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Q92035 (ACES_BUNFA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase

Short name=AChE
EC=3.1.1.7
Gene names
Name:ACHE
OrganismBungarus fasciatus (Banded krait)
Taxonomic identifier8613 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Protein attributes

Sequence length606 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In muscle, it terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. In liver, its function is unclear: it could serve as a safeguard against any diffusion of acetylcholine from synapses into the circulation. In venom, its toxic role is unclear: It could result in less musculatory control by rapidly hydrolyzing acetylcholine, or that it works synergistically with alkaline phosphatase (ALP) in paralyzing prey through hypotension.

Catalytic activity

Acetylcholine + H2O = choline + acetate.

Subunit structure

Isoform S is monomeric. Isoform T can form oligomers, including collagen-tailed forms. Ref.2

Subcellular location

Cell junctionsynapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.

Tissue specificity

Liver and muscle contain both isoform T and isoform S. Venom gland predominantly contains isoform S. Ref.2

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Caution

It is uncertain whether Met-1 or Met-9 is the initiator.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHydrolase
Serine esterase
Toxin
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processacetylcholine catabolic process in synaptic cleft

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholinesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform T (identifier: Q92035-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform S (identifier: Q92035-1)

The sequence of this isoform differs from the canonical sequence as follows:
     567-606: DNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQDRCSEL → VDPPRADRRRRSARA

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 606578Acetylcholinesterase
PRO_0000008592

Sites

Active site2311Acyl-ester intermediate By similarity
Active site3581Charge relay system By similarity
Active site4711Charge relay system By similarity

Amino acid modifications

Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4841N-linked (GlcNAc...) Potential
Glycosylation5641N-linked (GlcNAc...) Potential
Disulfide bond98 ↔ 125 By similarity
Disulfide bond285 ↔ 296 By similarity
Disulfide bond433 ↔ 552 By similarity
Disulfide bond603Interchain; in isoform T By similarity

Natural variations

Alternative sequence567 – 60640DNIEE…RCSEL → VDPPRADRRRRSARA in isoform S.
VSP_008215

Experimental info

Mutagenesis1011M → Y: Increases peripheral site ligand binding.
Mutagenesis3161K → D: Increases peripheral site ligand binding.
Sequence conflict2681T → S AA sequence Ref.3
Sequence conflict3501V → L AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform T [UniParc].

Last modified September 19, 2003. Version 2.
Checksum: B95998AEEA0E5709

FASTA60668,074
        10         20         30         40         50         60 
MPSCQPGKMP APWPWWLQLL LCIPSCVAVL PGRAGELKVS TQTGSVRGLS LPVLDGHVSA 

        70         80         90        100        110        120 
FLGIPFAEPP LGRMRFLRPE PVKPWQHVLD ATSYKPACYQ MVDTSYPGFQ GTEMWNPNRG 

       130        140        150        160        170        180 
MSEDCLYLNI WVPSPRPKDA PVLVWIYGGG FYSGAASLDV YDGRFLTYTQ NVILVSLSYR 

       190        200        210        220        230        240 
VGAFGFLGLP GSPEAPGNMG LLDQRLALQW IQNNIHPFGG NPRAVTVFGE SAGAASVGMH 

       250        260        270        280        290        300 
LLSTQSRTLF QRAILQSGGP NAPWATVTPA ESRGRAALLG KQLGCHFNND SELVSCLRSK 

       310        320        330        340        350        360 
NPQELIDEEW SVLPYKSIFR FPFVPVIDGD FFPDTPEAML SSGNFKETQV LLGVVKDEGS 

       370        380        390        400        410        420 
YFLIYGLPGF SKDNESLISR ADFLEGVRMS VPHANDIATD AVVLQYTDWQ DQDNREKNRE 

       430        440        450        460        470        480 
ALDDIVGDHN VICPVVQFAN DYAKRNSKVY AYLFDHRASN LLWPPWMGVP HGYEIEFVFG 

       490        500        510        520        530        540 
LPLNDSLNYT PQEKELSRRM MRYWANFART GNPTDPADKS GAWPTYTASQ PQYVQLNTQP 

       550        560        570        580        590        600 
LATQPSLRAQ ICAFWNHFLP KLLNATDNIE EAERQWKLEF HLWSAYMMHW KSQFDHYNKQ 


DRCSEL 

« Hide

Isoform S [UniParc].

Checksum: 436C3CBE457E399F
Show »

FASTA58164,723

References

[1]"Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of COOH-terminal domain; involvement of a positively charged residue in the peripheral site."
Cousin X., Bon S., Duval N., Massoulie J., Bon C.
J. Biol. Chem. 271:15099-15108(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S).
Tissue: Venom gland.
[2]"Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle."
Cousin X., Bon S., Massoulie J., Bon C.
J. Biol. Chem. 273:9812-9820(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-606 (ISOFORMS S AND T), SUBUNIT, TISSUE SPECIFICITY.
Tissue: Liver and Muscle.
[3]"Acetylcholinesterase from Bungarus venom: a monomeric species."
Cousin X., Creminon C., Grassi J., Meflah K., Cornu G., Saliou B., Bon S., Massoulie J., Bon C.
FEBS Lett. 387:196-200(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 206-220; 253-272; 321-340; 347-372 AND 503-511.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U54591 mRNA. Translation: AAC59905.1.
AF045238 Genomic DNA. Translation: AAC16420.1.
AF045238 Genomic DNA. Translation: AAC16421.1.

3D structure databases

ProteinModelPortalQ92035.
SMRQ92035. Positions 36-600.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008839.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00879. ACHEFISH.
PR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_BUNFA
AccessionPrimary (citable) accession number: Q92035
Secondary accession number(s): O73748, Q10720
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 19, 2003
Last modified: January 22, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families