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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)DescriptionActionsGraphical viewLength
Active sitei231Acyl-ester intermediatePROSITE-ProRule annotation1
Active sitei358Charge relay systemBy similarity1
Active sitei471Charge relay systemBy similarity1

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)DescriptionActionsGraphical viewLength
Mutagenesisi101M → Y: Increases peripheral site ligand binding. 1
Mutagenesisi316K → D: Increases peripheral site ligand binding. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000859229 – 606AcetylcholinesteraseAdd BLAST578

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi98 ↔ 125By similarity
Disulfide bondi285 ↔ 296By similarity
Glycosylationi289N-linked (GlcNAc...)Sequence analysis1
Glycosylationi374N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi433 ↔ 552By similarity
Glycosylationi484N-linked (GlcNAc...)Sequence analysis1
Glycosylationi564N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi603Interchain; in isoform TBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ92035.

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

1606
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 41Combined sources4
Beta strandi44 – 47Combined sources4
Beta strandi49 – 53Combined sources5
Beta strandi56 – 67Combined sources12
Helixi72 – 74Combined sources3
Beta strandi86 – 90Combined sources5
Helixi110 – 113Combined sources4
Beta strandi121 – 123Combined sources3
Beta strandi127 – 135Combined sources9
Beta strandi138 – 146Combined sources9
Turni150 – 152Combined sources3
Helixi159 – 161Combined sources3
Helixi164 – 170Combined sources7
Beta strandi173 – 176Combined sources4
Helixi183 – 186Combined sources4
Helixi199 – 214Combined sources16
Helixi216 – 218Combined sources3
Beta strandi220 – 230Combined sources11
Helixi232 – 242Combined sources11
Beta strandi246 – 249Combined sources4
Beta strandi251 – 257Combined sources7
Turni263 – 265Combined sources3
Helixi269 – 282Combined sources14
Beta strandi288 – 290Combined sources3
Helixi291 – 299Combined sources9
Helixi302 – 309Combined sources8
Helixi310 – 312Combined sources3
Beta strandi314 – 316Combined sources3
Beta strandi329 – 331Combined sources3
Helixi336 – 342Combined sources7
Beta strandi350 – 359Combined sources10
Helixi360 – 363Combined sources4
Turni364 – 366Combined sources3
Helixi380 – 390Combined sources11
Helixi396 – 405Combined sources10
Beta strandi409 – 411Combined sources3
Helixi415 – 430Combined sources16
Helixi432 – 443Combined sources12
Turni444 – 446Combined sources3
Beta strandi449 – 454Combined sources6
Helixi465 – 467Combined sources3
Turni471 – 474Combined sources4
Helixi475 – 478Combined sources4
Helixi481 – 483Combined sources3
Helixi485 – 487Combined sources3
Helixi491 – 509Combined sources19
Beta strandi511 – 514Combined sources4
Beta strandi528 – 530Combined sources3
Beta strandi533 – 539Combined sources7
Beta strandi542 – 545Combined sources4
Helixi549 – 556Combined sources8
Helixi558 – 565Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QWWX-ray2.70A/B32-566[»]
ProteinModelPortaliQ92035.
SMRiQ92035.
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)DescriptionActionsGraphical viewLength
Sequence conflicti268T → S AA sequence (PubMed:8674549).Curated1
Sequence conflicti350V → L AA sequence (PubMed:8674549).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_008215567 – 606DNIEE…RCSEL → VDPPRADRRRRSARA in isoform S. 1 PublicationAdd BLAST40

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4QWWX-ray2.70A/B32-566[»]
ProteinModelPortaliQ92035.
SMRiQ92035.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERibunfa-ACHE. AChE.
MEROPSiS09.979.

Proteomic databases

PRIDEiQ92035.

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...

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: November 2, 2016
This is version 94 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

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 one 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.