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Protein

Acetylcholinesterase

Gene

ACHE

Organism
Naja oxiana (Central Asian cobra) (Oxus cobra)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei76 – 761Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei132 – 1321Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. neurotransmitter catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase, Toxin

Keywords - Biological processi

Neurotransmitter degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ACHE
OrganismiNaja oxiana (Central Asian cobra) (Oxus cobra)
Taxonomic identifieri8657 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-SubCell
  3. plasma membrane Source: UniProtKB-SubCell
  4. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›181›181AcetylcholinesterasePRO_0000408518Add
BLAST

Post-translational modificationi

The N-terminus is blocked.By similarity

Expressioni

Tissue specificityi

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

Structurei

3D structure databases

ProteinModelPortaliQ7LZG1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Fragments.

Q7LZG1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SELKVATQTG FVRGLSLPVL AGHVSAHLGV PFAEPFLRPE PVKPGAEMWN
60 70 80 90 100
PNLNIWVPSG RVGAFXFLTV TLFGESAGAA SVGMXLLSTQ RAILQSGAPN
110 120 130 140 150
APWAQVQPAE SRFPFVPVID GEFFPLGVNK DEGSFGVPGF SKXXESLINQ
160 170 180
AVPHANDIYT DWQDQDNGGL PLTGNPTXPH N
Length:181
Mass (Da):19,255
Last modified:May 30, 2011 - v2
Checksum:i19AB68C1423C4BD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-adjacent residuesi35 – 362Curated
Non-adjacent residuesi44 – 452Curated
Non-adjacent residuesi52 – 532Curated
Non-adjacent residuesi61 – 622Curated
Non-adjacent residuesi68 – 692Curated
Non-adjacent residuesi91 – 922Curated
Non-adjacent residuesi125 – 1262Curated
Non-adjacent residuesi135 – 1362Curated
Non-adjacent residuesi151 – 1522Curated
Non-adjacent residuesi158 – 1592Curated
Non-adjacent residuesi168 – 1692Curated
Non-adjacent residuesi172 – 1732Curated
Non-terminal residuei181 – 1811

Sequence databases

PIRiA39022.
A41117.

Cross-referencesi

Sequence databases

PIRiA39022.
A41117.

3D structure databases

ProteinModelPortaliQ7LZG1.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(1989) [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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 45-52.
    Tissue: Venom.

Entry informationi

Entry nameiACES_NAJOX
AccessioniPrimary (citable) accession number: Q7LZG1
Secondary accession number(s): Q7LZ27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2011
Last sequence update: May 30, 2011
Last modified: January 6, 2015
This is version 44 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. 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.