ID   CHLE_FELCA              Reviewed;         602 AA.
AC   O62760;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 122.
DE   RecName: Full=Cholinesterase;
DE            EC=3.1.1.8;
DE   AltName: Full=Acylcholine acylhydrolase;
DE   AltName: Full=Butyrylcholine esterase;
DE   AltName: Full=Choline esterase II;
DE   AltName: Full=Pseudocholinesterase;
DE   Flags: Precursor;
GN   Name=BCHE;
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 [MRNA].
RC   TISSUE=Pituitary;
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: Esterase with broad substrate specificity. Contributes to the
CC       inactivation of the neurotransmitter acetylcholine. Can degrade
CC       neurotoxic organophosphate esters (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acylcholine + H2O = a carboxylate + choline + H(+);
CC         Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8;
CC   -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF053483; AAC06261.1; -; mRNA.
DR   RefSeq; NP_001009364.1; NM_001009364.1.
DR   AlphaFoldDB; O62760; -.
DR   SMR; O62760; -.
DR   STRING; 9685.ENSFCAP00000026088; -.
DR   ESTHER; felca-BCHE; BCHE.
DR   MEROPS; S09.980; -.
DR   GlyCosmos; O62760; 9 sites, No reported glycans.
DR   PaxDb; 9685-ENSFCAP00000016618; -.
DR   Ensembl; ENSFCAT00000026436.4; ENSFCAP00000016618.1; ENSFCAG00000030105.4.
DR   GeneID; 493960; -.
DR   KEGG; fca:493960; -.
DR   VGNC; VGNC:69221; BCHE.
DR   eggNOG; KOG4389; Eukaryota.
DR   GeneTree; ENSGT00940000157023; -.
DR   HOGENOM; CLU_006586_13_0_1; -.
DR   InParanoid; O62760; -.
DR   OrthoDB; 4386at2759; -.
DR   Proteomes; UP000011712; Chromosome C2.
DR   Bgee; ENSFCAG00000030105; Expressed in eyeball of camera-type eye and 10 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
DR   GO; GO:0004104; F:cholinesterase activity; ISS:UniProtKB.
DR   GO; GO:0006581; P:acetylcholine catabolic process; IBA:GO_Central.
DR   GO; GO:0019695; P:choline metabolic process; IBA:GO_Central.
DR   CDD; cd00312; Esterase_lipase; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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   PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR   PANTHER; PTHR43918:SF5; CHOLINESTERASE; 1.
DR   Pfam; PF08674; AChE_tetra; 1.
DR   Pfam; PF00135; COesterase; 1.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Phosphoprotein;
KW   Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..602
FT                   /note="Cholinesterase"
FT                   /id="PRO_0000008612"
FT   ACT_SITE        226
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        353
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        466
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         144..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06276"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        483
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        509
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        93..120
FT                   /evidence="ECO:0000250"
FT   DISULFID        280..291
FT                   /evidence="ECO:0000250"
FT   DISULFID        428..547
FT                   /evidence="ECO:0000250"
FT   DISULFID        599
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   602 AA;  68328 MW;  ECB8879232B74B9C CRC64;
     MQSKGTIISI QFLLRFLLLW VLIGKSHTEE DIIITTKNGK VRGMNLPVLD GTVTAFLGIP
     YAQPPLGRLR FKKPQFLTKW SDIWNATKYA NSCYQNADQS FPGFPGSEMW NPNTDLSEDC
     LYLNVWIPTP KPKNATVMIW IYGGGFQTGT SSLPVYDGKF LARVERVIVV SMNYRVGALG
     FLALPGNPEV PGNMGLFDQQ LALQWVQKNI AAFGGNPKSV TLFGESAGAG SVSLHLLSPR
     SQPLFTRAIL QSGSSNAPWA VMSLDEAKNR TLTLAKFIGC SKENDTEIIK CLRNKDPQEI
     LLNELLVVPS DTLLSVNFGP VVDGDFLTDM PDTLLQLGQF KKTQILVGVN KDEGTAFLVY
     GAPGFSKDND SIITRKEFQE GLKIYFPGVS EFGREAILFY YVDLLDDQRA EKYREALDDV
     LGDYNIICPA LEFTTKFSEL GNNAFFYYFE HRSSQLPWPE WMGVMHGYEI EFVFGLPLER
     RVNYTRAEEI LSRSIMNYWA NFAKYGNPNG TQNNSTRWPA FRSTDQKYLT LNAESPKVYT
     KLRAQQCRFW TLFFPKVLEM TGNIDEAERE WRAGFYRWNN YMMDWKNQFN DYTSKKESCA
     GL
//