A4_CAEEL
ID A4_CAEEL Reviewed; 686 AA.
AC Q10651; Q18583; Q95ZX1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Amyloid-beta-like protein {ECO:0000305};
DE Flags: Precursor;
GN Name=apl-1 {ECO:0000312|WormBase:C42D8.8a};
GN ORFNames=C42D8.8 {ECO:0000312|WormBase:C42D8.8a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-686.
RC STRAIN=Bristol N2;
RX PubMed=8265668; DOI=10.1073/pnas.90.24.12045;
RA Daigle I., Li C.;
RT "apl-1, a Caenorhabditis elegans gene encoding a protein related to the
RT human beta-amyloid protein precursor.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:12045-12049(1993).
RN [3]
RP INTERACTION WITH FEH-1, AND DISRUPTION PHENOTYPE.
RX PubMed=11896189; DOI=10.1242/jcs.115.7.1411;
RA Zambrano N., Bimonte M., Arbucci S., Gianni D., Russo T., Bazzicalupo P.;
RT "feh-1 and apl-1, the Caenorhabditis elegans orthologues of mammalian Fe65
RT and beta-amyloid precursor protein genes, are involved in the same pathway
RT that controls nematode pharyngeal pumping.";
RL J. Cell Sci. 115:1411-1422(2002).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, PROTEOLYTIC CLEAVAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLU-377.
RX PubMed=17267616; DOI=10.1073/pnas.0603997104;
RA Hornsten A., Lieberthal J., Fadia S., Malins R., Ha L., Xu X., Daigle I.,
RA Markowitz M., O'Connor G., Plasterk R., Li C.;
RT "APL-1, a Caenorhabditis elegans protein related to the human beta-amyloid
RT precursor protein, is essential for viability.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1971-1976(2007).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18262516; DOI=10.1016/j.ydbio.2007.12.044;
RA Niwa R., Zhou F., Li C., Slack F.J.;
RT "The expression of the Alzheimer's amyloid precursor protein-like gene is
RT regulated by developmental timing microRNAs and their targets in
RT Caenorhabditis elegans.";
RL Dev. Biol. 315:418-425(2008).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20862215; DOI=10.1371/journal.pone.0012790;
RA Wiese M., Antebi A., Zheng H.;
RT "Intracellular trafficking and synaptic function of APL-1 in Caenorhabditis
RT elegans.";
RL PLoS ONE 5:3307-3314(2010).
RN [8]
RP FUNCTION.
RX PubMed=22466039; DOI=10.1534/genetics.112.138768;
RA Ewald C.Y., Raps D.A., Li C.;
RT "APL-1, the Alzheimer's Amyloid precursor protein in Caenorhabditis
RT elegans, modulates multiple metabolic pathways throughout development.";
RL Genetics 191:493-507(2012).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=28933985; DOI=10.1080/15384101.2017.1344798;
RA Metheetrairut C., Ahuja Y., Slack F.J.;
RT "acn-1, a C. elegans homologue of ACE, genetically interacts with the let-7
RT microRNA and other heterochronic genes.";
RL Cell Cycle 16:1800-1809(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 240-478 IN COMPLEX WITH HEPARIN
RP ANALOG, AND MUTAGENESIS OF ASN-252; HIS-254; ASP-348; SER-368; ARG-374;
RP GLU-377; LYS-378 AND HIS-382.
RX PubMed=19906646; DOI=10.1074/jbc.m109.018432;
RA Hoopes J.T., Liu X., Xu X., Demeler B., Folta-Stogniew E., Li C., Ha Y.;
RT "Structural characterization of the E2 domain of APL-1, a Caenorhabditis
RT elegans homolog of human amyloid precursor protein, and its heparin binding
RT site.";
RL J. Biol. Chem. 285:2165-2173(2010).
RN [11]
RP STRUCTURE BY NMR OF 135-197, DISULFIDE BONDS, AND LACK OF COPPER-BINDING.
RX PubMed=24276282; DOI=10.1039/c3mt00258f;
RA Leong S.L., Young T.R., Barnham K.J., Wedd A.G., Hinds M.G., Xiao Z.,
RA Cappai R.;
RT "Quantification of copper binding to amyloid precursor protein domain 2 and
RT its Caenorhabditis elegans ortholog. Implications for biological
RT function.";
RL Metallomics 6:105-116(2014).
CC -!- FUNCTION: Required for normal developmental progression throughout all
CC life stages (PubMed:18262516, PubMed:22466039). Specifically required
CC for the molt stage during all larval transitions and morphogenesis
CC (PubMed:18262516, PubMed:17267616, PubMed:22466039). Acts with
CC heterochronic genes, including members of the let-7 family, to regulate
CC larval stage to adult transition (PubMed:18262516, PubMed:28933985).
CC Acts synergistically with acn-1 in let-7 regulated postembryonic cell
CC division of hypodermal seam cells (PubMed:28933985). Acts in multiple
CC pathways to influence daf-12 and daf-16 activity to in turn regulate
CC physiological and reproductive processes such as body size and egg-
CC laying (PubMed:22466039). May play a role in neurotransmission
CC (PubMed:20862215). {ECO:0000269|PubMed:17267616,
CC ECO:0000269|PubMed:18262516, ECO:0000269|PubMed:20862215,
CC ECO:0000269|PubMed:22466039, ECO:0000269|PubMed:28933985}.
CC -!- SUBUNIT: Interacts (via cytoplasmic domain) with feh-1 (via PID 2
CC domain). {ECO:0000269|PubMed:11896189}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Early endosome
CC {ECO:0000269|PubMed:20862215}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q10651-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q10651-2; Sequence=VSP_000017;
CC -!- TISSUE SPECIFICITY: Expressed in the head, pharynx, spermatheca,
CC uterus, vulva, tail and ventral neurons (PubMed:18262516). Specifically
CC expressed in nerve ring interneurons, the ventral cord, socket and
CC amphids in the head, with strong expression in junctional cells,
CC including the pharyngeal intestinal valve and uterine seam junction,
CC and the excretory cell and weak expression in epidermal epithelial
CC cells, including hyp7 cells, vulval cells, rectal valve cells,
CC pharyngeal arcade cells and the tail hypodermis (PubMed:20862215).
CC {ECO:0000269|PubMed:17267616, ECO:0000269|PubMed:20862215}.
CC -!- DEVELOPMENTAL STAGE: Similar expression pattern in larval and adult
CC cells with expression in neuronal, muscle, hypodermal and supporting
CC cells (PubMed:17267616). Temporally expressed in seam cells from the
CC middle of larval stage L4 and throughout adult stages (PubMed:18262516,
CC PubMed:28933985). {ECO:0000269|PubMed:17267616,
CC ECO:0000269|PubMed:18262516, ECO:0000269|PubMed:28933985}.
CC -!- DOMAIN: The NPXY motif mediates the interaction with clathrin.
CC {ECO:0000255}.
CC -!- PTM: Extracellular region is proteolytically cleaved.
CC {ECO:0000269|PubMed:17267616}.
CC -!- DISRUPTION PHENOTYPE: Larval lethality during the L1 stage, with the
CC formation of vacuoles in syncytial hypoderm, organ morphology defects,
CC and molting defects (PubMed:17267616, PubMed:20862215). RNAi-mediated
CC knockdown results in a reduced body size, transparent appearance,
CC sluggish movement and insensitivity to touch (PubMed:18262516,
CC PubMed:20862215). Delayed development and a molting defect that begins
CC at the L3 to L4 larval stage transition and continues through to
CC transition from the L4 larval stage to the young adult stage
CC (PubMed:20862215). Increased sensitivity to acetylcholine inhibition
CC (PubMed:20862215). Increased pharyngeal pumping (PubMed:11896189). In a
CC let-7 mutant background, partial suppression of the let-7 bursting
CC vulva phenotype (PubMed:28933985). Double RNAi-mediated knockdown with
CC acn-1 in a let-7 mutant background leads to complete suppression of the
CC heterochronic seam cell defects (PubMed:28933985).
CC {ECO:0000269|PubMed:11896189, ECO:0000269|PubMed:17267616,
CC ECO:0000269|PubMed:18262516, ECO:0000269|PubMed:20862215,
CC ECO:0000269|PubMed:28933985}.
CC -!- MISCELLANEOUS: Lacks conserved metal-binding sites and has only weak
CC affinity for copper in vitro. {ECO:0000269|PubMed:24276282}.
CC -!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01217}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC46470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FO080659; CCD65568.1; -; Genomic_DNA.
DR EMBL; FO080659; CCD65569.1; -; Genomic_DNA.
DR EMBL; U00240; AAC46470.1; ALT_INIT; mRNA.
DR PIR; T15795; T15795.
DR RefSeq; NP_508870.3; NM_076469.5. [Q10651-1]
DR RefSeq; NP_508871.1; NM_076470.4. [Q10651-2]
DR PDB; 2M05; NMR; -; A=135-197.
DR PDB; 3K66; X-ray; 2.70 A; A=240-478.
DR PDB; 3K6B; X-ray; 2.80 A; A=240-478.
DR PDBsum; 2M05; -.
DR PDBsum; 3K66; -.
DR PDBsum; 3K6B; -.
DR AlphaFoldDB; Q10651; -.
DR BMRB; Q10651; -.
DR SMR; Q10651; -.
DR BioGRID; 45718; 4.
DR DIP; DIP-25431N; -.
DR STRING; 6239.C42D8.8a; -.
DR iPTMnet; Q10651; -.
DR EPD; Q10651; -.
DR PaxDb; Q10651; -.
DR PeptideAtlas; Q10651; -.
DR EnsemblMetazoa; C42D8.8a.1; C42D8.8a.1; WBGene00000149. [Q10651-1]
DR EnsemblMetazoa; C42D8.8b.1; C42D8.8b.1; WBGene00000149. [Q10651-2]
DR GeneID; 180783; -.
DR KEGG; cel:CELE_C42D8.8; -.
DR UCSC; C42D8.8a; c. elegans. [Q10651-1]
DR CTD; 180783; -.
DR WormBase; C42D8.8a; CE04209; WBGene00000149; apl-1. [Q10651-1]
DR WormBase; C42D8.8b; CE27845; WBGene00000149; apl-1. [Q10651-2]
DR eggNOG; KOG3540; Eukaryota.
DR GeneTree; ENSGT00530000063252; -.
DR InParanoid; Q10651; -.
DR OMA; HEKFIPM; -.
DR OrthoDB; 953529at2759; -.
DR PhylomeDB; Q10651; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-3000178; ECM proteoglycans.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-416476; G alpha (q) signalling events.
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR Reactome; R-CEL-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; Q10651; -.
DR PRO; PR:Q10651; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000149; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR Gene3D; 1.20.120.770; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.1490.140; -; 1.
DR Gene3D; 3.90.570.10; -; 1.
DR InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR InterPro; IPR008155; Amyloid_glyco.
DR InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR InterPro; IPR008154; Amyloid_glyco_extra.
DR InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR InterPro; IPR019543; APP_amyloid_C.
DR InterPro; IPR019744; APP_CUBD_CS.
DR InterPro; IPR036176; E2_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR23103; PTHR23103; 1.
DR Pfam; PF10515; APP_amyloid; 1.
DR Pfam; PF12924; APP_Cu_bd; 1.
DR Pfam; PF12925; APP_E2; 1.
DR Pfam; PF02177; APP_N; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR SMART; SM00006; A4_EXTRA; 1.
DR SUPFAM; SSF109843; SSF109843; 1.
DR SUPFAM; SSF56491; SSF56491; 1.
DR SUPFAM; SSF89811; SSF89811; 1.
DR PROSITE; PS00319; APP_CUBD; 1.
DR PROSITE; PS51869; APP_E1; 1.
DR PROSITE; PS51870; APP_E2; 1.
DR PROSITE; PS00320; APP_INTRA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amyloid; Developmental protein;
KW Differentiation; Disulfide bond; Endosome; Glycoprotein; Membrane;
KW Neurogenesis; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..686
FT /note="Amyloid-beta-like protein"
FT /evidence="ECO:0000305"
FT /id="PRO_0000000201"
FT TOPO_DOM 22..621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..686
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..197
FT /note="E1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DOMAIN 240..440
FT /note="E2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
FT REGION 32..125
FT /note="GFLD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 133..197
FT /note="CuBD subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT REGION 201..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 674..679
FT /note="YENPXY motif"
FT /evidence="ECO:0000250|UniProtKB:P05067"
FT COMPBIAS 210..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..573
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 252..255
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000269|PubMed:19906646"
FT BINDING 382
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000269|PubMed:19906646"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 76..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 101..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT DISULFID 135..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217,
FT ECO:0000269|PubMed:19906646, ECO:0000269|PubMed:24276282"
FT DISULFID 146..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217,
FT ECO:0000269|PubMed:19906646, ECO:0000269|PubMed:24276282"
FT DISULFID 160..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01217,
FT ECO:0000269|PubMed:19906646, ECO:0000269|PubMed:24276282"
FT VAR_SEQ 538..539
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_000017"
FT MUTAGEN 252
FT /note="N->A: Reduced heparin binding."
FT /evidence="ECO:0000269|PubMed:19906646"
FT MUTAGEN 254
FT /note="H->A: Reduced heparin binding."
FT /evidence="ECO:0000269|PubMed:19906646"
FT MUTAGEN 254
FT /note="H->P: Reduced heparin binding."
FT /evidence="ECO:0000269|PubMed:19906646"
FT MUTAGEN 348
FT /note="D->C: Results in destabilized protein structure;
FT when associated with C-368 and K-377."
FT /evidence="ECO:0000269|PubMed:19906646"
FT MUTAGEN 368
FT /note="S->C: Results in destabilized protein structure;
FT when associated with C-348 and K-377."
FT /evidence="ECO:0000269|PubMed:19906646"
FT MUTAGEN 374
FT /note="R->A: Reduced heparin binding; when associated with
FT A-378."
FT /evidence="ECO:0000269|PubMed:19906646"
FT MUTAGEN 377
FT /note="E->K: In yn32: Results in lethality and destabilized
FT protein structure."
FT /evidence="ECO:0000269|PubMed:17267616,
FT ECO:0000269|PubMed:19906646"
FT MUTAGEN 378
FT /note="K->A: Reduced heparin binding; when associated with
FT A-374."
FT /evidence="ECO:0000269|PubMed:19906646"
FT MUTAGEN 382
FT /note="H->A: Moderately reduced heparin binding."
FT /evidence="ECO:0000269|PubMed:19906646"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:2M05"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:2M05"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2M05"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:2M05"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:3K66"
FT HELIX 253..292
FT /evidence="ECO:0007829|PDB:3K66"
FT HELIX 294..358
FT /evidence="ECO:0007829|PDB:3K66"
FT HELIX 362..393
FT /evidence="ECO:0007829|PDB:3K66"
FT HELIX 395..399
FT /evidence="ECO:0007829|PDB:3K66"
FT HELIX 402..421
FT /evidence="ECO:0007829|PDB:3K66"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:3K66"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:3K66"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:3K6B"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:3K66"
SQ SEQUENCE 686 AA; 79435 MW; A0816858FDD48608 CRC64;
MTVGKLMIGL LIPILVATVY AEGSPAGSKR HEKFIPMVAF SCGYRNQYMT EEGSWKTDDE
RYATCFSGKL DILKYCRKAY PSMNITNIVE YSHEVSISDW CREEGSPCKW THSVRPYHCI
DGEFHSEALQ VPHDCQFSHV NSRDQCNDYQ HWKDEAGKQC KTKKSKGNKD MIVRSFAVLE
PCALDMFTGV EFVCCPNDQT NKTDVQKTKE DEDDDDDEDD AYEDDYSEES DEKDEEEPSS
QDPYFKIANW TNEHDDFKKA EMRMDEKHRK KVDKVMKEWG DLETRYNEQK AKDPKGAEKF
KSQMNARFQK TVSSLEEEHK RMRKEIEAVH EERVQAMLNE KKRDATHDYR QALATHVNKP
NKHSVLQSLK AYIRAEEKDR MHTLNRYRHL LKADSKEAAA YKPTVIHRLR YIDLRINGTL
AMLRDFPDLE KYVRPIAVTY WKDYRDEVSP DISVEDSELT PIIHDDEFSK NAKLDVKAPT
TTAKPVKETD NAKVLPTEAS DSEEEADEYY EDEDDEQVKK TPDMKKKVKV VDIKPKEIKV
TIEEEKKAPK LVETSVQTDD EDDDEDSSSS TSSESDEDED KNIKELRVDI EPIIDEPASF
YRHDKLIQSP EVERSASSVF QPYVLASAMF ITAICIIAFA ITNARRRRAM RGFIEVDVYT
PEERHVAGMQ VNGYENPTYS FFDSKA
