CHLE_RABIT
ID CHLE_RABIT Reviewed; 581 AA.
AC P21927;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=New Zealand;
RX PubMed=2374720; DOI=10.1093/nar/18.13.3990;
RA Jbilo O., Roudani S., Chatonnet A.;
RT "Complete sequence of rabbit butyrylcholinesterase.";
RL Nucleic Acids Res. 18:3990-3990(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-215.
RC TISSUE=Liver;
RX PubMed=2016308; DOI=10.1016/s0021-9258(20)89597-0;
RA Arpagaus M., Chatonnet A., Masson P., Newton M., Vaughan T.A.,
RA Bartels C.F., Nogueira C.P., la Du B.N., Lockridge O.;
RT "Use of the polymerase chain reaction for homology probing of
RT butyrylcholinesterase from several vertebrates.";
RL J. Biol. Chem. 266:6966-6974(1991).
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 -!- TISSUE SPECIFICITY: Present in most cells except erythrocytes.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X52090; CAA36308.1; -; Genomic_DNA.
DR EMBL; X52091; CAA36308.1; JOINED; Genomic_DNA.
DR EMBL; X52092; CAA36308.1; JOINED; Genomic_DNA.
DR EMBL; M62779; AAA31169.1; -; Genomic_DNA.
DR PIR; S10255; C39768.
DR AlphaFoldDB; P21927; -.
DR SMR; P21927; -.
DR STRING; 9986.ENSOCUP00000006971; -.
DR ESTHER; rabit-BCHE; BCHE.
DR MEROPS; S09.980; -.
DR eggNOG; KOG4389; Eukaryota.
DR InParanoid; P21927; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
DR GO; GO:0004104; F:cholinesterase activity; ISS:UniProtKB.
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..8
FT /evidence="ECO:0000255"
FT CHAIN 9..581
FT /note="Cholinesterase"
FT /id="PRO_0000008616"
FT ACT_SITE 205
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 332
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 445
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 123..124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06276"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..99
FT /evidence="ECO:0000250"
FT DISULFID 259..270
FT /evidence="ECO:0000250"
FT DISULFID 407..526
FT /evidence="ECO:0000250"
FT DISULFID 578
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 581 AA; 66156 MW; FE8B199E7B32EB0A CRC64;
MVTRSSHTED VIITTKNGRI RGINLPVFGG TVTAFLGIPY AQPPLGRLRF KKPQSLTKWS
DIWNATKYAN SCCQNIDQSF PGFHGSEMWN PNTDLSEDCL YLNVWIPTPK PKNATVMIWI
YGGGFQTGTS SLQVYDGKFL TRVERVIVVS MNYRVGALGF LALPGNPEAP GNMGLFDQQL
ALQWVQKNIA AFGGNPKSVT LFGESAGAAS VSLHLLSPRS HPLFTRAILQ SGSSNAPWEV
MSLHEARNRT LTLAKFVGCS TENETEIIKC LRNKDAQEIL LNEVFVVPFD SLLSVNFGPT
VDGDFLTDMP DTLLQLGQLK KTQILVGVNK DEGTAFLVYG APGFSKDNTS IITRKEFQEG
LKIFFPGVSE FGKESILFHY TDWVDEQRPE NYREALDDVV GDYNFICPAL EFTKKFSEWG
NNAFFYYFEH RSSKLPWPEW MGVMHGYEIE FVFGLPLERR VNYTKAEEIL SRSIMKRWAN
FAKYGNPNGT QNNSTRWPVF KSTEQKYLTL NTESPRIYTK LRAQQCRFWT LFFPKVLEMT
GNIDEAEQEW KAGFHRWNNY MMAWKNHFND YTSKKERCAG F
