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-APR-2013, entry version 84.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC 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;
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
CC to the inactivation of the neurotransmitter acetylcholine. Can
CC degrade neurotoxic organophosphate esters (By similarity).
CC -!- CATALYTIC ACTIVITY: An acylcholine + H(2)O = choline + a
CC carboxylate.
CC -!- SUBUNIT: Homotetramer; disulfide-linked. Dimer of dimers (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC -!- TISSUE SPECIFICITY: Present in most cells except erythrocytes.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
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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 ProteinModelPortal; P21927; -.
DR SMR; P21927; 11-541, 543-572.
DR STRING; 9986.ENSOCUP00000006971; -.
DR MEROPS; S09.980; -.
DR eggNOG; COG2272; -.
DR HOGENOM; HOG000091866; -.
DR HOVERGEN; HBG008839; -.
DR OrthoDB; EOG46WZ86; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
DR GO; GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
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 ProDom; PD415333; AChE_tetra; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
KW Phosphoprotein; Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1 8 Potential.
FT CHAIN 9 581 Cholinesterase.
FT /FTId=PRO_0000008616.
FT REGION 123 124 Substrate binding (By similarity).
FT ACT_SITE 205 205 Acyl-ester intermediate (By similarity).
FT ACT_SITE 332 332 Charge relay system (By similarity).
FT ACT_SITE 445 445 Charge relay system (By similarity).
FT MOD_RES 205 205 Phosphoserine (By similarity).
FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 113 113 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 248 248 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 263 263 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 348 348 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 462 462 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 488 488 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 492 492 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 493 493 N-linked (GlcNAc...) (Potential).
FT DISULFID 72 99 By similarity.
FT DISULFID 259 270 By similarity.
FT DISULFID 407 526 By similarity.
FT DISULFID 578 578 Interchain (By similarity).
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
//
