ID   ACES_TORMA              Reviewed;         590 AA.
AC   P07692;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   13-SEP-2023, entry version 129.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
GN   Name=ache;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Electric organ;
RX   PubMed=2820709; DOI=10.1002/j.1460-2075.1987.tb02445.x;
RA   Sikorav J.-L., Krejci E., Massoulie J.;
RT   "cDNA sequences of Torpedo marmorata acetylcholinesterase: primary
RT   structure of the precursor of a catalytic subunit; existence of multiple
RT   5'-untranslated regions.";
RL   EMBO J. 6:1865-1873(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-47.
RX   PubMed=3792544; DOI=10.1016/0014-5793(86)81112-7;
RA   Bon S., Chang J.Y., Strosberg A.D.;
RT   "Identical N-terminal peptide sequences of asymmetric forms and of low-
RT   salt-soluble and detergent-soluble amphiphilic dimers of Torpedo
RT   acetylcholinesterase. Comparison with bovine acetylcholinesterase.";
RL   FEBS Lett. 209:206-212(1986).
RN   [3]
RP   ALTERNATIVE SPLICING.
RC   TISSUE=Electric organ;
RX   PubMed=3181125; DOI=10.1002/j.1460-2075.1988.tb03161.x;
RA   Sikorav J.-L., Duval N., Anselmet A., Bon S., Krejci E., Legay C.,
RA   Osterlund M., Reimund B., Massoulie J.;
RT   "Complex alternative splicing of acetylcholinesterase transcripts in
RT   Torpedo electric organ; primary structure of the precursor of the
RT   glycolipid-anchored dimeric form.";
RL   EMBO J. 7:2983-2993(1988).
RN   [4]
RP   SUBUNITS INTERACTION.
RC   TISSUE=Electric organ;
RX   PubMed=1380451; DOI=10.1002/j.1460-2075.1992.tb05403.x;
RA   Duval N., Krejci E., Grassi J., Coussen F., Massoulie J., Bon S.;
RT   "Molecular architecture of acetylcholinesterase collagen-tailed forms;
RT   construction of a glycolipid-tailed tetramer.";
RL   EMBO J. 11:3255-3261(1992).
RN   [5]
RP   SUBUNITS INTERACTION, AND SEQUENCE REVISION TO 421.
RX   PubMed=1639848; DOI=10.1083/jcb.118.3.641;
RA   Duval N., Massoulie J., Bon S.;
RT   "H and T subunits of acetylcholinesterase from Torpedo, expressed in COS
RT   cells, generate all types of globular forms.";
RL   J. Cell Biol. 118:641-653(1992).
CC   -!- FUNCTION: Terminates signal transduction at the neuromuscular junction
CC       by rapid hydrolysis of the acetylcholine released into the synaptic
CC       cleft. May be involved in cell-cell interactions.
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: Isoform H form is a homodimer; the asymmetric form is a
CC       disulfide-bonded oligomer composed of a collagenic subunit (Q) and a
CC       variable number of T catalytic subunits. {ECO:0000269|PubMed:1380451,
CC       ECO:0000269|PubMed:1639848}.
CC   -!- SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-
CC       anchor. Synapse.
CC   -!- SUBCELLULAR LOCATION: [Isoform T]: Cell membrane; Peripheral membrane
CC       protein. Synapse. Note=Attached to the membrane through disulfide
CC       linkage with the collagenic subunit, itself bound to the membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=H; Synonyms=Globular;
CC         IsoId=P07692-1; Sequence=Displayed;
CC       Name=T;
CC         IsoId=P07692-2; Sequence=VSP_001461;
CC       Name=3;
CC         IsoId=P07692-3; Sequence=VSP_001462;
CC   -!- TISSUE SPECIFICITY: Found in the synapses and to a lower extent in
CC       extrajunctional areas of muscle and nerve, and on erythrocyte
CC       membranes.
CC   -!- PTM: An interchain disulfide bond is present in what becomes position
CC       596 of the T isoform. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform H]: GPI-anchored form.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; X05497; CAA29047.1; -; mRNA.
DR   EMBL; X13172; CAA31570.1; -; mRNA.
DR   EMBL; X13174; CAA31572.1; -; mRNA.
DR   EMBL; X13173; CAA31571.1; -; mRNA.
DR   PIR; A38868; A38868.
DR   PIR; S01293; S01293.
DR   AlphaFoldDB; P07692; -.
DR   SMR; P07692; -.
DR   BindingDB; P07692; -.
DR   ESTHER; torma-ACHE; ACHE.
DR   MEROPS; S09.980; -.
DR   GlyCosmos; P07692; 4 sites, No reported glycans.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
DR   GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IEA:InterPro.
DR   CDD; cd00312; Esterase_lipase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000908; Acylcholinesterase_fish/snake.
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; PF00135; COesterase; 1.
DR   PRINTS; PR00879; ACHEFISH.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Neurotransmitter degradation; Serine esterase; Signal; Synapse.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:3792544"
FT   CHAIN           25..567
FT                   /note="Acetylcholinesterase"
FT                   /id="PRO_0000008597"
FT   PROPEP          568..590
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000008598"
FT   ACT_SITE        224
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        351
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        464
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   LIPID           567
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        91..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        278..289
FT                   /evidence="ECO:0000250"
FT   DISULFID        426..545
FT                   /evidence="ECO:0000250"
FT   DISULFID        561
FT                   /note="Interchain"
FT   VAR_SEQ         560..590
FT                   /note="ACDGELSSSGTSSSKGIIFYVLFSILYLIFY -> GNVFAFHMQKVRTPAKT
FT                   YHFGVIVAHLLLLSLPTASDVPRLASSKWWAHSDPLCSRRCWESWGRIL (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001462"
FT   VAR_SEQ         560..590
FT                   /note="ACDGELSSSGTSSSKGIIFYVLFSILYLIFY -> ETIDEAERQWKTEFHRW
FT                   SSYMMHWKNQFDQYSRHENCAEL (in isoform T)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001461"
FT   CONFLICT        41
FT                   /note="R -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   590 AA;  66744 MW;  73FAC284C9784F25 CRC64;
     MREMNLLVTS SLGVLLHLVV LCQADDDSEL LVNTKSGKVM RTRIPVLSSH ISAFLGIPFA
     EPPVGNMRFR RPEPKKPWSG VWNASTYPNN CQQYVDEQFP GFPGSEMWNP NREMSEDCLY
     LNIWVPSPRP KSATVMLWIY GGGFYSGSST LDVYNGKYLA YTEEVVLVSL SYRVGAFGFL
     ALHGSQEAPG NMGLLDQRMA LQWVHDNIQF FGGDPKTVTL FGESAGRASV GMHILSPGSR
     DLFRRAILQS GSPNCPWASV SVAEGRRRAV ELRRNLNCNL NSDEDLIQCL REKKPQELID
     VEWNVLPFDS IFRFSFVPVI DGEFFPTSLE SMLNAGNFKK TQILLGVNKD EGSFFLLYGA
     PGFSKDSESK ISREDFMSGV KLSVPHANDL GLDAVTLQYT DWMDDNNGIK NRDGLDDIVG
     DHNVICPLMH FVNKYTKFGN GTYLYFFNHR ASNLVWPEWM GVIHGYEIEF VFGLPLVKEL
     NYTAEEEALS RRIMHYWATF AKTGNPNEPH SQESKWPLFT TKEQKFIDLN TEPIKVHQRL
     RVQMCVFWNQ FLPKLLNATA CDGELSSSGT SSSKGIIFYV LFSILYLIFY
//