Reviewed, UniProtKB/Swiss-Prot Q29499 (ACES_RABIT)

Names and origin

Protein names

Recommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7

Gene names

Name:

ACHE

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	584 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.
Subunit structure	Homotetramer; composed of disulfide-linked homodimers. Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers By similarity.
Subcellular location	Cell junction › synapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.
Miscellaneous	Synapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes. This is the catalytic subunit of an asymmetric or soluble form of ACHE.
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
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
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-SubCell extracellular region 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 cholinesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	‹1	›1	Potential
	Chain	2 – 584	583	Acetylcholinesterase		PRO_0000008589
Sites
	Active site	204	1	Acyl-ester intermediate By similarity
	Active site	335	1	Charge relay system By similarity
	Active site	448	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	266	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Glycosylation	465	1	N-linked (GlcNAc...) Potential
	Disulfide bond	70 ↔ 97		By similarity
	Disulfide bond	258 ↔ 273		By similarity
	Disulfide bond	410 ↔ 530		By similarity
	Disulfide bond	581		Interchain By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q29499-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 2AE157F3063649FE	FASTA	584	64,630
	10 20 30 40 50 60 AEGREDPELL VTVRGGRLRG LRLKAPGGPV SAFLGIPFEE PPVGPRRFLP PEPKRPWAGV 70 80 90 100 110 120 LDATAFQSVC YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPT SPTPVLVWIY 130 140 150 160 170 180 GGGFYSGASS LDVYYGRFLV QAEGTVLVAM NYRVGAFGFT CLPGSREAPG NVGLLDQRLA 190 200 210 220 230 240 LQWVQENVAA FGGDPASVTL FGESAGAASV GLHLLSPPSR GLFHRAVLQS GAPNGPWATV 250 260 270 280 290 300 GVGEARRRAT LLARLVVCPP GGAGGNDTEL VACLRTRPAQ DLVDHEWRVL PQESIFRFSF 310 320 330 340 350 360 VPVVDGDFLS DTPEALINAG DFQGLQVLVG VVKDEGTYFL VYGAPGFSKD NESFISRAQF 370 380 390 400 410 420 LAGVRVGVPQ ASDLAAEAVV LHYTDWLHPE DPARLRDALS DVVGDHNVVC PVAQLAGRLA 430 440 450 460 470 480 AQGARVYAYV FEHRASTLSW PLWMGVPHGY EIEFIFGLPL EPSLNYTEEE RIFAQRLMRY 490 500 510 520 530 540 WANFARTGDP NEPRDAKAPQ WPPYTAGAQQ YVSLNLRPLE VRRGLRAQAC AFWNRFLPKL 550 560 570 580 LSATDTLDEA ERQWKAEFHR WSSYMVHWKN QFDHYSKQDR CSDL

References

[1]	"Acetylcholinesterase and butyrylcholinesterase expression in adult rabbit tissues and during development." Jbilo O., L'Hermite Y., Talesa V., Toutant J.-P., Chatonnet A. Eur. J. Biochem. 225:115-124(1994) [PubMed: 7925428] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Muscle.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U05036 mRNA. Translation: AAA53235.1.
PIR	S48724.
UniGene	Ocu.2012
3D structure databases
HSSP	HSSP built from PDB template 1F8U based on UniProtKB P22303.
ModBase	Search...
Protein family/group databases
MEROPS	S09.979.
Phylogenomic databases
HOVERGEN	Q29499.
Enzyme and pathway databases
BRENDA	3.1.1.7. 255.
Family and domain databases
InterPro	IPR014788. AChE_tetra. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view]
PANTHER	PTHR11559. CarbesteraseB. 1 hit.
Pfam	PF08674. AChE_tetra. 1 hit. PF00135. COesterase. 1 hit. [Graphical view]
PRINTS	PR00878. CHOLNESTRASE.
PROSITE	PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACES_RABIT

Accession

Primary (citable) accession number: Q29499

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)