ID   ACES_NAJOX              Reviewed;         181 AA.
AC   Q7LZG1; Q7LZ27;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Fragments;
GN   Name=ACHE;
OS   Naja oxiana (Central Asian cobra) (Oxus cobra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX   NCBI_TaxID=8657;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-44 AND 53-181.
RC   TISSUE=Venom;
RX   PubMed=2340076; DOI=10.1007/bf01024984;
RA   Weise C., Kreienkamp H.J., Raba R., Aaviksaar A., Hucho F.;
RT   "The active site and partial sequence of cobra venom
RT   acetylcholinesterase.";
RL   J. Protein Chem. 9:53-57(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 45-52.
RC   TISSUE=Venom;
RX   PubMed=2068091; DOI=10.1073/pnas.88.14.6117;
RA   Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F.;
RT   "Anionic subsites of the catalytic center of acetylcholinesterase from
RT   Torpedo and from cobra venom.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991).
CC   -!- FUNCTION: In venom, its toxic role is unclear: it could result in less
CC       musculatory control by rapidly hydrolyzing acetylcholine, or that it
CC       works synergistically with alkaline phosphatase (ALP) in paralyzing
CC       prey through hypotension. In muscle, it terminates signal transduction
CC       at the neuromuscular junction by rapid hydrolysis of the acetylcholine
CC       released into the synaptic cleft. In liver, its function is unclear: it
CC       could serve as a safeguard against any diffusion of acetylcholine from
CC       synapses into the circulation.
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         Evidence={ECO:0000250|UniProtKB:Q92035};
CC   -!- SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. Is also probably
CC       expressed by liver and muscle.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   PIR; A39022; A39022.
DR   PIR; A41117; A41117.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   Pfam; PF00135; COesterase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Hydrolase; Membrane;
KW   Neurotransmitter degradation; Secreted; Serine esterase; Synapse; Toxin.
FT   CHAIN           <1..>181
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000408518"
FT   REGION          160..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        76
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        132
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   NON_CONS        35..36
FT                   /evidence="ECO:0000305"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000305"
FT   NON_CONS        52..53
FT                   /evidence="ECO:0000305"
FT   NON_CONS        61..62
FT                   /evidence="ECO:0000305"
FT   NON_CONS        68..69
FT                   /evidence="ECO:0000305"
FT   NON_CONS        91..92
FT                   /evidence="ECO:0000305"
FT   NON_CONS        125..126
FT                   /evidence="ECO:0000305"
FT   NON_CONS        135..136
FT                   /evidence="ECO:0000305"
FT   NON_CONS        151..152
FT                   /evidence="ECO:0000305"
FT   NON_CONS        158..159
FT                   /evidence="ECO:0000305"
FT   NON_CONS        168..169
FT                   /evidence="ECO:0000305"
FT   NON_CONS        172..173
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         181
SQ   SEQUENCE   181 AA;  19255 MW;  19AB68C1423C4BD2 CRC64;
     SELKVATQTG FVRGLSLPVL AGHVSAHLGV PFAEPFLRPE PVKPGAEMWN PNLNIWVPSG
     RVGAFXFLTV TLFGESAGAA SVGMXLLSTQ RAILQSGAPN APWAQVQPAE SRFPFVPVID
     GEFFPLGVNK DEGSFGVPGF SKXXESLINQ AVPHANDIYT DWQDQDNGGL PLTGNPTXPH
     N