type."
FT /evidence="ECO:0000269|PubMed:28391618"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:5IFP"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 164..183
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 321..332
FT /evidence="ECO:0007829|PDB:5IFP"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:5MGD"
FT STRAND 426..434
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 482..497
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 523..528
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 539..547
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 560..566
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 590..594
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 602..611
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 614..623
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 625..631
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 656..660
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 718..721
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 728..735
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 742..748
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 755..759
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 762..767
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 774..781
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 790..797
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 818..824
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 833..839
FT /evidence="ECO:0007829|PDB:5IFP"
FT TURN 840..843
FT /evidence="ECO:0007829|PDB:5IFP"
FT TURN 848..850
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 852..854
FT /evidence="ECO:0007829|PDB:5IFP"
FT HELIX 859..862
FT /evidence="ECO:0007829|PDB:5IFP"
FT TURN 863..866
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:5IFP"
FT TURN 880..882
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 884..899
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 908..912
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 921..927
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 930..936
FT /evidence="ECO:0007829|PDB:5IFP"
FT TURN 937..939
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 944..947
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 955..966
FT /evidence="ECO:0007829|PDB:5IFP"
FT STRAND 977..981
FT /evidence="ECO:0007829|PDB:5IFP"
SQ SEQUENCE 1007 AA; 109712 MW; CD1E91854D7A8A0A CRC64;
MKLSSACAIA LLAAQAAGAS IKHRINGFTL TEHSDPAKRE LLQKYVTWDD KSLFINGERI
MIFSGEFHPF RLPVKELQLD IFQKVKALGF NCVSFYVDWA LVEGKPGEYR ADGIFDLEPF
FDAASEAGIY LLARPGPYIN AESSGGGFPG WLQRVNGTLR SSDKAYLDAT DNYVSHVAAT
IAKYQITNGG PIILYQPENE YTSGCCGVEF PDPVYMQYVE DQARNAGVVI PLINNDASAS
GNNAPGTGKG AVDIYGHDSY PLGFDCANPT VWPSGDLPTN FRTLHLEQSP TTPYAIVEFQ
GGSYDPWGGP GFAACSELLN NEFERVFYKN DFSFQIAIMN LYMIFGGTNW GNLGYPNGYT
SYDYGSAVTE SRNITREKYS ELKLLGNFAK VSPGYLTASP GNLTTSGYAD TTDLTVTPLL
GNSTGSFFVV RHSDYSSEES TSYKLRLPTS AGSVTIPQLG GTLTLNGRDS KIHVTDYNVS
GTNIIYSTAE VFTWKKFADG KVLVLYGGAG EHHELAISTK SNVTVIEGSE SGISSKQTSS
SVVVGWDVST TRRIIQVGDL KILLLDRNSA YNYWVPQLAT DGTSPGFSTP EKVASSIIVK
AGYLVRTAYL KGSGLYLTAD FNATTSVEVI GVPSTAKNLF INGDKTSHTV DKNGIWSATV
DYNAPDISLP SLKDLDWKYV DTLPEIQSSY DDSLWPAADL KQTKNTLRSL TTPTSLYSSD
YGFHTGYLLY RGHFTATGNE STFAIDTQGG SAFGSSVWLN GTYLGSWTGL YANSDYNATY
NLPQLQAGKT YVITVVIDNM GLEENWTVGE DLMKTPRGIL NFLLAGRPSS AISWKLTGNL
GGEDYEDKVR GPLNEGGLYA ERQGFHQPEP PSQNWKSSSP LEGLSEAGIG FYSASFDLDL
PKGWDVPLFL NIGNSTTPSP YRVQVYVNGY QYAKYISNIG PQTSFPVPEG ILNYRGTNWL
AVTLWALDSA GGKLESLELS YTTPVLTALG EVESVDQPKY KKRKGAY
