ENPP3_MOUSE
ID ENPP3_MOUSE Reviewed; 874 AA.
AC Q6DYE8; E9QMU8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 3;
DE Short=E-NPP 3;
DE AltName: Full=Phosphodiesterase I beta;
DE Short=PD-Ibeta;
DE AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 3;
DE AltName: CD_antigen=CD203c;
DE Includes:
DE RecName: Full=Alkaline phosphodiesterase I;
DE EC=3.1.4.1 {ECO:0000250|UniProtKB:P06802};
DE Includes:
DE RecName: Full=Nucleotide pyrophosphatase;
DE Short=NPPase;
DE EC=3.6.1.9 {ECO:0000305|PubMed:25692702, ECO:0000305|PubMed:28225814};
DE AltName: Full=Nucleotide diphosphatase {ECO:0000305};
GN Name=Enpp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lynch K.R., Lee S.;
RT "Characterization of mouse ENPP3 (gp130RB13-6) as a lysophospholipase D.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-594.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY ACTIVATION OF FC EPSILON
RP RECEPTOR, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=25692702; DOI=10.1016/j.immuni.2015.01.015;
RA Tsai S.H., Kinoshita M., Kusu T., Kayama H., Okumura R., Ikeda K.,
RA Shimada Y., Takeda A., Yoshikawa S., Obata-Ninomiya K., Kurashima Y.,
RA Sato S., Umemoto E., Kiyono H., Karasuyama H., Takeda K.;
RT "The ectoenzyme E-NPP3 negatively regulates ATP-dependent chronic allergic
RT responses by basophils and mast cells.";
RL Immunity 42:279-293(2015).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=28225814; DOI=10.1371/journal.pone.0172509;
RA Furuta Y., Tsai S.H., Kinoshita M., Fujimoto K., Okumura R., Umemoto E.,
RA Kurashima Y., Kiyono H., Kayama H., Takeda K.;
RT "E-NPP3 controls plasmacytoid dendritic cell numbers in the small
RT intestine.";
RL PLoS ONE 12:E0172509-E0172509(2017).
CC -!- FUNCTION: Hydrolase that metabolizes extracellular nucleotides,
CC including ATP, GTP, UTP and CTP (By similarity). Limits mast cell and
CC basophil responses during inflammation and during the chronic phases of
CC allergic responses by eliminating the extracellular ATP that functions
CC as signaling molecule and activates basophils and mast cells and
CC induces the release of inflammatory cytokines (PubMed:25692702).
CC Metabolizes extracellular ATP in the lumen of the small intestine, and
CC thereby prevents ATP-induced apoptosis of intestinal plasmacytoid
CC dendritic cells (PubMed:28225814). Has also alkaline phosphodiesterase
CC activity (By similarity). {ECO:0000250|UniProtKB:O14638,
CC ECO:0000269|PubMed:25692702, ECO:0000269|PubMed:28225814}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000250|UniProtKB:O14638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC phosphate + diphosphate + H(+); Xref=Rhea:RHEA:23996,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.9;
CC Evidence={ECO:0000305|PubMed:25692702, ECO:0000305|PubMed:28225814};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-
CC deoxyribonucleoside 5'-phosphate + diphosphate + H(+);
CC Xref=Rhea:RHEA:44644, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:65317; EC=3.6.1.9;
CC Evidence={ECO:0000305|PubMed:25692702, ECO:0000305|PubMed:28225814};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O14638};
CC Note=Binds 2 zinc ions per subunit. {ECO:0000250|UniProtKB:O14638};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:O14638}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25692702};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}.
CC Apical cell membrane {ECO:0000250|UniProtKB:O14638}; Single-pass type
CC II membrane protein {ECO:0000250|UniProtKB:O14638}. Secreted
CC {ECO:0000250|UniProtKB:O14638}. Note=Detected at the cell surface of
CC basophils (PubMed:25692702). Detected at the apical plasma membrane of
CC bile duct cells. Located to the apical surface in intestinal and kidney
CC epithelial cells. Secreted in serum, and in lumen of epithelial cells
CC (By similarity). {ECO:0000250|UniProtKB:O14638,
CC ECO:0000269|PubMed:25692702}.
CC -!- TISSUE SPECIFICITY: Detected at the tip of villi in the small intestine
CC (PubMed:28225814). Detected on basophils and mast cells (at protein
CC level) (PubMed:25692702). Detected in the epithelial layer of the small
CC intestine; expression is higher in the proximal part and lower in the
CC distal part of the small intestine (PubMed:28225814).
CC {ECO:0000269|PubMed:25692702, ECO:0000269|PubMed:28225814}.
CC -!- INDUCTION: In bone marrow-derived mast cells and basophils, induced by
CC activation of the high affinity immunoglobulin epsilon receptor 1 (Fc
CC epsilon RI). {ECO:0000269|PubMed:25692702}.
CC -!- PTM: N-glycosylated. N-glycosylation is necessary for normal transport
CC to the cell membrane, but is not the apical targeting signal.
CC {ECO:0000250|UniProtKB:P97675}.
CC -!- DISRUPTION PHENOTYPE: Mice appear healthy, and have normal numbers of
CC peripheral lymphocytes, eosinophils and neutrophils. Basophil numbers
CC are normal in bone marrow, but are markedly increased in peripheral
CC blood and spleen. Likewise, mutant mice have an increased number of
CC mast cells in the small and large intestine. Both mast cells and
CC basophils show increased proliferation in response to extracellular
CC ATP. Mutant mice display normal immediate reaction to allergens, but
CC strongly increased chronic allergic inflammation in skin, intestine and
CC lung that lead to severe tissue damage. Extracellular ATP levels are
CC normal in the absence of allergen, and strongly increased after
CC exposure to allergen, due to impaired clearance of extracellular ATP
CC (PubMed:25692702). Mutant mice display increased levels of
CC extracellular ATP in the lumen of the small intestine. They have
CC decreased numbers of plasmacytoid dendritic cells in the small
CC intestine lamia propria and in Peyer patches; the decrease is due to
CC increased ATP levels that cause increased apoptosis of plasmacytoid
CC dendritic cells (PubMed:28225814). {ECO:0000269|PubMed:25692702,
CC ECO:0000269|PubMed:28225814}.
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DR EMBL; AY630402; AAT64421.1; -; mRNA.
DR EMBL; AC158616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23752.1; -.
DR RefSeq; NP_598766.2; NM_134005.2.
DR AlphaFoldDB; Q6DYE8; -.
DR SMR; Q6DYE8; -.
DR BioGRID; 229091; 1.
DR STRING; 10090.ENSMUSP00000020169; -.
DR GlyGen; Q6DYE8; 9 sites.
DR iPTMnet; Q6DYE8; -.
DR PhosphoSitePlus; Q6DYE8; -.
DR jPOST; Q6DYE8; -.
DR MaxQB; Q6DYE8; -.
DR PaxDb; Q6DYE8; -.
DR PeptideAtlas; Q6DYE8; -.
DR PRIDE; Q6DYE8; -.
DR ProteomicsDB; 275909; -.
DR Antibodypedia; 32905; 480 antibodies from 36 providers.
DR DNASU; 209558; -.
DR Ensembl; ENSMUST00000020169; ENSMUSP00000020169; ENSMUSG00000019989.
DR GeneID; 209558; -.
DR KEGG; mmu:209558; -.
DR UCSC; uc007era.1; mouse.
DR CTD; 5169; -.
DR MGI; MGI:2143702; Enpp3.
DR VEuPathDB; HostDB:ENSMUSG00000019989; -.
DR eggNOG; KOG2645; Eukaryota.
DR GeneTree; ENSGT00940000159640; -.
DR HOGENOM; CLU_012256_0_1_1; -.
DR InParanoid; Q6DYE8; -.
DR OMA; CETDLLH; -.
DR OrthoDB; 999163at2759; -.
DR PhylomeDB; Q6DYE8; -.
DR TreeFam; TF330032; -.
DR BioGRID-ORCS; 209558; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Enpp3; mouse.
DR PRO; PR:Q6DYE8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6DYE8; protein.
DR Bgee; ENSMUSG00000019989; Expressed in epithelium of small intestine and 175 other tissues.
DR ExpressionAtlas; Q6DYE8; baseline and differential.
DR Genevisible; Q6DYE8; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IMP:UniProtKB.
DR GO; GO:0004528; F:phosphodiesterase I activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; IMP:UniProtKB.
DR GO; GO:0002276; P:basophil activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0033007; P:negative regulation of mast cell activation involved in immune response; IMP:UniProtKB.
DR GO; GO:0070667; P:negative regulation of mast cell proliferation; IMP:UniProtKB.
DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISO:MGI.
DR GO; GO:0055062; P:phosphate ion homeostasis; IDA:MGI.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:MGI.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.570.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR036024; Somatomedin_B-like_dom_sf.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF01033; Somatomedin_B; 2.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SMART; SM00201; SO; 2.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF90188; SSF90188; 2.
DR PROSITE; PS00524; SMB_1; 2.
DR PROSITE; PS50958; SMB_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW Metal-binding; Multifunctional enzyme; Reference proteome; Repeat;
KW Secreted; Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..874
FT /note="Ectonucleotide pyrophosphatase/phosphodiesterase
FT family member 3"
FT /id="PRO_0000281652"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..874
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 51..93
FT /note="SMB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DOMAIN 94..138
FT /note="SMB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT REGION 140..509
FT /note="Phosphodiesterase"
FT REGION 605..874
FT /note="Nuclease"
FT MOTIF 78..80
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15396"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 751
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 753
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 755
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 757
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT BINDING 759
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 701
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 54..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 58..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 69..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 69..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 75..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 82..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00350"
FT DISULFID 98..115
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 103..133
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 113..126
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 119..125
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 144..190
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 152..364
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 380..477
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 428..817
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 561..623
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 574..679
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 576..664
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT DISULFID 786..796
FT /evidence="ECO:0000250|UniProtKB:O14638"
FT CONFLICT 212
FT /note="I -> S (in Ref. 1; AAT64421)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="D -> V (in Ref. 1; AAT64421)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="A -> V (in Ref. 1; AAT64421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 874 AA; 98662 MW; 6CFF970ECC830D08 CRC64;
MDSRLALATE EPIKKDSLKK YKILCVVLLA LLVIVSLGLG LGLGLRKPEE QGSCRKKCFD
SSHRGLEGCR CDSGCTGRGD CCWDFEDTCV KSTQIWTCNL FRCGENRLET ALCSCADDCL
QRKDCCADYK TVCQGESPWV TEACASSQEP QCPPGFDLPP VILFSMDGFR AEYLQTWSTL
LPNINKLKTC GIHSKYMRAM YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VHLNKNFSLS
SVEKSNPAWW SGQPIWLTAM YQGLKAACYY WPGSDVAVNG SFPTIYRNYS NSVPYERRIT
TLLQWLDLPK ADRPSFYTIY VEEPDSAGHS SGPVSAGVIK ALQSVDNAFG MLMEGLKQRN
LHNCVNIIVL ADHGMDQTSC DRVEYMTDYF PKINFYMYQG PAPRIRTRNI PQDFFTFNSE
EIVRNLSCRK PDQHFKPYLT PDLPKRLHYA KNVRIDKAHL MVDRQWLAFR SKGSSNCGGG
THGYNNEFKS MEAIFLAHGP SFIEKTVIEP FENIEVYNLL CDLLHIEPAP NNGTHGSLNH
LLKTPFYKPS HAGELSTPAD CGFTTPLPTD PLDCSCPALQ NTPGLEEQAN QRLNLSEGEV
AATVKANLPF GRPRVMQKNG DHCLLYHRDY ISGYGKAMKM PMWSSYTVLK PGDTSSLPPT
VPDCLRADVR VAPSESQKCS FYLADKNITH GFLYPAIKGT NESRYDALIT SNLVPMYKEF
KKMWDYFHEV LLIKYAIERN GLNVVSGPIF DYNYDGHFDA PDEITQYVAG TDVPIPTHYF
VVLTSCKDQT HTPDSCPGWL DVLPFIVPHR PTNIESCSEN KTEDLWVEER FQAHAARVRD
VELLTGLDFY QEKAQPVSQI LQLKTYLPTF ETII
