CHLE_FELCA
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 03-AUG-2022, entry version 115.
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.ENSFCAP00000016618; -.
DR ESTHER; felca-BCHE; BCHE.
DR MEROPS; S09.980; -.
DR Ensembl; ENSFCAT00000026436; ENSFCAP00000016618; ENSFCAG00000030105.
DR GeneID; 493960; -.
DR KEGG; fca:493960; -.
DR CTD; 590; -.
DR VGNC; VGNC:69221; BCHE.
DR eggNOG; KOG4389; Eukaryota.
DR GeneTree; ENSGT00940000157023; -.
DR HOGENOM; CLU_006586_13_0_1; -.
DR InParanoid; O62760; -.
DR OMA; EMRYICP; -.
DR OrthoDB; 754103at2759; -.
DR Proteomes; UP000011712; Chromosome C2.
DR Bgee; ENSFCAG00000030105; Expressed in eyeball of camera-type eye and 10 other 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:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
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 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 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
