LPH_SHEEP
ID LPH_SHEEP Reviewed; 1931 AA.
AC W5PLZ6;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Lactase/phlorizin hydrolase {ECO:0000303|PubMed:12594539};
DE AltName: Full=Lactase/glycosylceramidase;
DE Includes:
DE RecName: Full=Lactase {ECO:0000250|UniProtKB:P09848};
DE EC=3.2.1.108 {ECO:0000250|UniProtKB:P09848};
DE Includes:
DE RecName: Full=Glycosylceramidase {ECO:0000250|UniProtKB:Q02401};
DE EC=3.2.1.62 {ECO:0000250|UniProtKB:Q02401};
DE AltName: Full=Phlorizin hydrolase {ECO:0000250|UniProtKB:P09848};
DE Flags: Precursor;
GN Name=LCT {ECO:0000250|UniProtKB:P09848};
GN Synonyms=LPH {ECO:0000303|PubMed:12594539};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12594539; DOI=10.1007/s00394-003-0397-3;
RA Nemeth K., Plumb G.W., Berrin J.-G., Juge N., Jacob R., Naim H.Y.,
RA Williamson G., Swallow D.M., Kroon P.A.;
RT "Deglycosylation by small intestinal epithelial cell beta-glucosidases is a
RT critical step in the absorption and metabolism of dietary flavonoid
RT glycosides in humans.";
RL Eur. J. Nutr. 42:29-42(2003).
CC -!- FUNCTION: Broad specificity glycosidase of the intestinal brush border
CC membrane that hydrolyzes lactose, the main sugar in mammalian milk, to
CC produce D-glucose and D-galactose (By similarity). The mature protein
CC is composed of two domains that catalyze the hydrolysis of beta-
CC glucopyranosides and beta-galactopyranosides, with a preference for
CC hydrophilic aglycones (in lactose and cellobiose) for one domain and
CC hydrophobic aglycones (in phlorizin and glycosylceramides) for the
CC other (PubMed:12594539). {ECO:0000250|UniProtKB:P09848,
CC ECO:0000269|PubMed:12594539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + lactose = beta-D-galactose + D-glucose;
CC Xref=Rhea:RHEA:10076, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17716, ChEBI:CHEBI:27667; EC=3.2.1.108;
CC Evidence={ECO:0000250|UniProtKB:P09848};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10077;
CC Evidence={ECO:0000250|UniProtKB:P09848};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + phlorizin = beta-D-glucose + phloretin;
CC Xref=Rhea:RHEA:69639, ChEBI:CHEBI:8113, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17276;
CC Evidence={ECO:0000250|UniProtKB:P09848};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69640;
CC Evidence={ECO:0000250|UniProtKB:P09848};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-cellobiose + H2O = beta-D-glucose + D-glucose;
CC Xref=Rhea:RHEA:30679, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17057;
CC Evidence={ECO:0000250|UniProtKB:P09848};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30680;
CC Evidence={ECO:0000250|UniProtKB:P09848};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + quercetin 4'-O-beta-D-glucoside = beta-D-glucose +
CC quercetin; Xref=Rhea:RHEA:69647, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:57694, ChEBI:CHEBI:187902;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69648;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + quercetin 3-O-beta-D-glucoside = beta-D-glucose +
CC quercetin; Xref=Rhea:RHEA:69655, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:57694, ChEBI:CHEBI:144437;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69656;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + kaempferol 3-O-beta-D-glucoside = beta-D-glucose +
CC kaempferol; Xref=Rhea:RHEA:69659, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:58573, ChEBI:CHEBI:169942;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69660;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + luteolin 7-O-beta-D-glucoside = beta-D-glucose +
CC luteolin; Xref=Rhea:RHEA:69663, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:57545, ChEBI:CHEBI:77791;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69664;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + luteolin 4'-O-beta-D-glucoside = beta-D-glucose +
CC luteolin; Xref=Rhea:RHEA:69667, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:57545, ChEBI:CHEBI:187903;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69668;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-naringenin 7-O-beta-D-glucoside + H2O = (2S)-naringenin +
CC beta-D-glucose; Xref=Rhea:RHEA:69671, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17846, ChEBI:CHEBI:28327;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69672;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eriodictyol-7-O-beta-D-glucoside + H2O = (S)-eriodictyol +
CC beta-D-glucose; Xref=Rhea:RHEA:69675, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:28412, ChEBI:CHEBI:139458;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69676;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apigenin 7-O-beta-D-glucoside + H2O = apigenin + beta-D-
CC glucose; Xref=Rhea:RHEA:69679, ChEBI:CHEBI:15377, ChEBI:CHEBI:15903,
CC ChEBI:CHEBI:58470, ChEBI:CHEBI:77722;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69680;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=daidzein 7-O-beta-D-glucoside + H2O = beta-D-glucose +
CC daidzein + H(+); Xref=Rhea:RHEA:69683, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15903, ChEBI:CHEBI:42202,
CC ChEBI:CHEBI:77764; Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69684;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=genistein 7-O-beta-D-glucoside + H2O = beta-D-glucose +
CC genistein; Xref=Rhea:RHEA:69687, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:74224, ChEBI:CHEBI:140305;
CC Evidence={ECO:0000269|PubMed:12594539};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69688;
CC Evidence={ECO:0000305|PubMed:12594539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycosyl-N-acylsphingosine + H2O = N-acylsphingosine + a
CC sugar.; EC=3.2.1.62; Evidence={ECO:0000250|UniProtKB:Q02401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1')-N-hexadecanoylsphing-4-enine + H2O =
CC beta-D-glucose + N-hexadecanoylsphing-4-enine; Xref=Rhea:RHEA:69699,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:72959,
CC ChEBI:CHEBI:84716; Evidence={ECO:0000250|UniProtKB:Q02401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69700;
CC Evidence={ECO:0000250|UniProtKB:Q02401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1')-N-hexadecanoylsphingosine + H2O =
CC beta-D-galactose + N-hexadecanoylsphing-4-enine;
CC Xref=Rhea:RHEA:69703, ChEBI:CHEBI:15377, ChEBI:CHEBI:27667,
CC ChEBI:CHEBI:72959, ChEBI:CHEBI:83259;
CC Evidence={ECO:0000250|UniProtKB:Q02401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69704;
CC Evidence={ECO:0000250|UniProtKB:Q02401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galactosyl-(1<->1')-N-hexadecanoylsphinganine + H2O =
CC beta-D-galactose + N-hexadecanoylsphinganine; Xref=Rhea:RHEA:69707,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:27667, ChEBI:CHEBI:67042,
CC ChEBI:CHEBI:84783; Evidence={ECO:0000250|UniProtKB:Q02401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69708;
CC Evidence={ECO:0000250|UniProtKB:Q02401};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosyl-(1<->1')-N-hexadecanoylsphinganine + H2O =
CC beta-D-glucose + N-hexadecanoylsphinganine; Xref=Rhea:RHEA:69711,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15903, ChEBI:CHEBI:67042,
CC ChEBI:CHEBI:84782; Evidence={ECO:0000250|UniProtKB:Q02401};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69712;
CC Evidence={ECO:0000250|UniProtKB:Q02401};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P09848}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P09848}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P09848}. Note=Brush border.
CC {ECO:0000250|UniProtKB:P09849}.
CC -!- DOMAIN: The glycosyl hydrolase-1 3/region III carries the phlorizin
CC hydrolase/glycosylceramidase activities.
CC {ECO:0000250|UniProtKB:P09848}.
CC -!- DOMAIN: The glycosyl hydrolase-1 4/region IV carries the lactase
CC activity. {ECO:0000250|UniProtKB:P09848}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09848}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR EMBL; AMGL01054137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01054138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; W5PLZ6; -.
DR STRING; 9940.ENSOARP00000011470; -.
DR PRIDE; W5PLZ6; -.
DR Ensembl; ENSOART00000011631; ENSOARP00000011470; ENSOARG00000010689.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_5_3_1; -.
DR OMA; RIYYLRT; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000010689; Expressed in duodenum and 6 other tissues.
DR GO; GO:0098591; C:external side of apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0004336; F:galactosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0004348; F:glucosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0000016; F:lactase activity; ISS:UniProtKB.
DR GO; GO:0140749; F:phlorizin hydrolase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:2000892; P:cellobiose catabolic process; ISS:UniProtKB.
DR GO; GO:0046477; P:glycosylceramide catabolic process; ISS:UniProtKB.
DR GO; GO:0005990; P:lactose catabolic process; ISS:UniProtKB.
DR GO; GO:1901733; P:quercetin catabolic process; ISS:UniProtKB.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR018120; Glyco_hydro_1_AS.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 3.
DR Pfam; PF00232; Glyco_hydro_1; 4.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 4.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 2.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Multifunctional enzyme; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1931
FT /note="Lactase/phlorizin hydrolase"
FT /evidence="ECO:0000255"
FT /id="PRO_5004869293"
FT PROPEP 20..871
FT /note="XBetaGly"
FT /evidence="ECO:0000250|UniProtKB:P09849"
FT /id="PRO_0000455295"
FT CHAIN 872..1931
FT /note="Lactase/phlorizin hydrolase"
FT /evidence="ECO:0000250|UniProtKB:P09849"
FT /id="PRO_0000455296"
FT TOPO_DOM 20..1886
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1887..1907
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1908..1931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 44..286
FT /note="Glycosyl hydrolase-1 1; Region I"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT REGION 364..858
FT /note="Glycosyl hydrolase-1 2; Region II"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT REGION 905..1368
FT /note="Glycosyl hydrolase-1 3; Region III. Phlorizin
FT hydrolase/glycosylceramidase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT REGION 1375..1848
FT /note="Glycosyl hydrolase-1 4; Region IV. Lactase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT REGION 1649..1931
FT /note="Required for homodimerization and transport to the
FT plasma membrane"
FT /evidence="ECO:0000250|UniProtKB:P09848"
FT ACT_SITE 1068
FT /note="Proton donor; for phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000250|UniProtKB:P09848"
FT ACT_SITE 1275
FT /note="Nucleophile; for phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000250|UniProtKB:P09848,
FT ECO:0000255|PROSITE-ProRule:PRU10055"
FT ACT_SITE 1540
FT /note="Proton donor; for lactase activity"
FT /evidence="ECO:0000250|UniProtKB:P09848"
FT ACT_SITE 1751
FT /note="Nucleophile; for lactase activity"
FT /evidence="ECO:0000250|UniProtKB:P09848,
FT ECO:0000255|PROSITE-ProRule:PRU10055"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1038
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1931 AA; 219154 MW; CE514190F51AA6FC CRC64;
MELAWHLVLI VLLSFSCWGL DWDSDKNFIS AAGPLTNNLL HNLRDPLGNQ DPPFVAEDEE
IYVCRQPLPA FLPEYFRSVR ASMITHYKVF LPWAQLLPEG ISENPDKGTV LCYRQLLEAL
KTAQLQPLVV LHHQTLPAST LQRTEAFADL FAAYASFAFR SFGDLVEIWF TFSDLERVIT
KLPHQESRSS RLQILTDAHR KAYEIYQEKY AAQGGKLSVV LQAEMVSKLL LEPSTSVLVK
DAVDFVSLDL SYECHNEADL PQKLSELQTI EPKVKVFIFS LKLQNCLSTG NDIAQLLFGL
LKAINEDQVL VVGFDISTFL SCPSSSKKSW ACSLSDSLTL QTALQLGPDT AAYAWPPCSA
YQRVWEAFAN QSKAERDAFL QDVFPEGFLW GVSTGAFNVE GGWAEDGRGP SIWDRVGHQN
TIKGQATPEV ASDSYHKVDT DVALLRGLQA QVYKFSISWS RIFPTGQGHN PNPRGVAYYN
KLIDSLLDSH IEPMATLFHW DLPQALQDRG GWQSEDVVDA FLDYAAFCFS TFGDRVKLWV
TFHEPWVMSY AGYGTGQHAP GISDPGVASF KKVAHMVLKA HAKAWHLYNS HHRPQQQGRV
GIVLNSDWAE PLSPERPEDL RAAERFLHFM LGWFAHPIFV DGDYPAALRA QIQQMNKQCP
SPVAQLPEFT EAEKQLLKGS ADFLGLSHYT SRLVSTAQGD TCIPSYDTIG GFSQHIDPMW
PQTASSWIRV VPWGIRRLLK FVSLEYTKGK VPIYLAGNGM PIGESEDLID DSLRVDYFNQ
YINEVLKAIK EDSVAVQSYV ARSFIDGFEG PSGYSQRFGL YHVNFNDSSR PRTARKSAYF
FTSMIEKNGF LNKVVKRQSS PGIANIPRKI RAFTFPSEVP SKAKVVWEKF SNQPKFERDL
FYHGTFRDDF LWGVSSSAYQ IEGAWDADGK GPSIWDNFTH TPGSNVKDNA TGDVACDSYN
HLDADLNMLQ ALKVKAYRFS ISWSRIFPTG RNTSVNTHGV DYYNKLINGL VENNISPMVT
LFHWDLPQAL QDIGGWENPS LIDLFNSYAD FCFQTFGDRV KFWMTFNEPT YQAWLGYGSG
EFPPNVNDPG WGPYRIGHTI IKAHARVYHT YDEKYRQEQK GVISLSLSSH WAEPQSLVPR
DVEAADRMLQ FSLGWFAHPI FRNGDYPDAM KWKVGNRSEL QHLATSRLPS FTEEEKRYIA
ATADVFCLNT YSSRIVQHTT PRLNPPSYTS DQELLEWEDT SWPATAMNRA AAWGTRRLLN
WIKEEYGDIP VYITENGVGL TDPELEDTDR IFYHKTYINE ALKAYRLDGV NLRGYAAWSL
MDNFEWLNGY TVKFGLYHVD FNDVNRSRTA RASARYYTEV ITNNGMPLSK EDEFLYGQFP
KDFIWSAATA AYQIEGAWRA DGKGLSIWDT FSHTPLKVEN NDTGDVACDS YHKIAEDLVA
LQTLGVTHYR LSISWTRILP DGTNKYVNEA GLNYYVRLID TLLAANIQPQ VTIYHWDLPQ
ALQDVGGWEN ETIVQRFKEY AEVLFQRLGD KVKFWITLNE PYVVANQGYG YGTAAPGISF
RPGTAPYIVG HNLIKAHAEV WHLYNDVYRA RQGGIISITI SSDWAEPRDP SNQEDVEAAR
RYVQFMGGWF AHPIFKNGDY PEVMKTRIRD RSLAEGLNKS RLPEFTESEK RRINGTYDFF
GFNHYTTVLA YNLNYASWIS SFDADRGVAS ITDRSWPDSG SFWLKMTPFG FRRILNWLKE
EYNNPPIYVT ENGVSHRGEA NLNDTSRIYY LRSYINEALK ALQDKVDLRG YTVWTLMDNF
EWATGFSDKF GLHFVNYTDP ALPRIPRESA KVYASIIRCR GFPDPAAGPH ACLQQEDAEP
TASPASPVSQ KIQFLGLRLS TTEAQTALNV LFAFMLLGVC GVAFLSYKYF KHSKQKHTQP
GEHELSHRSS F
