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Q7LZG1 (ACES_NAJOX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. 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·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
OrganismNaja oxiana (Central Asian cobra) (Oxus cobra)
Taxonomic identifier8657 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Protein attributes

Sequence length181 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.

Catalytic activity

Acetylcholine + H2O = choline + acetate.

Subcellular location

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

Tissue specificity

Expressed by the venom gland. Is also probably expressed by liver and muscle.

Post-translational modification

The N-terminus is blocked By similarity.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   Molecular functionHydrolase
Serine esterase
Toxin
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processneurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›181›181Acetylcholinesterase
PRO_0000408518

Sites

Active site761Acyl-ester intermediate By similarity
Active site1321Charge relay system By similarity

Experimental info

Non-adjacent residues35 – 362
Non-adjacent residues44 – 452
Non-adjacent residues52 – 532
Non-adjacent residues61 – 622
Non-adjacent residues68 – 692
Non-adjacent residues91 – 922
Non-adjacent residues125 – 1262
Non-adjacent residues135 – 1362
Non-adjacent residues151 – 1522
Non-adjacent residues158 – 1592
Non-adjacent residues168 – 1692
Non-adjacent residues172 – 1732
Non-terminal residue11
Non-terminal residue1811

Sequences

Sequence LengthMass (Da)Tools
Q7LZG1 [UniParc].

Last modified May 31, 2011. Version 2.
Checksum: 19AB68C1423C4BD2

FASTA18119,255
        10         20         30         40         50         60 
SELKVATQTG FVRGLSLPVL AGHVSAHLGV PFAEPFLRPE PVKPGAEMWN PNLNIWVPSG 

        70         80         90        100        110        120 
RVGAFXFLTV TLFGESAGAA SVGMXLLSTQ RAILQSGAPN APWAQVQPAE SRFPFVPVID 

       130        140        150        160        170        180 
GEFFPLGVNK DEGSFGVPGF SKXXESLINQ AVPHANDIYT DWQDQDNGGL PLTGNPTXPH 


N 

« Hide

References

[1]"The active site and partial sequence of cobra venom acetylcholinesterase."
Weise C., Kreienkamp H.J., Raba R., Aaviksaar A., Hucho F.
J. Protein Chem. 9:53-57(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-44 AND 53-181.
Tissue: Venom.
[2]"Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom."
Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F.
Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 45-52.
Tissue: Venom.

Cross-references

Sequence databases

PIRA39022.
A41117.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002018. CarbesteraseB.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_NAJOX
AccessionPrimary (citable) accession number: Q7LZG1
Secondary accession number(s): Q7LZ27
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: May 31, 2011
Last modified: February 19, 2014
This is version 39 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