SWS_DROME
ID SWS_DROME Reviewed; 1425 AA.
AC Q9U969; A8E6M7; Q8IRN7; Q95RE9; Q9W3M0;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Neuropathy target esterase sws;
DE AltName: Full=Swiss cheese;
DE Short=DSWS;
DE EC=3.1.1.5;
GN Name=sws; ORFNames=CG2212;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, ALTERNATIVE SPLICING,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-648 AND
RP GLY-956.
RX PubMed=9295388; DOI=10.1523/jneurosci.17-19-07425.1997;
RA Kretzschmar D., Hasan G., Sharma S., Heisenberg M., Benzer S.;
RT "The swiss cheese mutant causes glial hyperwrapping and brain degeneration
RT in Drosophila.";
RL J. Neurosci. 17:7425-7432(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1052-1425 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF SER-985.
RX PubMed=15772346; DOI=10.1523/jneurosci.5097-04.2005;
RA Muehlig-Versen M., da Cruz A.B., Tschaepe J.-A., Moser M., Buettner R.,
RA Athenstaedt K., Glynn P., Kretzschmar D.;
RT "Loss of swiss cheese/neuropathy target esterase activity causes disruption
RT of phosphatidylcholine homeostasis and neuronal and glial death in adult
RT Drosophila.";
RL J. Neurosci. 25:2865-2873(2005).
RN [7]
RP FUNCTION, INTERACTION WITH PKA-C3, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ARG-133.
RX PubMed=18945896; DOI=10.1523/jneurosci.3015-08.2008;
RA Bettencourt da Cruz A., Wentzell J., Kretzschmar D.;
RT "Swiss cheese, a protein involved in progressive neurodegeneration, acts as
RT a noncanonical regulatory subunit for PKA-C3.";
RL J. Neurosci. 28:10885-10892(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-453 AND SER-1160,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Phospholipase B that deacylates intracellular
CC phosphatidylcholine (PtdCho), generating glycerophosphocholine
CC (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of
CC PtdCho. Its specific chemical modification by certain organophosphorus
CC (OP) compounds leads to distal axonopathy. Plays a role in the
CC signaling mechanism between neurons and glia that regulates glia
CC wrapping during development of the adult brain. Essential for membrane
CC lipid homeostasis and cell survival in both neurons and glia of the
CC adult brain. {ECO:0000269|PubMed:15772346, ECO:0000269|PubMed:18945896,
CC ECO:0000269|PubMed:9295388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000269|PubMed:15772346};
CC -!- SUBUNIT: Interacts with Pka-C3; interaction inhibits the catalytic
CC function of Pka-C3 and the esterase activity of sws.
CC {ECO:0000269|PubMed:18945896}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15772346, ECO:0000269|PubMed:18945896}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:15772346,
CC ECO:0000269|PubMed:18945896}. Note=Sws tethers Pka-C3 to the membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=Long;
CC IsoId=Q9U969-1; Sequence=Displayed;
CC Name=B; Synonyms=Short;
CC IsoId=Q9U969-2; Sequence=VSP_038398, VSP_038399, VSP_038400;
CC Name=C;
CC IsoId=Q9U969-3; Sequence=VSP_038399, VSP_038400;
CC -!- TISSUE SPECIFICITY: Isoform A and isoform B are expressed in the entire
CC brain cortex; cortical cell bodies of adult brain. Sws and Pka-C3 are
CC colocalized in all neurons. {ECO:0000269|PubMed:15772346,
CC ECO:0000269|PubMed:18945896, ECO:0000269|PubMed:9295388}.
CC -!- DEVELOPMENTAL STAGE: Isoform A is expressed in all developmental stages
CC with highest levels in young embryos and adults. Isoform B is detected
CC only in adult head. {ECO:0000269|PubMed:9295388}.
CC -!- DISRUPTION PHENOTYPE: Progressive degeneration of the adult nervous
CC system, associated with apoptotic cell death, glial hyperwrapping, and
CC neuronal apoptosis. Also, vacuolization in the neuropil.
CC {ECO:0000269|PubMed:18945896}.
CC -!- SIMILARITY: Belongs to the NTE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28979.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z97187; CAB51772.1; -; mRNA.
DR EMBL; AE014298; AAF46305.3; -; Genomic_DNA.
DR EMBL; AE014298; AAN09223.1; -; Genomic_DNA.
DR EMBL; BT030819; ABV82201.1; -; mRNA.
DR EMBL; AY061431; AAL28979.1; ALT_INIT; mRNA.
DR RefSeq; NP_511075.3; NM_078520.3. [Q9U969-1]
DR RefSeq; NP_727225.1; NM_167141.3. [Q9U969-2]
DR AlphaFoldDB; Q9U969; -.
DR SMR; Q9U969; -.
DR BioGRID; 58188; 5.
DR IntAct; Q9U969; 2.
DR STRING; 7227.FBpp0071077; -.
DR iPTMnet; Q9U969; -.
DR PaxDb; Q9U969; -.
DR PRIDE; Q9U969; -.
DR DNASU; 31716; -.
DR EnsemblMetazoa; FBtr0071125; FBpp0071077; FBgn0003656. [Q9U969-1]
DR EnsemblMetazoa; FBtr0071126; FBpp0071078; FBgn0003656. [Q9U969-2]
DR GeneID; 31716; -.
DR KEGG; dme:Dmel_CG2212; -.
DR UCSC; CG2212-RB; d. melanogaster.
DR CTD; 31716; -.
DR FlyBase; FBgn0003656; sws.
DR VEuPathDB; VectorBase:FBgn0003656; -.
DR eggNOG; KOG2968; Eukaryota.
DR GeneTree; ENSGT00940000168388; -.
DR HOGENOM; CLU_000960_1_0_1; -.
DR InParanoid; Q9U969; -.
DR OMA; FMYFKRL; -.
DR PhylomeDB; Q9U969; -.
DR Reactome; R-DME-6814848; Glycerophospholipid catabolism.
DR BioGRID-ORCS; 31716; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31716; -.
DR PRO; PR:Q9U969; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003656; Expressed in egg cell and 26 other tissues.
DR ExpressionAtlas; Q9U969; baseline and differential.
DR Genevisible; Q9U969; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:FlyBase.
DR GO; GO:0007272; P:ensheathment of neurons; IMP:FlyBase.
DR GO; GO:0034349; P:glial cell apoptotic process; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006643; P:membrane lipid metabolic process; IDA:FlyBase.
DR GO; GO:0061024; P:membrane organization; IDA:FlyBase.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IMP:FlyBase.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:FlyBase.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:FlyBase.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:FlyBase.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0072657; P:protein localization to membrane; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR CDD; cd00038; CAP_ED; 3.
DR Gene3D; 2.60.120.10; -; 3.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR001423; LysoPLipase_patatin_CS.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF01734; Patatin; 1.
DR SMART; SM00100; cNMP; 3.
DR SUPFAM; SSF51206; SSF51206; 3.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 3.
DR PROSITE; PS51635; PNPLA; 1.
DR PROSITE; PS01237; UPF0028; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Endoplasmic reticulum;
KW Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Neurogenesis;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1425
FT /note="Neuropathy target esterase sws"
FT /id="PRO_0000172527"
FT TOPO_DOM 1..34
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..1425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 952..1118
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 332..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 956..961
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 983..987
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 1105..1107
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 332..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 985
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 1105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT BINDING 174..301
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 482..609
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT BINDING 598..727
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="3"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..1084
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_038398"
FT VAR_SEQ 1087..1098
FT /note="LSGYMPPLCDPK -> IAGVFPPFCDYR (in isoform B and
FT isoform C)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_038399"
FT VAR_SEQ 1107..1112
FT /note="GYVNNL -> CYTNNV (in isoform B and isoform C)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_038400"
FT MUTAGEN 133
FT /note="R->A: Has no effect on nervous system function but
FT reduces binding to Pka-C3."
FT /evidence="ECO:0000269|PubMed:18945896"
FT MUTAGEN 648
FT /note="G->R: In allele sws-5; age-dependent
FT neurodegeneration."
FT /evidence="ECO:0000269|PubMed:9295388"
FT MUTAGEN 956
FT /note="G->D: In allele sws-4; age-dependent
FT neurodegeneration."
FT /evidence="ECO:0000269|PubMed:9295388"
FT MUTAGEN 985
FT /note="S->D: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15772346"
FT CONFLICT 18
FT /note="I -> T (in Ref. 1; CAB51772)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="L -> F (in Ref. 4; ABV82201)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="G -> P (in Ref. 1; CAB51772)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="R -> H (in Ref. 1; CAB51772)"
FT /evidence="ECO:0000305"
FT CONFLICT 1076
FT /note="S -> H (in Ref. 4; ABV82201)"
FT /evidence="ECO:0000305"
FT CONFLICT 1081..1083
FT /note="VRS -> CRA (in Ref. 4; ABV82201)"
FT /evidence="ECO:0000305"
FT CONFLICT 1377
FT /note="T -> N (in Ref. 1; CAB51772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1425 AA; 160573 MW; A7FEE533B1C2B628 CRC64;
MDVLEMLRAS ASGSYNTIFS DAWCQYVSKQ ITATVYMYFA LVMMSLLFIA WFLYFKRMAR
LRLRDEIARS ISTVTNSSGD MRGLRFRKRD KMLFYGRRML RKMKNVSGQM YSSGKGYKRR
AVMRFARRIL QLRRDNMPLE MRTVEPPAEY LEETIEGSDR VPPDALYMLQ SIRIFGHFEK
PVFLRLCKHT QLLELMAGDY LFKITDPDDS VYIVQSGMIN VYISNADGST LSLKTVRKGE
SVTSLLSFID VLSGNPSYYK TVTAKAIEKS VVIRLPMQAF EEVFQDNPDV MIRVIQVIMI
RLQRVLFTAL RNYLGLNAEL VQNHMRYKSV STMSGPINSQ TSQSSRQAPN GPPMVISQMN
LMQSAVSGTG SSGVSVTVTR PPSSPSRHSR EEHTLSDPNP NPDGSFHGTT NLFTEVHGDA
PNADLFHQQQ QQHSVGNLST RRSSITLMAP DGSHSCLQTP GVTTSIDMRL VQSSAVDSLR
KELGLSEEDS HIIEPFVELR ELEPNVTLIT EGNADDVCVW FVMTGTLAVY QSNQDATRAK
QDKSDMLIHF VHPGEIVGGL AMLTGEASAY TIRSRSITRI AFIRRAAIYQ IMRQRPRIVL
DLGNGVVRRL SPLVRQCDYA LDWIFLESGR AVYRQDESSD STYIVLSGRM RSVITHPGGK
KEIVGEYGKG DLVGIVEMIT ETSRTTTVMA VRDSELAKLP EGLFNAIKLR YPIVVTKLIS
FLSHRFLGSM QTRSGSGAPG APVEANPVTH KYSTVALVPI TDEVPMTPFT YELYHSLCAI
GPVLRLTSDV VRKQLGSNIF EAANEYRLTS WLAQQEDRNI ITLYQCDSSL SAWTQRCMRQ
ADVILIVGLG DRSHLVGKFE REIDRLAMRT QKELVLLYPE ASNAKPANTL SWLNARPWVT
KHHHVLCVKR IFTRKSQYRI NDLYSRVLLS EPNMHSDFSR LARWLTGNSI GLVLGGGGAR
GAAHIGMLKA IQEAGIPVDM VGGVSIGALM GALWCSERNI TTVTQKAREW SKKMTKWFLQ
LLDLTYPITS MFSGREFNKT IHDTFGDVSI EDLWIPYFTL TTDITASCHR IHTNGSLWRY
VRSSMSLSGY MPPLCDPKDG HLLLDGGYVN NLPADVMHNL GAAHIIAIDV GSQDDTDLTN
YGDDLSGWWL LYKKWNPFTS PVKVPDLPDI QSRLAYVSCV RQLEEVKNSD YCEYIRPPID
KYKTLAFGSF DEIRDVGYVF GKNYFESMAK AGRLGRFNQW FNKEPPKRVN HASLNEYTFI
DLAQIVCRLP ETYAVNTAEL FSEDEDCDGY ISEPTTLNTD RRRIQVSRAG NSLSFSETEM
DSDVELDLKL ERKTDKSTQS SPPSNSRSDM RGKEEARHMS NWHWGVKHKD ETGSGATEAT
KTQTGQEQEL QQEQQDQGAT AEQLVDKDKE ENKENRSSPN NETKN
