ID ACES_DROME Reviewed; 649 AA. AC P07140; Q9VFY0; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 24-JAN-2024, entry version 211. DE RecName: Full=Acetylcholinesterase; DE Short=AChE; DE EC=3.1.1.7; DE Contains: DE RecName: Full=Acetylcholinesterase 16 kDa subunit; DE Contains: DE RecName: Full=Acetylcholinesterase 55 kDa subunit; DE Flags: Precursor; GN Name=Ace; ORFNames=CG17907; 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]. RX PubMed=3024971; DOI=10.1002/j.1460-2075.1986.tb04591.x; RA Hall L.M.C., Spierer P.; RT "The Ace locus of Drosophila melanogaster: structural gene for RT acetylcholinesterase with an unusual 5' leader."; RL EMBO J. 5:2949-2954(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Canton-S, MH19, and Oregon-R; TISSUE=Embryo, and Pupae; RX PubMed=2511327; DOI=10.1016/0022-2836(89)90287-8; RA Fournier D., Karch F., Bride J.-M., Hall L.M.C., Berge J.-B., Spierer P.; RT "Drosophila melanogaster acetylcholinesterase gene. Structure, evolution RT and mutations."; RL J. Mol. Biol. 210:15-22(1989). RN [3] 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 [4] RP GENOME REANNOTATION. 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 [5] RP SUBUNIT. RX PubMed=3139459; DOI=10.1016/0014-5793(88)80507-6; RA Fournier D., Bride J.-M., Karsch F., Berge J.-B.; RT "Acetylcholinesterase from Drosophila melanogaster. Identification of two RT subunits encoded by the same gene."; RL FEBS Lett. 238:333-337(1988). RN [6] RP PROTEOLYTIC PROCESSING, GPI-ANCHOR, AND PROTEIN SEQUENCE OF 40-43. RX PubMed=2975507; DOI=10.1021/bi00417a038; RA Haas R., Marshall T.L., Rosenberry T.L.; RT "Drosophila acetylcholinesterase: demonstration of a glycoinositol RT phospholipid anchor and an endogenous proteolytic cleavage."; RL Biochemistry 27:6453-6457(1988). RN [7] RP GPI-ANCHOR. RX PubMed=2831298; DOI=10.1111/j.1471-4159.1988.tb10587.x; RA Fournier D., Berge J.-B., Cardoso de Almeida M.L., Bordier C.; RT "Acetylcholinesterases from Musca domestica and Drosophila melanogaster RT brain are linked to membranes by a glycophospholipid anchor sensitive to an RT endogenous phospholipase."; RL J. Neurochem. 50:1158-1163(1988). RN [8] RP GLYCOSYLATION AT ASN-126; ASN-174; ASN-331 AND ASN-531, LACK OF RP GLYCOSYLATION AT ASN-569, INTERCHAIN AT CYS-615, AND MUTAGENESIS OF RP ASN-126; ASN-174; CYS-328; ASN-331; ASN-531; ASN-569 AND CYS-615. RX PubMed=1730712; DOI=10.1016/s0021-9258(18)46001-2; RA Mutero A., Fournier D.; RT "Post-translational modifications of Drosophila acetylcholinesterase. In RT vitro mutagenesis and expression in Xenopus oocytes."; RL J. Biol. Chem. 267:1695-1700(1992). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 41-623 IN COMPLEX WITH INHIBITOR. RX PubMed=10892800; DOI=10.1110/ps.9.6.1063; RA Harel M., Kryger G., Rosenberry T.L., Mallender W.D., Lewis T., RA Fletcher R.J., Guss J.M., Silman I., Sussman J.L.; RT "Three-dimensional structures of Drosophila melanogaster RT acetylcholinesterase and of its complexes with two potent inhibitors."; RL Protein Sci. 9:1063-1072(2000). CC -!- FUNCTION: Rapidly hydrolyzes choline released into the synapse. It can CC hydrolyze butyrylthiocholine. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetylcholine + H2O = acetate + choline + H(+); CC Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7; CC -!- SUBUNIT: Homodimer; disulfide-linked. The active unit is formed by non- CC covalent association of the 55 kDa and 16 kDa subunits. CC {ECO:0000269|PubMed:10892800, ECO:0000269|PubMed:3139459}. CC -!- SUBCELLULAR LOCATION: Synapse. Cell membrane; Lipid-anchor, GPI-anchor. CC Note=Attached to the membrane of the neuronal cholinergic synapses by a CC GPI-anchor. CC -!- PTM: Proteolytic cleavage into the 16 kDa subunit and the 55 kDa CC subunits originates from the hydrophilic peptide, aa 148-180, and is CC associated with excretion out of the cell. CC {ECO:0000269|PubMed:2975507}. CC -!- PTM: Neither N-glycosylation nor dimerization is required for enzyme CC activity or substrate specificity, but protects the protein against CC proteolytic digestion. {ECO:0000269|PubMed:1730712}. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X05893; CAA29326.1; -; mRNA. DR EMBL; AE014297; AAF54915.1; -; Genomic_DNA. DR PIR; A25363; A25363. DR RefSeq; NP_001163600.1; NM_001170129.2. DR RefSeq; NP_476953.1; NM_057605.5. DR PDB; 6XYS; X-ray; 2.46 A; A=39-619. DR PDB; 6XYU; X-ray; 2.51 A; A=39-619. DR PDB; 6XYY; X-ray; 2.70 A; A=39-619. DR PDBsum; 6XYS; -. DR PDBsum; 6XYU; -. DR PDBsum; 6XYY; -. DR AlphaFoldDB; P07140; -. DR SMR; P07140; -. DR BioGRID; 66709; 9. DR STRING; 7227.FBpp0082248; -. DR BindingDB; P07140; -. DR ChEMBL; CHEMBL2242744; -. DR ESTHER; drome-ACHE; ACHE. DR MEROPS; S09.980; -. DR GlyCosmos; P07140; 4 sites, No reported glycans. DR GlyGen; P07140; 4 sites. DR iPTMnet; P07140; -. DR PaxDb; 7227-FBpp0289713; -. DR GeneID; 41625; -. DR KEGG; dme:Dmel_CG17907; -. DR AGR; FB:FBgn0000024; -. DR CTD; 1636; -. DR FlyBase; FBgn0000024; Ace. DR VEuPathDB; VectorBase:FBgn0000024; -. DR eggNOG; KOG4389; Eukaryota. DR InParanoid; P07140; -. DR OrthoDB; 4386at2759; -. DR PhylomeDB; P07140; -. DR BRENDA; 3.1.1.7; 1994. DR Reactome; R-DME-112311; Neurotransmitter clearance. DR Reactome; R-DME-1483191; Synthesis of PC. DR Reactome; R-DME-9749641; Aspirin ADME. DR BioGRID-ORCS; 41625; 0 hits in 3 CRISPR screens. DR EvolutionaryTrace; P07140; -. DR GenomeRNAi; 41625; -. DR PRO; PR:P07140; -. DR Proteomes; UP000000803; Chromosome 3R. DR ExpressionAtlas; P07140; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. DR GO; GO:0043083; C:synaptic cleft; IEA:GOC. DR GO; GO:0003990; F:acetylcholinesterase activity; IDA:FlyBase. DR GO; GO:0004104; F:cholinesterase activity; IDA:FlyBase. DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA. DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase. DR GO; GO:0043199; F:sulfate binding; IDA:CAFA. DR GO; GO:0006581; P:acetylcholine catabolic process; IDA:FlyBase. DR GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IEA:InterPro. DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase. DR GO; GO:0042426; P:choline catabolic process; IDA:FlyBase. DR GO; GO:0019695; P:choline metabolic process; IBA:GO_Central. DR DisProt; DP00346; -. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001445; Acylcholinesterase_insect. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019826; Carboxylesterase_B_AS. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR InterPro; IPR000997; Cholinesterase. DR PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1. DR PANTHER; PTHR43918:SF13; ACETYLCHOLINESTERASE; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR00880; ACHEINSECT. DR PRINTS; PR00878; CHOLNESTRASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. DR Genevisible; P07140; DM. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond; KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; KW Neurotransmitter degradation; Reference proteome; Serine esterase; Signal; KW Synapse. FT SIGNAL 1..38 FT CHAIN 39..619 FT /note="Acetylcholinesterase" FT /id="PRO_0000008603" FT CHAIN 39..? FT /note="Acetylcholinesterase 16 kDa subunit" FT /id="PRO_0000008604" FT CHAIN ?..619 FT /note="Acetylcholinesterase 55 kDa subunit" FT /id="PRO_0000008605" FT PROPEP 620..649 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000008606" FT ACT_SITE 276 FT /note="Acyl-ester intermediate" FT ACT_SITE 405 FT /note="Charge relay system" FT ACT_SITE 518 FT /note="Charge relay system" FT SITE 569 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:1730712" FT LIPID 619 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000255" FT CARBOHYD 126 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1730712" FT CARBOHYD 174 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1730712" FT CARBOHYD 331 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1730712" FT CARBOHYD 531 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1730712" FT DISULFID 104..131 FT DISULFID 330..345 FT DISULFID 480..598 FT DISULFID 615 FT /note="Interchain" FT MUTAGEN 126 FT /note="N->D: Decrease in apparent molecular weight of 16 FT kDa subunit." FT /evidence="ECO:0000269|PubMed:1730712" FT MUTAGEN 174 FT /note="N->S: Decrease in apparent molecular weight of 55 FT kDa subunit. Decrease in apparent molecular weight of 55 FT kDa subunit equivalent to the sum of decreases observed FT with S-174; D-133 and D-331; when associated with D-331 and FT D-531." FT /evidence="ECO:0000269|PubMed:1730712" FT MUTAGEN 328 FT /note="C->V: No effect on apparent molecular weight." FT /evidence="ECO:0000269|PubMed:1730712" FT MUTAGEN 331 FT /note="N->D: Decrease in apparent molecular weight of the FT 55 kDa subunit. Decrease in apparent molecular weight of 55 FT kDa subunit equivalent to the sum of individual decreases FT observed with S-174; D-331 and D-531; when associated with FT S-174 and D-531." FT /evidence="ECO:0000269|PubMed:1730712" FT MUTAGEN 531 FT /note="N->D: Decrease in apparent molecular weight of the FT 55 kDa subunit. Decrease in apparent molecular weight of 55 FT kDa subunit equivalent to the sum of individual decreases FT observed with S-174; D-331 and D-531; when associated with FT S-174 and D-331." FT /evidence="ECO:0000269|PubMed:1730712" FT MUTAGEN 569 FT /note="N->D: No change in apparent molecular weight of the FT 55 kDa subunit." FT /evidence="ECO:0000269|PubMed:1730712" FT MUTAGEN 615 FT /note="C->R: Formation of 75 kDa monomer." FT /evidence="ECO:0000269|PubMed:1730712" FT CONFLICT 99 FT /note="G -> R (in Ref. 3; AAF54915)" FT /evidence="ECO:0000305" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 50..53 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 55..59 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 62..71 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 116..119 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 133..139 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 179..185 FT /evidence="ECO:0007829|PDB:6XYS" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:6XYU" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 203..209 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 212..216 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 222..225 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 234..239 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 244..258 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 261..263 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 265..275 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 277..287 FT /evidence="ECO:0007829|PDB:6XYS" FT TURN 289..293 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 297..302 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 308..310 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 314..327 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:6XYS" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 341..347 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 351..357 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 358..361 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 376..379 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 383..389 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 396..402 FT /evidence="ECO:0007829|PDB:6XYS" FT TURN 403..406 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 407..413 FT /evidence="ECO:0007829|PDB:6XYS" FT TURN 414..417 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 420..422 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 429..438 FT /evidence="ECO:0007829|PDB:6XYS" FT TURN 439..441 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 444..453 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 457..459 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 463..477 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 479..491 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 495..501 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 512..514 FT /evidence="ECO:0007829|PDB:6XYS" FT TURN 518..521 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 522..525 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 528..530 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 538..557 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 572..574 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 577..580 FT /evidence="ECO:0007829|PDB:6XYS" FT STRAND 584..586 FT /evidence="ECO:0007829|PDB:6XYY" FT STRAND 588..590 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 592..602 FT /evidence="ECO:0007829|PDB:6XYS" FT HELIX 604..608 FT /evidence="ECO:0007829|PDB:6XYS" SQ SEQUENCE 649 AA; 71785 MW; 5863C73FF99028C0 CRC64; MAISCRQSRV LPMSLPLPLT IPLPLVLVLS LHLSGVCGVI DRLVVQTSSG PVRGRSVTVQ GREVHVYTGI PYAKPPVEDL RFRKPVPAEP WHGVLDATGL SATCVQERYE YFPGFSGEEI WNPNTNVSED CLYINVWAPA KARLRHGRGA NGGEHPNGKQ ADTDHLIHNG NPQNTTNGLP ILIWIYGGGF MTGSATLDIY NADIMAAVGN VIVASFQYRV GAFGFLHLAP EMPSEFAEEA PGNVGLWDQA LAIRWLKDNA HAFGGNPEWM TLFGESAGSS SVNAQLMSPV TRGLVKRGMM QSGTMNAPWS HMTSEKAVEI GKALINDCNC NASMLKTNPA HVMSCMRSVD AKTISVQQWN SYSGILSFPS APTIDGAFLP ADPMTLMKTA DLKDYDILMG NVRDEGTYFL LYDFIDYFDK DDATALPRDK YLEIMNNIFG KATQAEREAI IFQYTSWEGN PGYQNQQQIG RAVGDHFFTC PTNEYAQALA ERGASVHYYY FTHRTSTSLW GEWMGVLHGD EIEYFFGQPL NNSLQYRPVE RELGKRMLSA VIEFAKTGNP AQDGEEWPNF SKEDPVYYIF STDDKIEKLA RGPLAARCSF WNDYLPKVRS WAGTCDGDSG SASISPRLQL LGIAALIYIC AALRTKRVF //