ACES_FELCA
ID ACES_FELCA Reviewed; 611 AA.
AC O62763; O62762;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Acetylcholinesterase;
DE Short=AChE;
DE EC=3.1.1.7;
DE Flags: Precursor;
GN Name=ACHE;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS H AND T).
RX PubMed=10874122; DOI=10.1016/s0006-2952(00)00365-8;
RA Bartels C.F., Xie W., Miller-Lindholm A.K., Schopfer L.M., Lockridge O.;
RT "Determination of the DNA sequences of acetylcholinesterase and
RT butyrylcholinesterase from cat and demonstration of the existence of both
RT in cat plasma.";
RL Biochem. Pharmacol. 60:479-487(2000).
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=O62763-1; Sequence=Displayed;
CC Name=H;
CC IsoId=O62763-2; Sequence=VSP_001456;
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AF053485; AAC08995.1; -; Genomic_DNA.
DR EMBL; AF053485; AAC08996.1; -; Genomic_DNA.
DR RefSeq; NP_001009203.1; NM_001009203.1. [O62763-1]
DR RefSeq; XP_011288624.1; XM_011290322.2. [O62763-2]
DR RefSeq; XP_019675779.1; XM_019820220.1. [O62763-2]
DR RefSeq; XP_019675780.1; XM_019820221.1. [O62763-2]
DR AlphaFoldDB; O62763; -.
DR SMR; O62763; -.
DR STRING; 9685.ENSFCAP00000020757; -.
DR ESTHER; felca-ACHE; AChE.
DR MEROPS; S09.979; -.
DR Ensembl; ENSFCAT00000032091; ENSFCAP00000024567; ENSFCAG00000023546. [O62763-2]
DR Ensembl; ENSFCAT00000045236; ENSFCAP00000027951; ENSFCAG00000023546. [O62763-1]
DR GeneID; 493674; -.
DR KEGG; fca:493674; -.
DR CTD; 43; -.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157637; -.
DR InParanoid; O62763; -.
DR Proteomes; UP000011712; Chromosome E3.
DR Bgee; ENSFCAG00000023546; Expressed in prefrontal cortex and 10 other tissues.
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: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 3: Inferred from homology;
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:0000250"
FT CHAIN 32..611
FT /note="Acetylcholinesterase"
FT /id="PRO_0000008586"
FT ACT_SITE 231
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 362
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 475
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..124
FT /evidence="ECO:0000250"
FT DISULFID 285..300
FT /evidence="ECO:0000250"
FT DISULFID 437..557
FT /evidence="ECO:0000250"
FT DISULFID 608
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 572..611
FT /note="DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL -> ASKAPSTC
FT SGPAHGEAAPRPRPGLSLPLLLLLFLLLSRLLRL (in isoform H)"
FT /evidence="ECO:0000305"
FT /id="VSP_001456"
SQ SEQUENCE 611 AA; 67299 MW; DFA5C0885A225527 CRC64;
MRPPWCPLYT PSLAAPILLL LLFLLGGGAE AEDPELLVTV RGGQLRGVRL MAPGGPVSAF
LGIPFAEPPV GPRRFLPPEP KRPWPGVLDA TAFQSVCYQY VDTLYPGFEG TEMWNPNREL
SEDCLYLNVW TPYPRPASPT PVLVWIYGGG FYSGASSLDV YDGRFLAQAE GTVLVSMNYR
VGAFGFLALP GSREAPGNVG LLDQRLALQW VQDNVATFGG DPMSVTLFGE SAGAASVGMH
LLSPPSRGLF HRAVLQSGAP NGPWATVGVG EARRRATLLA RLVGCPPGGA GGNDTELVAC
LRTRPAQDLV DHEWHVLPQE SVFRFSFVPV VDGDFLSDTP EALINAGDFH GLQVLVGVVK
DEGSYFLVYG APGFSKDNES LISRAQFLAG VRVGVPQASD LAAEAVVLHY TDWLNPEDPA
RLREAMSDVV GDHNVVCPVA QLAGRLAAQG ARVYAYIFEH RASTLSWPLW MGVPHGYEIE
FIFGLPLEPS LNYTAEERIF AQRLMRYWAN FARTGDPNDP RDPKVPQWPP YTAGAQQYVS
LDLRPLEVRR GLRAQACAFW NRFLPKLLSA TDTLDEAERQ WKAEFHRWSS YMVHWKNQFD
HYSKQDRCSD L
