Q7LZG1 (ACES_NAJOX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylcholinesterase
Short name=AChE
EC=3.1.1.7

Gene names

Name:

ACHE

Organism

Naja oxiana (Central Asian cobra) (Oxus cobra)

Taxonomic identifier

8657 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Elapinae › Naja

Protein attributes

Sequence length	181 AA.
Sequence status	Fragments.
Protein existence	Evidence 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 junction › synapse. 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 process	Neurotransmitter degradation
Cellular component	Cell junction Cell membrane Membrane Secreted Synapse
Molecular function	Hydrolase Serine esterase Toxin
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell 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_function	acetylcholinesterase activity Inferred from electronic annotation. Source: EC carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›181	›181	Acetylcholinesterase		PRO_0000408518
Sites
	Active site	76	1	Acyl-ester intermediate By similarity
	Active site	132	1	Charge relay system By similarity
Experimental info
	Non-adjacent residues	35 – 36	2
	Non-adjacent residues	44 – 45	2
	Non-adjacent residues	52 – 53	2
	Non-adjacent residues	61 – 62	2
	Non-adjacent residues	68 – 69	2
	Non-adjacent residues	91 – 92	2
	Non-adjacent residues	125 – 126	2
	Non-adjacent residues	135 – 136	2
	Non-adjacent residues	151 – 152	2
	Non-adjacent residues	158 – 159	2
	Non-adjacent residues	168 – 169	2
	Non-adjacent residues	172 – 173	2
	Non-terminal residue	1	1
	Non-terminal residue	181	1

Sequences

	Sequence		Length	Mass (Da)
	Q7LZG1 [UniParc]. Last modified May 31, 2011. Version 2. Checksum: 19AB68C1423C4BD2	FASTA	181	19,255
	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

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
PIR	A39022. A41117.
3D structure databases
HSSP	HSSP built from PDB template 1EA5 based on UniProtKB P04058.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002018. CarbesteraseB. [Graphical view]
Pfam	PF00135. COesterase. 1 hit. [Graphical view]
PROSITE	PS00122. CARBOXYLESTERASE_B_1. Partial match. PS00941. CARBOXYLESTERASE_B_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACES_NAJOX

Accession

Primary (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:	April 3, 2013
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program