ACES_TORMA
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 03-AUG-2022, entry version 126.
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 GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.50.1820; -; 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 Pfam; PF00135; COesterase; 1.
DR PRINTS; PR00879; ACHEFISH.
DR PRINTS; PR00878; CHOLNESTRASE.
DR SUPFAM; SSF53474; SSF53474; 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
