ACES_CHICK
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 03-AUG-2022, entry version 115.
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 ChEMBL; CHEMBL3227914; -.
DR DrugCentral; P36196; -.
DR ESTHER; chick-ACHE; AChE.
DR VEuPathDB; HostDB:geneid_396388; -.
DR InParanoid; P36196; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P36196; -.
DR PRO; PR:P36196; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0052689; F:carboxylic ester hydrolase 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; -; 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 Pfam; PF08674; AChE_tetra; 1.
DR Pfam; PF00135; COesterase; 2.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; SSF53474; 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
