ACES_BOVIN
ID ACES_BOVIN Reviewed; 613 AA.
AC P23795; O97579; Q08D79;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE;
DE EC=3.1.1.7;
DE Flags: Precursor;
GN Name=ACHE;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC TISSUE=Kidney;
RX PubMed=9693127; DOI=10.1042/bj3340251;
RA Mendelson I., Kronman C., Ariel N., Shafferman A., Velan B.;
RT "Bovine acetylcholinesterase: cloning, expression and characterization.";
RL Biochem. J. 334:251-259(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 31-613 (ISOFORM H).
RC TISSUE=Fetal serum;
RX PubMed=2365060; DOI=10.1016/0014-5793(90)81522-p;
RA Doctor B.P., Chapman T.C., Christner C.E., Deal C.D., de la Hoz D.M.,
RA Gentry M.K., Ogert R.A., Rush R.S., Smyth K.K., Wolfe A.D.;
RT "Complete amino acid sequence of fetal bovine serum acetylcholinesterase
RT and its comparison in various regions with other cholinesterases.";
RL FEBS Lett. 266:123-127(1990).
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:
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: Interacts with PRIMA1. The interaction with PRIMA1 is required
CC to anchor it to the basal lamina of cells and organize into tetramers
CC (By similarity). Isoform H generates GPI-anchored dimers; disulfide
CC linked. Isoform T generates multiple structures, ranging from monomers
CC and dimers to collagen-tailed and hydrophobic-tailed forms, in which
CC catalytic tetramers are associated with anchoring proteins that attach
CC them to the basal lamina or to cell membranes. In the collagen-tailed
CC forms, isoform T subunits are associated with a specific collagen,
CC COLQ, which triggers the formation of isoform T tetramers, from
CC monomers and dimers. {ECO:0000250}.
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=2;
CC Name=T;
CC IsoId=P23795-1; Sequence=Displayed;
CC Name=H;
CC IsoId=P23795-2; Sequence=VSP_001455;
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AF061815; AAC64270.1; -; Genomic_DNA.
DR EMBL; AF061813; AAC64270.1; JOINED; Genomic_DNA.
DR EMBL; AF061814; AAC64270.1; JOINED; Genomic_DNA.
DR EMBL; BC123898; AAI23899.1; -; mRNA.
DR RefSeq; NP_001069688.1; NM_001076220.1.
DR AlphaFoldDB; P23795; -.
DR SMR; P23795; -.
DR STRING; 9913.ENSBTAP00000001517; -.
DR BindingDB; P23795; -.
DR ChEMBL; CHEMBL4768; -.
DR DrugCentral; P23795; -.
DR ESTHER; bovin-ACHE; AChE.
DR MEROPS; S09.979; -.
DR GlyConnect; 8; 21 N-Linked glycans.
DR PaxDb; P23795; -.
DR GeneID; 540446; -.
DR KEGG; bta:540446; -.
DR CTD; 43; -.
DR eggNOG; KOG4389; Eukaryota.
DR InParanoid; P23795; -.
DR OrthoDB; 754103at2759; -.
DR BRENDA; 3.1.1.7; 908.
DR Proteomes; UP000009136; 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:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0003990; F:acetylcholinesterase activity; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:HGNC-UCL.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
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; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Neurotransmitter degradation; Reference proteome; Secreted;
KW Serine esterase; Signal; Synapse.
FT SIGNAL 1..30
FT CHAIN 31..613
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008585"
FT ACT_SITE 233
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 364
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 477
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 99..126
FT /evidence="ECO:0000250"
FT DISULFID 287..302
FT /evidence="ECO:0000250"
FT DISULFID 439..559
FT /evidence="ECO:0000250"
FT DISULFID 610
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 574..613
FT /note="DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL -> ASEAPCTC
FT SGPAHGEAAPRPRPGLPLPLLLLLFLLSRLLRL (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_001455"
FT CONFLICT 24
FT /note="I -> L (in Ref. 2; AAI23899)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="R -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="T -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="W -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="S -> H (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="H -> V (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="L -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="D -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 549..554
FT /note="EVRRGL -> GVPQAS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 67664 MW; 698D4F0DF8624B12 CRC64;
MRPPWCPLHT PSLTPPLLLL LFLIGGGAEA EGPEDPELLV MVRGGRLRGL RLMAPRGPVS
AFLGIPFAEP PVGPRRFLPP EPKRPWPGVL NATAFQSVCY QYVDTLYPGF EGTEMWNPNR
ELSEDCLYLN VWTPYPRPSS PTPVLVWIYG GGFYSGASSL DVYDGRFLTQ AEGTVLVSMN
YRVGAFGFLA LPGSREAPGN VGLLDQRLAL QWVQENVAAF GGDPTSVTLF GESAGAASVG
MHLLSPPSRG LFHRAVLQSG APNGPWATVG VGEARRRATL LARLVGCPPG GAGGNDTELV
ACLRARPAQD LVDHEWRVLP QESVFRFSFV PVVDGDFLSD TPEALINAGD FHGLQVLVGV
VKDEGSYFLV YGAPGFSKDN ESLISRAQFL AGVRVGVPQA SDLAAEAVVL HYTDWLHPED
PARLREALSD VVGDHNVVCP VAQLAGRLAA QGARVYAYIF EHRASTLSWP LWMGVPHGYE
IEFIFGLPLE PSLNYTIEER TFAQRLMRYW ANFARTGDPN DPRDPKAPQW PPYTAGAQQY
VSLNLRPLEV RRGLRAQACA FWNRFLPKLL SATDTLDEAE RQWKAEFHRW SSYMVHWKNQ
FDHYSKQDRC SDL
