ID   ACES_CHICK              Reviewed;         767 AA.
AC   P36196;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
GN   Name=ACHE;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=8049273; DOI=10.1016/0167-4781(94)90204-6;
RA   Randall W.R., Rimer M., Gough N.R.;
RT   "Cloning and analysis of chicken acetylcholinesterase transcripts from
RT   muscle and brain.";
RL   Biochim. Biophys. Acta 1218:453-456(1994).
CC   -!- FUNCTION: Terminates signal transduction at the neuromuscular junction
CC       by rapid hydrolysis of the acetylcholine released into the synaptic
CC       cleft.
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: Oligomer composed of disulfide-linked homodimers.
CC   -!- SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; U03472; AAA60456.1; -; mRNA.
DR   PIR; S47639; S47639.
DR   AlphaFoldDB; P36196; -.
DR   SMR; P36196; -.
DR   STRING; 9031.ENSGALP00000074034; -.
DR   ChEMBL; CHEMBL3227914; -.
DR   DrugCentral; P36196; -.
DR   ESTHER; chick-ACHE; ACHE.
DR   GlyCosmos; P36196; 4 sites, No reported glycans.
DR   VEuPathDB; HostDB:geneid_396388; -.
DR   InParanoid; P36196; -.
DR   PhylomeDB; P36196; -.
DR   PRO; PR:P36196; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IBA:GO_Central.
DR   GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR   GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
DR   GO; GO:0010842; P:retina layer formation; IMP:AgBase.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR014788; AChE_tetra.
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:SF11; ACETYLCHOLINESTERASE; 1.
DR   Pfam; PF08674; AChE_tetra; 1.
DR   Pfam; PF00135; COesterase; 2.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
KW   Neurotransmitter degradation; Reference proteome; Secreted;
KW   Serine esterase; Signal; Synapse.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..767
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000008591"
FT   REGION          401..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        227
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        520
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        633
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        536
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        650
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        725
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        281..292
FT                   /evidence="ECO:0000250"
FT   DISULFID        595..713
FT                   /evidence="ECO:0000250"
FT   DISULFID        764
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   767 AA;  83020 MW;  B1B3DF29C31F6062 CRC64;
     MAPLFLLLLL LLSPSPTSAH RFAYSAPNRP EVRTTTGSVR GLLIPAGPSG STAAAFLGIP
     FAVPPLGPLR FRPPLPIPTP WTGIRDADSQ PFACYQMVDT TFPGFQGSEM WNPNREMSED
     CLYLNVWTQK GDPTEPPVLV WIYGGGFTGG SVSLDVYDGR YLAAAEEAVV VSMNYRVGSL
     GFLALAGHRD APGNVGLWDQ RLALQWVRDN AEAFGGDPDL ITLFGESAGA ASVGFHLLSP
     HSKGLFRRAV LQSGSPNGPW ATIGAAEGRR RAAALGRAVG CPYGNETEFL GCLRGKEAAD
     VLEGEGVVMP PQSVFRFAFV PVVDGDFVVD SPDVALWGDY GVKGGEGGHG VEGGDGGYGV
     KGGDGVKGGY GGGYGARGVR EGDGDGGYGV KEGLREGYGV KEGYGVEGDG ANAYGARVPP
     RPHRDETPPD AYGAKGSADA YGAKAAPRPH RDETSPDAYG AKMPPRPHRD EASPDTYGAK
     MPPRPHRDET SPDAYGAKMP PRPHRAGGEV EVLLGAVRVE GSYFLVYGVP GFGKDNESLI
     SREEFLGGVR MGVPQATELA AEAVVLHYTD WLDADNPVKN REALDDIVGD HNVVCPLMAF
     AQRWAQRGGK VYAYLFDHRS STLLWPSWMG VPHGYEIEFV FGLPLEPRNN YTREEVELSR
     RIMRYWGNFA RTGDPNGGVG GPRWPPYTPS GQRYAHLNAR PLSVGHGLRT QICAFWTRFL
     PKLLNATGPP EDAEREWRLE FHRWSSYMGR WRTQFEHYSR QQPCATL
//