ID   ACES_RABIT              Reviewed;         584 AA.
AC   Q29499;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor; Fragment;
GN   Name=ACHE;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=95010096; PubMed=7925428;
RX   DOI=10.1111/j.1432-1033.1994.00115.x;
RA   Jbilo O., L'Hermite Y., Talesa V., Toutant J.-P., Chatonnet A.;
RT   "Acetylcholinesterase and butyrylcholinesterase expression in adult
RT   rabbit tissues and during development.";
RL   Eur. J. Biochem. 225:115-124(1994).
CC   -!- FUNCTION: Terminates signal transduction at the neuromuscular
CC       junction by rapid hydrolysis of the acetylcholine released into
CC       the synaptic cleft.
CC   -!- CATALYTIC ACTIVITY: Acetylcholine + H(2)O = choline + acetate.
CC   -!- SUBUNIT: Homotetramer; composed of disulfide-linked homodimers.
CC       Interacts with PRIMA1. The interaction with PRIMA1 is required to
CC       anchor it to the basal lamina of cells and organize into tetramers
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse. Secreted. Cell
CC       membrane; Peripheral membrane protein (By similarity).
CC   -!- MISCELLANEOUS: Synapses usually contain asymmetric molecules of
CC       cholinesterase, with a collagen-like part disulfide-bonded to the
CC       catalytic part. A different, globular type of cholinesterase
CC       occurs on the outer surfaces of cell membranes, including those of
CC       erythrocytes.
CC   -!- MISCELLANEOUS: This is the catalytic subunit of an asymmetric or
CC       soluble form of ACHE.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U05036; AAA53235.1; -; mRNA.
DR   PIR; S48724; S48724.
DR   UniGene; Ocu.2012; -.
DR   HSSP; P22303; 1F8U.
DR   MEROPS; S09.979; -.
DR   HOVERGEN; Q29499; -.
DR   BRENDA; 3.1.1.7; 255.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IEA:EC.
DR   GO; GO:0004104; F:cholinesterase activity; IEA:InterPro.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
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; PTHR11559; CarbesteraseB; 1.
DR   Pfam; PF08674; AChE_tetra; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW   Membrane; Neurotransmitter degradation; Secreted; Serine esterase;
KW   Signal; Synapse.
FT   SIGNAL       <1      1       Potential.
FT   CHAIN         2    584       Acetylcholinesterase.
FT                                /FTId=PRO_0000008589.
FT   ACT_SITE    204    204       Acyl-ester intermediate (By similarity).
FT   ACT_SITE    335    335       Charge relay system (By similarity).
FT   ACT_SITE    448    448       Charge relay system (By similarity).
FT   CARBOHYD    266    266       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    351    351       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    465    465       N-linked (GlcNAc...) (Potential).
FT   DISULFID     70     97       By similarity.
FT   DISULFID    258    273       By similarity.
FT   DISULFID    410    530       By similarity.
FT   DISULFID    581    581       Interchain (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   584 AA;  64630 MW;  2AE157F3063649FE CRC64;
     AEGREDPELL VTVRGGRLRG LRLKAPGGPV SAFLGIPFEE PPVGPRRFLP PEPKRPWAGV
     LDATAFQSVC YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPT SPTPVLVWIY
     GGGFYSGASS LDVYYGRFLV QAEGTVLVAM NYRVGAFGFT CLPGSREAPG NVGLLDQRLA
     LQWVQENVAA FGGDPASVTL FGESAGAASV GLHLLSPPSR GLFHRAVLQS GAPNGPWATV
     GVGEARRRAT LLARLVVCPP GGAGGNDTEL VACLRTRPAQ DLVDHEWRVL PQESIFRFSF
     VPVVDGDFLS DTPEALINAG DFQGLQVLVG VVKDEGTYFL VYGAPGFSKD NESFISRAQF
     LAGVRVGVPQ ASDLAAEAVV LHYTDWLHPE DPARLRDALS DVVGDHNVVC PVAQLAGRLA
     AQGARVYAYV FEHRASTLSW PLWMGVPHGY EIEFIFGLPL EPSLNYTEEE RIFAQRLMRY
     WANFARTGDP NEPRDAKAPQ WPPYTAGAQQ YVSLNLRPLE VRRGLRAQAC AFWNRFLPKL
     LSATDTLDEA ERQWKAEFHR WSSYMVHWKN QFDHYSKQDR CSDL
//