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Protein

Acetylcholinesterase

Gene

ACHE

Organism
Bungarus fasciatus (Banded krait) (Pseudoboa fasciata)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei231 – 2311Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei358 – 3581Charge relay systemBy similarity
Active sitei471 – 4711Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase, Toxin

Keywords - Biological processi

Neurotransmitter degradation

Protein family/group databases

ESTHERibunfa-ACHE. AChE.
MEROPSiS09.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ACHE
OrganismiBungarus fasciatus (Banded krait) (Pseudoboa fasciata)
Taxonomic identifieri8613 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011M → Y: Increases peripheral site ligand binding.
Mutagenesisi316 – 3161K → D: Increases peripheral site ligand binding.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 606578AcetylcholinesterasePRO_0000008592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi98 ↔ 125By similarity
Disulfide bondi285 ↔ 296By similarity
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi433 ↔ 552By similarity
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi603 – 603Interchain; in isoform TBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Liver and muscle contain both isoform T and isoform S. Venom gland predominantly contains isoform S.1 Publication

Interactioni

Subunit structurei

Isoform S is monomeric. Isoform T can form oligomers, including collagen-tailed forms.1 Publication

Structurei

Secondary structure

1
606
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 414Combined sources
Beta strandi44 – 474Combined sources
Beta strandi49 – 535Combined sources
Beta strandi56 – 6712Combined sources
Helixi72 – 743Combined sources
Beta strandi86 – 905Combined sources
Helixi110 – 1134Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi127 – 1359Combined sources
Beta strandi138 – 1469Combined sources
Turni150 – 1523Combined sources
Helixi159 – 1613Combined sources
Helixi164 – 1707Combined sources
Beta strandi173 – 1764Combined sources
Helixi183 – 1864Combined sources
Helixi199 – 21416Combined sources
Helixi216 – 2183Combined sources
Beta strandi220 – 23011Combined sources
Helixi232 – 24211Combined sources
Beta strandi246 – 2494Combined sources
Beta strandi251 – 2577Combined sources
Turni263 – 2653Combined sources
Helixi269 – 28214Combined sources
Beta strandi288 – 2903Combined sources
Helixi291 – 2999Combined sources
Helixi302 – 3098Combined sources
Helixi310 – 3123Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi329 – 3313Combined sources
Helixi336 – 3427Combined sources
Beta strandi350 – 35910Combined sources
Helixi360 – 3634Combined sources
Turni364 – 3663Combined sources
Helixi380 – 39011Combined sources
Helixi396 – 40510Combined sources
Beta strandi409 – 4113Combined sources
Helixi415 – 43016Combined sources
Helixi432 – 44312Combined sources
Turni444 – 4463Combined sources
Beta strandi449 – 4546Combined sources
Helixi465 – 4673Combined sources
Turni471 – 4744Combined sources
Helixi475 – 4784Combined sources
Helixi481 – 4833Combined sources
Helixi485 – 4873Combined sources
Helixi491 – 50919Combined sources
Beta strandi511 – 5144Combined sources
Beta strandi528 – 5303Combined sources
Beta strandi533 – 5397Combined sources
Beta strandi542 – 5454Combined sources
Helixi549 – 5568Combined sources
Helixi558 – 5658Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QWWX-ray2.70A/B32-566[»]
ProteinModelPortaliQ92035.
SMRiQ92035. Positions 36-600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008839.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00879. ACHEFISH.
PR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform T (identifier: Q92035-2) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPSCQPGKMP APWPWWLQLL LCIPSCVAVL PGRAGELKVS TQTGSVRGLS
60 70 80 90 100
LPVLDGHVSA FLGIPFAEPP LGRMRFLRPE PVKPWQHVLD ATSYKPACYQ
110 120 130 140 150
MVDTSYPGFQ GTEMWNPNRG MSEDCLYLNI WVPSPRPKDA PVLVWIYGGG
160 170 180 190 200
FYSGAASLDV YDGRFLTYTQ NVILVSLSYR VGAFGFLGLP GSPEAPGNMG
210 220 230 240 250
LLDQRLALQW IQNNIHPFGG NPRAVTVFGE SAGAASVGMH LLSTQSRTLF
260 270 280 290 300
QRAILQSGGP NAPWATVTPA ESRGRAALLG KQLGCHFNND SELVSCLRSK
310 320 330 340 350
NPQELIDEEW SVLPYKSIFR FPFVPVIDGD FFPDTPEAML SSGNFKETQV
360 370 380 390 400
LLGVVKDEGS YFLIYGLPGF SKDNESLISR ADFLEGVRMS VPHANDIATD
410 420 430 440 450
AVVLQYTDWQ DQDNREKNRE ALDDIVGDHN VICPVVQFAN DYAKRNSKVY
460 470 480 490 500
AYLFDHRASN LLWPPWMGVP HGYEIEFVFG LPLNDSLNYT PQEKELSRRM
510 520 530 540 550
MRYWANFART GNPTDPADKS GAWPTYTASQ PQYVQLNTQP LATQPSLRAQ
560 570 580 590 600
ICAFWNHFLP KLLNATDNIE EAERQWKLEF HLWSAYMMHW KSQFDHYNKQ

DRCSEL
Length:606
Mass (Da):68,074
Last modified:September 19, 2003 - v2
Checksum:iB95998AEEA0E5709
GO
Isoform S (identifier: Q92035-1) [UniParc]FASTAAdd to basket

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

Show »
Length:581
Mass (Da):64,723
Checksum:i436C3CBE457E399F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681T → S AA sequence (PubMed:8674549).Curated
Sequence conflicti350 – 3501V → L AA sequence (PubMed:8674549).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei567 – 60640DNIEE…RCSEL → VDPPRADRRRRSARA in isoform S. 1 PublicationVSP_008215Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54591 mRNA. Translation: AAC59905.1.
AF045238 Genomic DNA. Translation: AAC16420.1.
AF045238 Genomic DNA. Translation: AAC16421.1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54591 mRNA. Translation: AAC59905.1.
AF045238 Genomic DNA. Translation: AAC16420.1.
AF045238 Genomic DNA. Translation: AAC16421.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4QWWX-ray2.70A/B32-566[»]
ProteinModelPortaliQ92035.
SMRiQ92035. Positions 36-600.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERibunfa-ACHE. AChE.
MEROPSiS09.979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008839.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00879. ACHEFISH.
PR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiACES_BUNFA
AccessioniPrimary (citable) accession number: Q92035
Secondary accession number(s): O73748, Q10720
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 19, 2003
Last modified: July 22, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.