ACES_RAT
ID ACES_RAT Reviewed; 614 AA.
AC P37136;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE;
DE EC=3.1.1.7 {ECO:0000269|PubMed:8417155};
DE Flags: Precursor;
GN Name=Ache;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM T), AND SUBUNIT.
RX PubMed=8417155; DOI=10.1111/j.1471-4159.1993.tb05856.x;
RA Legay C., Bon S., Vernier P., Coussen F., Massoulie J.;
RT "Cloning and expression of a rat acetylcholinesterase subunit: generation
RT of multiple molecular forms and complementarity with a Torpedo collagenic
RT subunit.";
RL J. Neurochem. 60:337-346(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H AND R).
RX PubMed=8417973; DOI=10.1016/0014-5793(93)81155-s;
RA Legay C., Bon S., Massoulie J.;
RT "Expression of a cDNA encoding the glycolipid-anchored form of rat
RT acetylcholinesterase.";
RL FEBS Lett. 315:163-166(1993).
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: [Isoform T]:
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:0000269|PubMed:8417155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17562;
CC Evidence={ECO:0000305|PubMed:8417155};
CC -!- SUBUNIT: Homotetramer; composed of disulfide-linked homodimers.
CC Catalytic forms H (GPI-anchor dimer) and T (asymmetric collagen-
CC tailed), which differ in their C-terminus, account for all types of
CC known ACHE forms (Probable). Interacts with PRIMA1. The interaction
CC with PRIMA1 is required to anchor it to the basal lamina of cells and
CC organize into tetramers (By similarity). {ECO:0000250,
CC ECO:0000305|PubMed:8417155}.
CC -!- SUBCELLULAR LOCATION: Synapse. Secreted. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-
CC anchor; Extracellular side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=T {ECO:0000303|PubMed:8417155};
CC IsoId=P37136-1; Sequence=Displayed;
CC Name=H {ECO:0000303|PubMed:8417155};
CC IsoId=P37136-2; Sequence=VSP_001458;
CC Name=R;
CC IsoId=P37136-3; Sequence=VSP_001459;
CC -!- TISSUE SPECIFICITY: Has been found in central nervous system and muscle
CC (PubMed:8417155). Found in embryonic liver and spleen but not in adult
CC liver (PubMed:8417155). {ECO:0000269|PubMed:8417155}.
CC -!- MISCELLANEOUS: [Isoform R]: May be not functional. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; S50879; AAB24586.1; -; mRNA.
DR EMBL; X70140; CAA49717.1; -; mRNA.
DR EMBL; X70141; CAA49718.1; -; mRNA.
DR PIR; JH0811; JH0811.
DR RefSeq; NP_742006.1; NM_172009.1. [P37136-1]
DR AlphaFoldDB; P37136; -.
DR SMR; P37136; -.
DR STRING; 10116.ENSRNOP00000064185; -.
DR BindingDB; P37136; -.
DR ChEMBL; CHEMBL3199; -.
DR DrugCentral; P37136; -.
DR ESTHER; ratno-ACHE; AChE.
DR MEROPS; S09.979; -.
DR GlyGen; P37136; 3 sites.
DR iPTMnet; P37136; -.
DR PhosphoSitePlus; P37136; -.
DR PRIDE; P37136; -.
DR GeneID; 83817; -.
DR KEGG; rno:83817; -.
DR CTD; 43; -.
DR RGD; 69313; Ache.
DR eggNOG; KOG4389; Eukaryota.
DR InParanoid; P37136; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P37136; -.
DR BRENDA; 3.1.1.7; 5301.
DR PRO; PR:P37136; -.
DR Proteomes; UP000002494; Unplaced.
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:0030424; C:axon; IDA:RGD.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR GO; GO:0042166; F:acetylcholine binding; IDA:RGD.
DR GO; GO:0003990; F:acetylcholinesterase activity; IDA:RGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0033265; F:choline binding; IDA:RGD.
DR GO; GO:0004104; F:cholinesterase activity; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0016787; F:hydrolase activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0043236; F:laminin binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0017171; F:serine hydrolase activity; ISO:RGD.
DR GO; GO:0006581; P:acetylcholine catabolic process; IDA:RGD.
DR GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IC:SynGO.
DR GO; GO:0008291; P:acetylcholine metabolic process; IMP:RGD.
DR GO; GO:0095500; P:acetylcholine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0019695; P:choline metabolic process; IDA:RGD.
DR GO; GO:0070997; P:neuron death; IMP:RGD.
DR GO; GO:0002076; P:osteoblast development; ISO:RGD.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IMP:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0001919; P:regulation of receptor recycling; ISO:RGD.
DR GO; GO:0046677; P:response to antibiotic; IDA:RGD.
DR GO; GO:0032868; P:response to insulin; IDA:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; IMP:RGD.
DR Gene3D; 3.40.50.1820; -; 1.
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; 1.
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; Disulfide bond; Glycoprotein;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation;
KW Reference proteome; Secreted; Serine esterase; Signal; Synapse.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..614
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008590"
FT ACT_SITE 234
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 365
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 478
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..127
FT /evidence="ECO:0000250"
FT DISULFID 288..303
FT /evidence="ECO:0000250"
FT DISULFID 440..560
FT /evidence="ECO:0000250"
FT DISULFID 611
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 575..614
FT /note="DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL -> ATEVPCTC
FT PSPAHGEAAPRPGPALSLSLLFFLFLLHSGLRWL (in isoform H)"
FT /evidence="ECO:0000303|PubMed:8417973"
FT /id="VSP_001458"
FT VAR_SEQ 575..614
FT /note="DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL -> GRRGVGKQ
FT GMHKAARVGRTGERKGGKHRM (in isoform R)"
FT /evidence="ECO:0000303|PubMed:8417973"
FT /id="VSP_001459"
SQ SEQUENCE 614 AA; 68196 MW; 2EDAE7D46282E7C0 CRC64;
MRPPWYPLHT PSLASPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG IRLKAPGGPV
SAFLGIPFAE PPVGSRRFMP PEPKRPWSGI LDATTFQNVC YQYVDTLYPG FEGTEMWNPN
RELSEDCLYL NVWTPYPRPT SPTPVLIWIY GGGFYSGASS LDVYDGRFLA QVEGTVLVSM
NYRVGTFGFL ALPGSREAPG NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV
GMHILSLPSR SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL
ISCLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPDALINTG DFQDLQVLVG
VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ ASDLAAEAVV LHYTDWLHPE
DPAHLRDAMS AVVGDHNVVC PVAQLAGRLA AQGARVYAYI FEHRASTLTW PLWMGVPHGY
EIEFIFGLPL DPSLNYTVEE RIFAQRLMQY WTNFARTGDP NDPRDSKSPR WPPYTTAAQQ
YVSLNLKPLE VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN
QFDHYSKQER CSDL
