ID   ACES_BUNFA              Reviewed;         606 AA.
AC   Q92035; O73748; Q10720;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   22-JUL-2015, entry version 89.
DE   RecName: Full=Acetylcholinesterase;
DE            Short=AChE;
DE            EC=3.1.1.7;
DE   Flags: Precursor;
GN   Name=ACHE;
OS   Bungarus fasciatus (Banded krait) (Pseudoboa fasciata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
OC   Toxicofera; Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX   NCBI_TaxID=8613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S).
RC   TISSUE=Venom gland;
RX   PubMed=8662867; DOI=10.1074/jbc.271.25.15099;
RA   Cousin X., Bon S., Duval N., Massoulie J., Bon C.;
RT   "Cloning and expression of acetylcholinesterase from Bungarus
RT   fasciatus venom. A new type of COOH-terminal domain; involvement of a
RT   positively charged residue in the peripheral site.";
RL   J. Biol. Chem. 271:15099-15108(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-606 (ISOFORMS S AND T),
RP   SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver, and Muscle;
RX   PubMed=9545320; DOI=10.1074/jbc.273.16.9812;
RA   Cousin X., Bon S., Massoulie J., Bon C.;
RT   "Identification of a novel type of alternatively spliced exon from the
RT   acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of
RT   acetylcholinesterase in the snake liver and muscle.";
RL   J. Biol. Chem. 273:9812-9820(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF 206-220; 253-272; 321-340; 347-372 AND 503-511.
RC   TISSUE=Venom;
RX   PubMed=8674549; DOI=10.1016/0014-5793(96)00447-4;
RA   Cousin X., Creminon C., Grassi J., Meflah K., Cornu G., Saliou B.,
RA   Bon S., Massoulie J., Bon C.;
RT   "Acetylcholinesterase from Bungarus venom: a monomeric species.";
RL   FEBS Lett. 387:196-200(1996).
CC   -!- FUNCTION: In muscle, it terminates signal transduction at the
CC       neuromuscular junction by rapid hydrolysis of the acetylcholine
CC       released into the synaptic cleft. In liver, its function is
CC       unclear: it could serve as a safeguard against any diffusion of
CC       acetylcholine from synapses into the circulation. In venom, its
CC       toxic role is unclear: It could result in less musculatory control
CC       by rapidly hydrolyzing acetylcholine, or that it works
CC       synergistically with alkaline phosphatase (ALP) in paralyzing prey
CC       through hypotension.
CC   -!- CATALYTIC ACTIVITY: Acetylcholine + H(2)O = choline + acetate.
CC   -!- SUBUNIT: Isoform S is monomeric. Isoform T can form oligomers,
CC       including collagen-tailed forms. {ECO:0000269|PubMed:9545320}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse. Secreted. Cell
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=T;
CC         IsoId=Q92035-2; Sequence=Displayed;
CC       Name=S;
CC         IsoId=Q92035-1; Sequence=VSP_008215;
CC   -!- TISSUE SPECIFICITY: Liver and muscle contain both isoform T and
CC       isoform S. Venom gland predominantly contains isoform S.
CC       {ECO:0000269|PubMed:9545320}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U54591; AAC59905.1; -; mRNA.
DR   EMBL; AF045238; AAC16420.1; -; Genomic_DNA.
DR   EMBL; AF045238; AAC16421.1; -; Genomic_DNA.
DR   PDB; 4QWW; X-ray; 2.70 A; A/B=32-566.
DR   PDBsum; 4QWW; -.
DR   ProteinModelPortal; Q92035; -.
DR   SMR; Q92035; 36-600.
DR   ESTHER; bunfa-ACHE; AChE.
DR   MEROPS; S09.979; -.
DR   HOVERGEN; HBG008839; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043083; C:synaptic cleft; IEA:GOC.
DR   GO; GO:0003990; F:acetylcholinesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001507; P:acetylcholine catabolic process in synaptic cleft; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR014788; AChE_tetra.
DR   InterPro; IPR000908; Acylcholinesterase_fish/snake.
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; PR00879; ACHEFISH.
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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Membrane; Neurotransmitter degradation; Secreted; Serine esterase;
KW   Signal; Synapse; Toxin.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29    606       Acetylcholinesterase.
FT                                /FTId=PRO_0000008592.
FT   ACT_SITE    231    231       Acyl-ester intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10039}.
FT   ACT_SITE    358    358       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    471    471       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    289    289       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    374    374       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    484    484       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    564    564       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     98    125       {ECO:0000250}.
FT   DISULFID    285    296       {ECO:0000250}.
FT   DISULFID    433    552       {ECO:0000250}.
FT   DISULFID    603    603       Interchain; in isoform T. {ECO:0000250}.
FT   VAR_SEQ     567    606       DNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQDRCSEL
FT                                -> VDPPRADRRRRSARA (in isoform S).
FT                                {ECO:0000303|PubMed:8662867}.
FT                                /FTId=VSP_008215.
FT   MUTAGEN     101    101       M->Y: Increases peripheral site ligand
FT                                binding.
FT   MUTAGEN     316    316       K->D: Increases peripheral site ligand
FT                                binding.
FT   CONFLICT    268    268       T -> S (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT    350    350       V -> L (in Ref. 3; AA sequence).
FT                                {ECO:0000305}.
FT   STRAND       38     41       {ECO:0000244|PDB:4QWW}.
FT   STRAND       44     47       {ECO:0000244|PDB:4QWW}.
FT   STRAND       49     53       {ECO:0000244|PDB:4QWW}.
FT   STRAND       56     67       {ECO:0000244|PDB:4QWW}.
FT   HELIX        72     74       {ECO:0000244|PDB:4QWW}.
FT   STRAND       86     90       {ECO:0000244|PDB:4QWW}.
FT   HELIX       110    113       {ECO:0000244|PDB:4QWW}.
FT   STRAND      121    123       {ECO:0000244|PDB:4QWW}.
FT   STRAND      127    135       {ECO:0000244|PDB:4QWW}.
FT   STRAND      138    146       {ECO:0000244|PDB:4QWW}.
FT   TURN        150    152       {ECO:0000244|PDB:4QWW}.
FT   HELIX       159    161       {ECO:0000244|PDB:4QWW}.
FT   HELIX       164    170       {ECO:0000244|PDB:4QWW}.
FT   STRAND      173    176       {ECO:0000244|PDB:4QWW}.
FT   HELIX       183    186       {ECO:0000244|PDB:4QWW}.
FT   HELIX       199    214       {ECO:0000244|PDB:4QWW}.
FT   HELIX       216    218       {ECO:0000244|PDB:4QWW}.
FT   STRAND      220    230       {ECO:0000244|PDB:4QWW}.
FT   HELIX       232    242       {ECO:0000244|PDB:4QWW}.
FT   STRAND      246    249       {ECO:0000244|PDB:4QWW}.
FT   STRAND      251    257       {ECO:0000244|PDB:4QWW}.
FT   TURN        263    265       {ECO:0000244|PDB:4QWW}.
FT   HELIX       269    282       {ECO:0000244|PDB:4QWW}.
FT   STRAND      288    290       {ECO:0000244|PDB:4QWW}.
FT   HELIX       291    299       {ECO:0000244|PDB:4QWW}.
FT   HELIX       302    309       {ECO:0000244|PDB:4QWW}.
FT   HELIX       310    312       {ECO:0000244|PDB:4QWW}.
FT   STRAND      314    316       {ECO:0000244|PDB:4QWW}.
FT   STRAND      329    331       {ECO:0000244|PDB:4QWW}.
FT   HELIX       336    342       {ECO:0000244|PDB:4QWW}.
FT   STRAND      350    359       {ECO:0000244|PDB:4QWW}.
FT   HELIX       360    363       {ECO:0000244|PDB:4QWW}.
FT   TURN        364    366       {ECO:0000244|PDB:4QWW}.
FT   HELIX       380    390       {ECO:0000244|PDB:4QWW}.
FT   HELIX       396    405       {ECO:0000244|PDB:4QWW}.
FT   STRAND      409    411       {ECO:0000244|PDB:4QWW}.
FT   HELIX       415    430       {ECO:0000244|PDB:4QWW}.
FT   HELIX       432    443       {ECO:0000244|PDB:4QWW}.
FT   TURN        444    446       {ECO:0000244|PDB:4QWW}.
FT   STRAND      449    454       {ECO:0000244|PDB:4QWW}.
FT   HELIX       465    467       {ECO:0000244|PDB:4QWW}.
FT   TURN        471    474       {ECO:0000244|PDB:4QWW}.
FT   HELIX       475    478       {ECO:0000244|PDB:4QWW}.
FT   HELIX       481    483       {ECO:0000244|PDB:4QWW}.
FT   HELIX       485    487       {ECO:0000244|PDB:4QWW}.
FT   HELIX       491    509       {ECO:0000244|PDB:4QWW}.
FT   STRAND      511    514       {ECO:0000244|PDB:4QWW}.
FT   STRAND      528    530       {ECO:0000244|PDB:4QWW}.
FT   STRAND      533    539       {ECO:0000244|PDB:4QWW}.
FT   STRAND      542    545       {ECO:0000244|PDB:4QWW}.
FT   HELIX       549    556       {ECO:0000244|PDB:4QWW}.
FT   HELIX       558    565       {ECO:0000244|PDB:4QWW}.
SQ   SEQUENCE   606 AA;  68074 MW;  B95998AEEA0E5709 CRC64;
     MPSCQPGKMP APWPWWLQLL LCIPSCVAVL PGRAGELKVS TQTGSVRGLS LPVLDGHVSA
     FLGIPFAEPP LGRMRFLRPE PVKPWQHVLD ATSYKPACYQ MVDTSYPGFQ GTEMWNPNRG
     MSEDCLYLNI WVPSPRPKDA PVLVWIYGGG FYSGAASLDV YDGRFLTYTQ NVILVSLSYR
     VGAFGFLGLP GSPEAPGNMG LLDQRLALQW IQNNIHPFGG NPRAVTVFGE SAGAASVGMH
     LLSTQSRTLF QRAILQSGGP NAPWATVTPA ESRGRAALLG KQLGCHFNND SELVSCLRSK
     NPQELIDEEW SVLPYKSIFR FPFVPVIDGD FFPDTPEAML SSGNFKETQV LLGVVKDEGS
     YFLIYGLPGF SKDNESLISR ADFLEGVRMS VPHANDIATD AVVLQYTDWQ DQDNREKNRE
     ALDDIVGDHN VICPVVQFAN DYAKRNSKVY AYLFDHRASN LLWPPWMGVP HGYEIEFVFG
     LPLNDSLNYT PQEKELSRRM MRYWANFART GNPTDPADKS GAWPTYTASQ PQYVQLNTQP
     LATQPSLRAQ ICAFWNHFLP KLLNATDNIE EAERQWKLEF HLWSAYMMHW KSQFDHYNKQ
     DRCSEL
//