LPH_RABIT
ID LPH_RABIT Reviewed; 1926 AA.
AC P09849;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Lactase/phlorizin hydrolase {ECO:0000305|PubMed:1388157};
DE AltName: Full=Lactase/glycosylceramidase {ECO:0000305|PubMed:1388157};
DE Includes:
DE RecName: Full=Lactase {ECO:0000305|PubMed:1388157};
DE EC=3.2.1.108 {ECO:0000269|PubMed:1388157};
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:0000303|PubMed:1388157};
DE Flags: Precursor;
GN Name=LCT {ECO:0000250|UniProtKB:P09848};
GN Synonyms=LPH {ECO:0000303|PubMed:2460343};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 867-885, AND TISSUE
RP SPECIFICITY.
RC STRAIN=New Zealand white;
RX PubMed=2460343; DOI=10.1002/j.1460-2075.1988.tb03124.x;
RA Mantei N., Villa M., Enzler T., Wacker H., Boll W., James P., Hunziker W.,
RA Semenza G.;
RT "Complete primary structure of human and rabbit lactase-phlorizin
RT hydrolase: implications for biosynthesis, membrane anchoring and evolution
RT of the enzyme.";
RL EMBO J. 7:2705-2713(1988).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN,
RP TISSUE SPECIFICITY, REGION, AND ACTIVE SITES.
RX PubMed=1388157; DOI=10.1016/s0021-9258(19)37024-3;
RA Wacker H., Keller P., Falchetto R., Legler G., Semenza G.;
RT "Location of the two catalytic sites in intestinal lactase-phlorizin
RT hydrolase. Comparison with sucrase-isomaltase and with other glycosidases,
RT the membrane anchor of lactase-phlorizin hydrolase.";
RL J. Biol. Chem. 267:18744-18752(1992).
RN [3]
RP DOMAIN.
RX PubMed=9762914; DOI=10.1016/s0014-5793(98)01076-x;
RA Zecca L., Mesonero J.E., Stutz A., Poiree J.C., Giudicelli J., Cursio R.,
RA Gloor S.M., Semenza G.;
RT "Intestinal lactase-phlorizin hydrolase (LPH): the two catalytic sites; the
RT role of the pancreas in pro-LPH maturation.";
RL FEBS Lett. 435:225-228(1998).
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 (PubMed:1388157). 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:1388157). {ECO:0000269|PubMed:1388157}.
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:0000269|PubMed:1388157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10077;
CC Evidence={ECO:0000269|PubMed:1388157};
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:0000250|UniProtKB:P09848};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69648;
CC Evidence={ECO:0000250|UniProtKB:P09848};
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:0000250|UniProtKB:P09848};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69656;
CC Evidence={ECO:0000250|UniProtKB:P09848};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69660;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69664;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69668;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69672;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69676;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69680;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69684;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000250|UniProtKB:W5PLZ6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69688;
CC Evidence={ECO:0000250|UniProtKB:W5PLZ6};
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:0000269|PubMed:1388157}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:1388157}. Note=Brush border.
CC {ECO:0000269|PubMed:1388157}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in small intestine.
CC {ECO:0000269|PubMed:1388157, ECO:0000269|PubMed:2460343}.
CC -!- DOMAIN: The glycosyl hydrolase-1 3/region III carries the phlorizin
CC hydrolase/glycosylceramidase activities (By similarity). The initial
CC assignment of the activities to different regions was revised by the
CC authors using alternative approaches (PubMed:1388157, PubMed:9762914).
CC {ECO:0000250|UniProtKB:P09848, ECO:0000269|PubMed:1388157,
CC ECO:0000269|PubMed:9762914}.
CC -!- DOMAIN: The glycosyl hydrolase-1 4/region IV carries the lactase
CC activity (By similarity). The initial assignment of the activities to
CC different regions was revised by the authors using alternative
CC approaches (PubMed:1388157, PubMed:9762914).
CC {ECO:0000250|UniProtKB:P09848, ECO:0000269|PubMed:1388157,
CC ECO:0000269|PubMed:9762914}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09848}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X07995; CAA30802.1; -; mRNA.
DR PIR; S01169; S01169.
DR RefSeq; NP_001095159.1; NM_001101689.1.
DR AlphaFoldDB; P09849; -.
DR SMR; P09849; -.
DR STRING; 9986.ENSOCUP00000015999; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR iPTMnet; P09849; -.
DR PRIDE; P09849; -.
DR Ensembl; ENSOCUT00000031459; ENSOCUP00000015999; ENSOCUG00000027277.
DR GeneID; 100009256; -.
DR KEGG; ocu:100009256; -.
DR CTD; 100009256; -.
DR eggNOG; KOG0626; Eukaryota.
DR GeneTree; ENSGT00940000155324; -.
DR InParanoid; P09849; -.
DR OrthoDB; 408001at2759; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000027277; Expressed in embryo and 17 other tissues.
DR ExpressionAtlas; P09849; baseline.
DR GO; GO:0098591; C:external side of apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008422; F:beta-glucosidase activity; ISS:UniProtKB.
DR GO; GO:0080079; F:cellobiose glucosidase activity; IEA:RHEA.
DR GO; GO:0004336; F:galactosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0004348; F:glucosylceramidase activity; ISS:UniProtKB.
DR GO; GO:0017042; F:glycosylceramidase activity; IEA:UniProtKB-EC.
DR GO; GO:0000016; F:lactase activity; IDA:UniProtKB.
DR GO; GO:0140749; F:phlorizin hydrolase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; Direct protein sequencing; Glycoprotein; Glycosidase;
KW Hydrolase; Membrane; Multifunctional enzyme; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..866
FT /note="XBetaGly"
FT /evidence="ECO:0000305|PubMed:2460343"
FT /id="PRO_0000011769"
FT CHAIN 867..1926
FT /note="Lactase/phlorizin hydrolase"
FT /evidence="ECO:0000305|PubMed:2460343"
FT /id="PRO_0000011770"
FT TOPO_DOM 20..1882
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1883..1901
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1902..1926
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 44..286
FT /note="Glycosyl hydrolase-1 1; Region I"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:1388157"
FT REGION 360..853
FT /note="Glycosyl hydrolase-1 2; Region II"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:1388157"
FT REGION 900..1364
FT /note="Glycosyl hydrolase-1 3; Region III. Phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:1388157,
FT ECO:0000305|PubMed:9762914"
FT REGION 1218..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1371..1845
FT /note="Glycosyl hydrolase-1 4; Region IV. Lactase activity"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:1388157,
FT ECO:0000305|PubMed:9762914"
FT ACT_SITE 1063
FT /note="Proton donor; for phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000305|PubMed:1388157"
FT ACT_SITE 1271
FT /note="Nucleophile; for phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055,
FT ECO:0000269|PubMed:1388157"
FT ACT_SITE 1536
FT /note="Proton donor; for lactase activity"
FT /evidence="ECO:0000305|PubMed:1388157"
FT ACT_SITE 1747
FT /note="Nucleophile; for lactase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10055,
FT ECO:0000269|PubMed:1388157"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 987
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1033
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1926 AA; 217849 MW; 2A21A7370D0CFC7A CRC64;
MELFWSIVFT VLLSFSCRGS DWESDSNFIS AAGPLTTDLL LSLQYPQGNQ TSDFAAGGKD
LYVCSQPLPA FLPEYFSSLR ASEITHYKVF LSWAQLLPAG HSGDPDGNAV RCYRQLLEAL
RAAQLQPMVV LHHQHLPASS ALRSAVFADL FAEYATFAFH AFGDLVGVWL TFSDLEAAIR
ELPQPESRAS RLQLLTEAHR KAYEIYHQKY AAQGGKVSVV LQAEEISELL LESSTSALAK
DSIDFLSLDL SYECQSEMSL PEKLSKLQTI EPKVKVFIFT LRLQDCPSSR KSPASLLFSF
IEAINKDQVL TLGFDVNAFL NCSSTSKKSI SCFLTDSLAL QTDHERAARN SAPVSTYQRV
WEMFAHQPRA ERDAFLQDTF PQGFLWGVST GAFNVEGGWA EGGRGPSVWD QFGHLKAAQG
QATPEVASDS YYKWASDVAL LRGLRAQVYK FSISWSRIFP MGRGSSPSPQ GVAYYNKLID
SLLDSHIEPM ATLFHWDLPQ ALQDEGGWQN ESVVDAFVDY AAFCFSAFGN RVKLWVTFHE
PWVMSYAGYG TGQHAPGISD PGIASFQVAH LVLKAHARTW HHYNSHHRPQ QQGRVGIVLN
SDWAEPLSPE RPEDLAASER FLHFMLGWFA HPIFVDGDYP ATMKAQIQQR NEQCPSPVAQ
LPEFTDTEKQ LLKGSADFLG LSHYTSRLIS KAPEDSCIPS YDTIGGFSQH TDPAWPQTSS
PWIRVVPWGI RRLLQFVSLE YTKGKVPIYL AGNGMPIGES ENLLSDSLRV DYFNQYINEV
LKAIKEDSVD VRSYIARSLM DGFEGPAGYS QRFGLYHVNF NESSKPRTPR KSAFLLTSII
EKNGFLTKAV KQPLPPNSAH LPSKTRASAL PSEVPSKAKV VWEKFSNQTK FERDLFYHGT
FRDDFLWGVS SSAYQIEGAW DADGKGPSIW DNFTHTPGNG VTDNSTGDIA CDSYNQLDAD
LNVLRALKVK AYRFSLSWSR IFPTGTNSSI NSHGVDYYNR LIDGLLASDI FPMVTLFHWD
LPQALQDIGG WENPSLIDLF DSYADYCFQT FGDRVKFWIT FNEPTYYSWW SYGSGTFPPN
VNDPGWAPYR ISHALIKAHA RVYHTYDEKY RQSQNGVISL SLVAQWAEPK SPDVLRDVEA
ADRKMQFTLG WYAHPIFKTG DYPDAMKWKV GNRSELQHLA TSRLPSFTEE EKSYIRGTAD
VFCLNTYSSK IVQHKTPALN PPSYEDDQEL AEEEDTSWPT TAMNRAASFG MRRLLNWIKE
EYGDIPIYIT ENGVGLTNPR LEDIDRIFYY KTYINEALKA YRLDGVNLRG YFAWSLMDNF
EWLQGYTIKF GLYHVDFENV NRPRTARISA SYYTELITNN GMPLPSEDEF VYGQFPEGFV
WSTSTAAFQI EGAWRADGKG LGIWDTFTHT RLKIENDDIA DVACDSYHKI SEDVVALQNL
AVTHYRFSIS WSRILPDGTT NYINEAGLNY YVRLIDALLA ANIKPQVTMY HFDLPQALQD
VGGWENETIV QRFKEYADVL FQRLGDKVKF WITLNEPFVV AYHGYGTGLY APGIYFRPGT
APYIVGHNLI KAHAEAWHLY NDVYRASQGG VISITISSDW AEPRDPSNQE DVEAAKRYVQ
FMGGWFAHPI FKNGDYNEVM KTQIRERSLA AGLNESRLPE FTESEKRRIN GTYDFFGFNH
YTTVLAYNFN YPSIMSTVDA DRGVASIVDR SWPGSGSYWL KMTPFGFRRI LNWIKEEYNN
PPIYVTENGV SHRGDSYLND TTRIYYLRSY INEALKAVQQ DKVDLRGYTV WTLMDNFEWY
TGFSDKFGLH FVNYSDPSLP RIPRESAKFY ASIVRCNGFP DPAEGPHPCL LQPEDTDPTM
SPVSQEEVQF LGLSLGSTEA ETALYVLFSL MLLGVCGLAF LSYALCKSSK QRKKLSQQEL
SPVSSF
