ACES_DROME
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 03-AUG-2022, entry version 203.
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}.
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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; 1DX4; X-ray; 2.70 A; A=39-623.
DR PDB; 1QO9; X-ray; 2.70 A; A=39-623.
DR PDB; 1QON; X-ray; 2.72 A; A=39-623.
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; 1DX4; -.
DR PDBsum; 1QO9; -.
DR PDBsum; 1QON; -.
DR PDBsum; 6XYS; -.
DR PDBsum; 6XYU; -.
DR PDBsum; 6XYY; -.
DR AlphaFoldDB; P07140; -.
DR SMR; P07140; -.
DR BioGRID; 66709; 9.
DR STRING; 7227.FBpp0289713; -.
DR BindingDB; P07140; -.
DR ChEMBL; CHEMBL2242744; -.
DR ESTHER; drome-ACHE; AChE.
DR MEROPS; S09.980; -.
DR GlyGen; P07140; 4 sites.
DR iPTMnet; P07140; -.
DR PaxDb; P07140; -.
DR GeneID; 41625; -.
DR KEGG; dme:Dmel_CG17907; -.
DR CTD; 1636; -.
DR FlyBase; FBgn0000024; Ace.
DR VEuPathDB; VectorBase:FBgn0000024; -.
DR eggNOG; KOG4389; Eukaryota.
DR InParanoid; P07140; -.
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 Genevisible; P07140; DM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
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; -; 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 Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00880; ACHEINSECT.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
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 HELIX 392..394
FT /evidence="ECO:0007829|PDB:1DX4"
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:1DX4"
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
