NEP2_DROME
ID NEP2_DROME Reviewed; 774 AA.
AC A0A0B4K692; D3DMK4; Q9XZ01;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Neprilysin-2 {ECO:0000303|PubMed:15554877};
DE EC=3.4.24.11 {ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960};
DE Contains:
DE RecName: Full=Neprilysin-2, soluble form {ECO:0000305};
GN Name=Nep2 {ECO:0000303|PubMed:15554877, ECO:0000312|FlyBase:FBgn0027570};
GN ORFNames=CG9761 {ECO:0000312|FlyBase:FBgn0027570};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAD34741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAD34741.1};
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [4] {ECO:0000312|EMBL:ADB91418.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-354.
RA Carlson J., Booth B., Frise E., Sandler J., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=15554877; DOI=10.1042/bj20041753;
RA Thomas J.E., Rylett C.M., Carhan A., Bland N.D., Bingham R.J.,
RA Shirras A.D., Turner A.J., Isaac R.E.;
RT "Drosophila melanogaster NEP2 is a new soluble member of the neprilysin
RT family of endopeptidases with implications for reproduction and renal
RT function.";
RL Biochem. J. 386:357-366(2005).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RX PubMed=17157960; DOI=10.1016/j.peptides.2006.08.032;
RA Bland N.D., Thomas J.E., Audsley N., Shirras A.D., Turner A.J., Isaac R.E.;
RT "Expression of NEP2, a soluble neprilysin-like endopeptidase, during
RT embryogenesis in Drosophila melanogaster.";
RL Peptides 28:127-135(2007).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24395329; DOI=10.1534/genetics.113.160945;
RA Sitnik J.L., Francis C., Hens K., Huybrechts R., Wolfner M.F.,
RA Callaerts P.;
RT "Neprilysins: an evolutionarily conserved family of metalloproteases that
RT play important roles in reproduction in Drosophila.";
RL Genetics 196:781-797(2014).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27629706; DOI=10.1523/jneurosci.3730-15.2016;
RA Turrel O., Lampin-Saint-Amaux A., Preat T., Goguel V.;
RT "Drosophila neprilysins are involved in middle-term and long-term memory.";
RL J. Neurosci. 36:9535-9546(2016).
CC -!- FUNCTION: Metalloendoprotease which cleaves peptides such as tachykinin
CC peptide TK-2 at the amino side of hydrophobic residues
CC (PubMed:15554877, PubMed:17157960). Functions in female fertility,
CC embryogenesis and memory formation (PubMed:24395329, PubMed:27629706).
CC Required in females for normal patterns of egg laying, probably due to
CC its function in sperm retention and preventing sperm displacement by
CC rival ejaculates (PubMed:24395329). Also required for normal patterns
CC of hatching due to its important role in early embryonic development
CC (PubMed:24395329). Required in the dorsal paired medial neurons for the
CC proper formation of middle-term memory (PubMed:27629706). Also required
CC in the mushroom body neurons where it functions redundantly with
CC neprilysins Nep3 and Nep4 in normal long-term memory formation
CC (PubMed:27629706). {ECO:0000269|PubMed:15554877,
CC ECO:0000269|PubMed:17157960, ECO:0000269|PubMed:24395329,
CC ECO:0000269|PubMed:27629706}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage of polypeptides between hydrophobic
CC residues, particularly with Phe or Tyr at P1'.; EC=3.4.24.11;
CC Evidence={ECO:0000269|PubMed:15554877, ECO:0000269|PubMed:17157960};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P08473};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P08473};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-7.5 at 35 degrees Celsius.
CC {ECO:0000269|PubMed:17157960};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:15554877,
CC ECO:0000269|PubMed:17157960}. Note=A secreted form exists that is
CC probably produced by proteolytic cleavage (Probable). In embryos, adult
CC Malpighian tubules and testes, detected in the soluble fraction but is
CC not detected in the membrane fraction (PubMed:15554877,
CC PubMed:17157960). {ECO:0000269|PubMed:15554877,
CC ECO:0000269|PubMed:17157960, ECO:0000305|PubMed:15554877,
CC ECO:0000305|PubMed:17157960}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0027570};
CC IsoId=A0A0B4K692-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0027570}; Synonyms=C
CC {ECO:0000312|FlyBase:FBgn0027570};
CC IsoId=A0A0B4K692-2; Sequence=VSP_059155;
CC -!- TISSUE SPECIFICITY: Detected in the stellate cells in the main segment
CC and the bar-shaped cells in the initial segment of male and female
CC Malpighian tubules (at protein level) (PubMed:15554877). Expressed in
CC the spermatheca (at protein level) (PubMed:24395329). Expressed in the
CC somatic cyst cells of the testes, with increased expression at the tail
CC end of elongating cysts (PubMed:15554877, PubMed:24395329). Expressed
CC in the ovaries with strong expression in the posterior polar cells and
CC in border cells of stage 8, 9, and 10 follicles (PubMed:24395329). In
CC adults and third-instar larvae, expressed in the brain, ventral
CC ganglion, and stellate cells (PubMed:24395329). Also expressed in the
CC foregut and the imaginal disks (eye, antennal and leg) of third-instar
CC larvae (PubMed:24395329). In stage 17 embryos, expressed in the
CC tracheal system, foregut, hindgut and epidermis (PubMed:24395329). Also
CC expressed in the stellate cell progenitors of the caudal visceral
CC mesoderm in embryos (PubMed:17157960). {ECO:0000269|PubMed:15554877,
CC ECO:0000269|PubMed:17157960, ECO:0000269|PubMed:24395329}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17157960}.
CC -!- PTM: The soluble form is probably produced by proteolytic cleavage.
CC {ECO:0000305|PubMed:15554877, ECO:0000305|PubMed:17157960}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in females mated to wild-
CC type males results in laying of fewer eggs due to impaired sperm
CC retention and increased sperm displacement by rival ejaculates
CC (PubMed:24395329). Females also show a reduced hatch rate and only 20%
CC of their progeny reach the adult stage (PubMed:24395329). Unhatched
CC eggs are fertilized but contain a clear polar body rosette instead of
CC an embryo, suggesting that the eggs activate and complete meiosis but
CC then embryogenesis is arrested (PubMed:24395329). Wild-type females
CC mated to males that undergo RNAi-mediated knockdown, display a slight
CC reduction in fertility but lay the same number of eggs and have the
CC same hatch rate as those mated to wild-type males (PubMed:24395329).
CC RNAi-mediated knockdown in the dorsal paired medial neurons impairs
CC middle-term memory (MTM), but has no effect on long-term memory (LTM)
CC formation, normal aversion learning and anesthesia-resistant memory
CC (ARM) (PubMed:27629706). RNAi-mediated knockdown in all mushroom body
CC neurons has no effect on learning, ARM and LTM (PubMed:27629706).
CC However, simultaneous knockdown with Nep3 does impair LTM, and
CC simultaneous knockdown with both Nep3 and Nep4 results in a further
CC reduction in LTM formation (PubMed:27629706). Simultaneous knockdown
CC with only Nep4 has no effect on LTM formation (PubMed:27629706).
CC {ECO:0000269|PubMed:24395329, ECO:0000269|PubMed:27629706}.
CC -!- SIMILARITY: Belongs to the peptidase M13 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01233, ECO:0000305}.
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DR EMBL; AE014297; AAF52100.1; -; Genomic_DNA.
DR EMBL; AE014297; AFH06233.1; -; Genomic_DNA.
DR EMBL; AE014297; AGB95643.1; -; Genomic_DNA.
DR EMBL; AF132153; AAD34741.1; -; mRNA.
DR EMBL; BT120170; ADB91418.1; -; mRNA.
DR RefSeq; NP_001246914.1; NM_001259985.2. [A0A0B4K692-1]
DR RefSeq; NP_001262260.1; NM_001275331.1. [A0A0B4K692-2]
DR RefSeq; NP_524227.1; NM_079503.4. [A0A0B4K692-2]
DR AlphaFoldDB; A0A0B4K692; -.
DR SMR; A0A0B4K692; -.
DR STRING; 7227.FBpp0293663; -.
DR MEROPS; M13.012; -.
DR GlyGen; A0A0B4K692; 8 sites.
DR PaxDb; A0A0B4K692; -.
DR DNASU; 40588; -.
DR EnsemblMetazoa; FBtr0078891; FBpp0078531; FBgn0027570. [A0A0B4K692-2]
DR EnsemblMetazoa; FBtr0305133; FBpp0293663; FBgn0027570. [A0A0B4K692-1]
DR EnsemblMetazoa; FBtr0333922; FBpp0306050; FBgn0027570. [A0A0B4K692-2]
DR GeneID; 40588; -.
DR KEGG; dme:Dmel_CG9761; -.
DR UCSC; CG9761-RA; d. melanogaster.
DR CTD; 40588; -.
DR FlyBase; FBgn0027570; Nep2.
DR VEuPathDB; VectorBase:FBgn0027570; -.
DR eggNOG; KOG3624; Eukaryota.
DR OMA; EKLGGWP; -.
DR PhylomeDB; A0A0B4K692; -.
DR BRENDA; 3.4.24.B14; 1994.
DR Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 40588; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Nep2; fly.
DR GenomeRNAi; 40588; -.
DR PRO; PR:A0A0B4K692; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0027570; Expressed in spermathecum and 37 other tissues.
DR ExpressionAtlas; A0A0B4K692; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0004175; F:endopeptidase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IMP:FlyBase.
DR GO; GO:0008237; F:metallopeptidase activity; ISM:FlyBase.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:FlyBase.
DR GO; GO:0046692; P:sperm competition; IMP:FlyBase.
DR CDD; cd08662; M13; 1.
DR Gene3D; 1.10.1380.10; -; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR000718; Peptidase_M13.
DR InterPro; IPR018497; Peptidase_M13_C.
DR InterPro; IPR042089; Peptidase_M13_dom_2.
DR InterPro; IPR008753; Peptidase_M13_N.
DR PANTHER; PTHR11733; PTHR11733; 1.
DR Pfam; PF01431; Peptidase_M13; 1.
DR Pfam; PF05649; Peptidase_M13_N; 1.
DR PRINTS; PR00786; NEPRILYSIN.
DR PROSITE; PS51885; NEPRILYSIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..774
FT /note="Neprilysin-2"
FT /id="PRO_0000441990"
FT CHAIN ?..774
FT /note="Neprilysin-2, soluble form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000441991"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..774
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 83..774
FT /note="Peptidase M13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT REGION 50..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 675
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT BINDING 609
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 613
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 653
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 84..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 107..759
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 115..719
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 171..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT DISULFID 646..771
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01233"
FT VAR_SEQ 432..442
FT /note="Missing (in isoform A)"
FT /id="VSP_059155"
SQ SEQUENCE 774 AA; 88125 MW; 7E00BC75EF4472E4 CRC64;
MQTVIQNPNW WRRRNKLEKS LLVSLGIMFV VLATGFGLWI GKVLRTSPPS NPQATALHGD
STTINQVPTG TASKGKSGDS GDVCLTQECI HTASTVLRKM KPEVEPCDNF YEFACGTYLE
EENIPDDKVS ISTFSVISDK LQEQLKDIIT AERPETEPKH FRLPNLLYKA CMNKTLIETL
GPEPITRVAE RLGGWPLIKG DSWNADDSWT WQEQVKKFRT AGFSMDYIID FSIGVDLQNS
TKRLIDLDQS SLALSREYLV KGFNETLVTA YYKYMVDIAV LFGANRDLAK TELLLSLEFE
MALANISWPN EKRRNSSELY NLRTPAQLQA AYPYVQWVDY MNALLPEGLN VAEDEMINLS
VPSFFEDLGK LLAKTPKRVI ANYMFWRIHG FSVGFLSEEF RKRQLQYATA LSGRQEQEAR
WKECVDIATS SMDEVCEDDF DSLGISVGSL YVGKHFHKDS KANALEMVNE IRNVFNDILD
EVNWMDAKTK KEAKLKLHSM ATHIGYPDEM LDNEKLAAYY AKLDIDPDKY FESFLGMNIF
GTDYSFNKLR LPVNKTDWVR HARPAIVNAF YSSLENSIQF PAGILQGHFF NAQRPKYMNF
GAIGYVIGHE ITHGFDDQGR QFDVKGNLRD WWHPDTQKAY LAKAKCIIEQ YGNYTERATG
LNLNGINTQG ENIADNGGVK ESYIAYRRWA EKHGPEAKLP GLDYTPEQMF WVAAGQTWCA
KYRKESLKMR ITTGVHSPSE FRVLGSLSNM KDFAKDFHCP EGSPMNPVQK CEVW
