LPH_RAT
ID LPH_RAT Reviewed; 1928 AA.
AC Q02401; Q63712; Q63719;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Lactase/phlorizin hydrolase {ECO:0000305|PubMed:4752949};
DE AltName: Full=Lactase/glycosylceramidase {ECO:0000305|PubMed:4752949};
DE Includes:
DE RecName: Full=Lactase {ECO:0000305|PubMed:4752949};
DE EC=3.2.1.108 {ECO:0000269|PubMed:4752949};
DE Includes:
DE RecName: Full=Glycosylceramidase {ECO:0000305|PubMed:4752949};
DE EC=3.2.1.62 {ECO:0000269|PubMed:4752949};
DE AltName: Full=Phlorizin hydrolase {ECO:0000305|PubMed:4752949};
DE Flags: Precursor;
GN Name=Lct {ECO:0000312|RGD:620823};
GN Synonyms=Lph {ECO:0000303|PubMed:1909681};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Intestine;
RX PubMed=1909681; DOI=10.1016/0378-1119(91)90286-k;
RA Duluc I., Boukamel R., Mantei N., Semenza G., Raul F., Freund J.-N.;
RT "Sequence of the precursor of intestinal lactase-phlorizin hydrolase from
RT fetal rat.";
RL Gene 103:275-276(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
RC STRAIN=Sprague-Dawley;
RX PubMed=1339333; DOI=10.3109/10425179209034006;
RA Boukamel R., Freund J.-N.;
RT "The rat LPH gene 5' region: comparative structure with the human gene.";
RL DNA Seq. 3:119-121(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1288-1370, AND TISSUE SPECIFICITY.
RX PubMed=1691182; DOI=10.1016/s0021-9258(19)39247-6;
RA Bueller H.A., Kothe M.J., Goldman D.A., Grubman S.A., Sasak W.V.,
RA Matsudaira P.T., Montgomery R.K., Grand R.J.;
RT "Coordinate expression of lactase-phlorizin hydrolase mRNA and enzyme
RT levels in rat intestine during development.";
RL J. Biol. Chem. 265:6978-6983(1990).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4752949; DOI=10.1016/s0021-9258(19)43209-2;
RA Leese H.J., Semenza G.;
RT "On the identity between the small intestinal enzymes phlorizin hydrolase
RT and glycosylceramidase.";
RL J. Biol. Chem. 248:8170-8173(1973).
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:4752949). 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:4752949). {ECO:0000269|PubMed:4752949}.
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:4752949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10077;
CC Evidence={ECO:0000305|PubMed:4752949};
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:0000269|PubMed:4752949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69640;
CC Evidence={ECO:0000305|PubMed:4752949};
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:0000269|PubMed:4752949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30680;
CC Evidence={ECO:0000305|PubMed:4752949};
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:0000269|PubMed:4752949};
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:0000269|PubMed:4752949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69700;
CC Evidence={ECO:0000305|PubMed:4752949};
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:0000269|PubMed:4752949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69704;
CC Evidence={ECO:0000305|PubMed:4752949};
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:0000269|PubMed:4752949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69708;
CC Evidence={ECO:0000305|PubMed:4752949};
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:0000269|PubMed:4752949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69712;
CC Evidence={ECO:0000305|PubMed:4752949};
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 -!- TISSUE SPECIFICITY: Intestine. {ECO:0000269|PubMed:1691182}.
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; X56748; CAA40070.1; -; Genomic_DNA.
DR EMBL; X56747; CAA40069.1; -; mRNA.
DR EMBL; L04635; AAA41539.1; -; Genomic_DNA.
DR PIR; JS0610; JS0610.
DR AlphaFoldDB; Q02401; -.
DR SMR; Q02401; -.
DR STRING; 10116.ENSRNOP00000004908; -.
DR BindingDB; Q02401; -.
DR ChEMBL; CHEMBL3389; -.
DR DrugCentral; Q02401; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR iPTMnet; Q02401; -.
DR PhosphoSitePlus; Q02401; -.
DR PaxDb; Q02401; -.
DR UCSC; RGD:620823; rat.
DR RGD; 620823; Lct.
DR eggNOG; KOG0626; Eukaryota.
DR InParanoid; Q02401; -.
DR PhylomeDB; Q02401; -.
DR BRENDA; 3.2.1.108; 5301.
DR BRENDA; 3.7.1.4; 5301.
DR Reactome; R-RNO-189085; Digestion of dietary carbohydrate.
DR PRO; PR:Q02401; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005903; C:brush border; IDA:RGD.
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; IDA:UniProtKB.
DR GO; GO:0080079; F:cellobiose glucosidase activity; IEA:RHEA.
DR GO; GO:0004336; F:galactosylceramidase activity; IDA:UniProtKB.
DR GO; GO:0015926; F:glucosidase activity; ISO:RGD.
DR GO; GO:0004348; F:glucosylceramidase activity; IDA: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; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IDA:RGD.
DR GO; GO:2000892; P:cellobiose catabolic process; IDA:UniProtKB.
DR GO; GO:0046477; P:glycosylceramide catabolic process; IDA:UniProtKB.
DR GO; GO:0005990; P:lactose catabolic process; IDA:UniProtKB.
DR GO; GO:1901733; P:quercetin catabolic process; ISS:UniProtKB.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0010040; P:response to iron(II) ion; IDA:RGD.
DR GO; GO:0010288; P:response to lead ion; IDA:RGD.
DR GO; GO:0010045; P:response to nickel cation; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0010033; P:response to organic substance; IDA:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0009744; P:response to sucrose; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
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; 5.
DR Pfam; PF00232; Glyco_hydro_1; 4.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 4.
DR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 2.
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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..867
FT /note="XBetaGly"
FT /evidence="ECO:0000250|UniProtKB:P09849"
FT /id="PRO_0000011771"
FT CHAIN 868..1928
FT /note="Lactase/phlorizin hydrolase"
FT /evidence="ECO:0000250|UniProtKB:P09849"
FT /id="PRO_0000011772"
FT TOPO_DOM 22..1883
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1884..1902
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1903..1928
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 46..289
FT /note="Glycosyl hydrolase-1 1; Region I"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT REGION 364..856
FT /note="Glycosyl hydrolase-1 2; Region II"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT REGION 904..1367
FT /note="Glycosyl hydrolase-1 3; Region III. Phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT REGION 1374..1847
FT /note="Glycosyl hydrolase-1 4; Region IV. Lactase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849, ECO:0000255"
FT ACT_SITE 1067
FT /note="Proton donor; for phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849"
FT ACT_SITE 1274
FT /note="Nucleophile; for phlorizin
FT hydrolase/Glycosylceramidase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849,
FT ECO:0000255|PROSITE-ProRule:PRU10055"
FT ACT_SITE 1539
FT /note="Proton donor; for lactase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849"
FT ACT_SITE 1750
FT /note="Nucleophile; for lactase activity"
FT /evidence="ECO:0000250|UniProtKB:P09849,
FT ECO:0000255|PROSITE-ProRule:PRU10055"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 824
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1037
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 1240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 7
FT /note="A -> R (in Ref. 1; AAA41539)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Q -> E (in Ref. 1; AAA41539)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> D (in Ref. 1; AAA41539)"
FT /evidence="ECO:0000305"
FT CONFLICT 1337
FT /note="Y -> H (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1357..1359
FT /note="PDL -> AEV (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 1369..1370
FT /note="RE -> GK (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1928 AA; 217268 MW; 56DDCAAC4ACAEA85 CRC64;
MELPWTALFL STVLLGLSCQ GSDWESDRNF ISAAGPLTND LVLNLNYPPG KQGSDVVSGN
TDHLLCQQPL PSFLSQYFSS LRASQVTHYK VLLSWAQLLP TGSSKNPDQE AVQCYRQLLQ
SLKDAQLEPM VVLCHQTPPT SSAIQREGAF ADLFADYATL AFQSFGDLVE IWFTFSDLEK
VIMDLPHKDL KASALQTLSN AHRRAFEIYH RKFSSQGGKL SVVLKAEDIP ELLPDPALAA
LVQGSVDFLS LDLSYECQSV ATLPQKLSEL QNLEPKVKVF IYTLKLEDCP ATGTSPSSLL
ISLLEAINKD QIQTVGFDVN AFLSCTSNSE ESPSCSLTDS LALQTEQQQE TAVPSSPGSA
YQRVWAAFAN QSREERDAFL QDVFPEGFLW GISTGAFNVE GGWAEGGRGP SIWDHYGNLN
AAEGQATAKV ASDSYHKPAS DVALLRGIRA QVYKFSISWS GLFPLGQKST PNRQGVAYYN
KLIDRLLDSH IEPMATLFHW DLPQALQEQG GWQNESVVEA FLDYAAFCFS TFGDRVKLWV
TFHEPWVMSY AGYGTGQHAP AISDPGMASF KVAHLILKAH ARTWHLYDLH HRLQQQGRVG
IVLNSDLAEP LDRKSPQDLA AAERFLHFML GWFAHPIFVD GDYPTTSAQI QHINQQCGHP
LAQLPEFTEA EKRLLKGSAD FLGLSHYTSR LISKAGRQTC TSSYDNIGGF SQHVDPEWPQ
TASPWIRVVP WGIRRLLRFA SMEYTKGKLP IFLAGNGMPV GEEADLFDDS VRVNYFNWYI
NEVLKAVKED LVDVRSYIVR SLIDGYEGPL GFSQRFGLYH VNFNDSSRPR TPRKSAYLFT
SIIEKNGFSA KKVKRNPLPV RADFTSRARV TDSLPSEVPS KAKISVEKFS KQPRFERDLF
YDGRFRDDFL WGVSSSPYQI EGGWNADGKG PSIWDNFTHT PGNGVKDNAT GDVACDSYHQ
LDADLNILRT LKVKSYRFSI SWSRIFPTGR NSTINKQGVD YYNRLIDSLV DNNIFPMVTL
FHWDLPQALQ DIGGWENPSL IELFDSYADY CFKTFGDRVK FWMTFNEPWC HVVLGYSSGI
FPPSVQEPGW LPYKVSHIVI KAHARVYHTY DEKYRSEQKG VISLSLNTHW AEPKDPGLQR
DVEAADRMLQ FTMGWFAHPI FKNGDYPDVM KWTVGNRSEL QHLASSRLPT FTEEEKNYVR
GTADVFCHNT YTSVFVQHST PRLNPPSYDD DMELKLIEMN SSTGVMHQDV PWGTRRLLNW
IKEEYGNIPI YITENGQGLE NPTLDDTERI FYHKTYINEA LKAYKLDGVD LRGYSAWTLM
DDFEWLLGYT MRFGLYYVDF NHVSRPRTAR ASARYYPDLI ANNGMPLARE DEFLYGEFPK
GFIWSAASAS YQVEGAWRAD GKGLSIWDTF SHTPLRIGND DNGDVACDSY HKIAEDVVAL
QNLGVSHYRF SIAWSRILPD GTTKFINEAG LSYYVRFIDA LLAAGITPQV TIYHWDLPQA
LQDVGGWENE TIVQRFKEYA DVLFQRLGDR VKFWITLNEP FVIAAQGYGT GVSAPGISFR
PGTAPYIAGH NLIKAHAEAW HLYNDVYRAR QGGTISITIS SDWGEPRDPT NREHVEAARS
YVQFMGGWFA HPIFKNGDYP EVMKTRIRDR SLGAGLNKSR LPEFTESEKS RIKGTFDFFG
FNHNTTVLAY NLDYPAAFSS FDADRGVASI ADSSWPVSGS FWLKVTPFGF RRILNWLKEE
YNNPPIYVTE NGVSRRGEPE LNDTDRIYYL RSYINEALKA VHDKVDLRGY TVWSIMDNFE
WATGFAERFG VHFVNRSDPS LPRIPRASAK FYATIVRCNG FPDPAQGPHP CLQQPEDAAP
TASPVQSEVP FLGLMLGIAE AQTALYVLFA LLLLGACSLA FLTYNTGRRS KQGNAQPSQH
QLSPISSF
