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Database: UniProt
Entry: P21927
LinkDB: P21927
Original site: P21927 
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   29-OCT-2014, entry version 91.
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       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: An acylcholine + H(2)O = choline + a
CC       carboxylate.
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   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   InParanoid; P21927; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0003990; F:acetylcholinesterase activity; ISS:UniProtKB.
DR   GO; GO:0004104; F:cholinesterase activity; ISS:UniProtKB.
DR   GO; GO:0008152; P:metabolic process; ISS:GOC.
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   ProDom; PD415333; AChE_tetra; 1.
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   Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
KW   Phosphoprotein; Reference proteome; Secreted; Serine esterase; Signal.
FT   SIGNAL        1      8       {ECO:0000255}.
FT   CHAIN         9    581       Cholinesterase.
FT                                /FTId=PRO_0000008616.
FT   REGION      123    124       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    205    205       Acyl-ester intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10039}.
FT   ACT_SITE    332    332       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    445    445       Charge relay system. {ECO:0000250}.
FT   MOD_RES     205    205       Phosphoserine. {ECO:0000250}.
FT   CARBOHYD     64     64       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    113    113       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    248    248       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    263    263       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    348    348       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    462    462       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    488    488       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    492    492       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    493    493       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     72     99       {ECO:0000250}.
FT   DISULFID    259    270       {ECO:0000250}.
FT   DISULFID    407    526       {ECO:0000250}.
FT   DISULFID    578    578       Interchain. {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
//
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