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Q29499 (ACES_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetylcholinesterase
Short name=AChE
EC=3.1.1.7
Gene names
Name:ACHE
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length584 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide‹1›1 Potential
Chain2 – 584583Acetylcholinesterase
PRO_0000008589

Sites

Active site2041Acyl-ester intermediate By similarity
Active site3351Charge relay system By similarity
Active site4481Charge relay system By similarity

Amino acid modifications

Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation3511N-linked (GlcNAc...) Potential
Glycosylation4651N-linked (GlcNAc...) Potential
Disulfide bond70 ↔ 97 By similarity
Disulfide bond258 ↔ 273 By similarity
Disulfide bond410 ↔ 530 By similarity
Disulfide bond581Interchain By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q29499 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 2AE157F3063649FE

FASTA58464,630
        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

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U05036 mRNA. Translation: AAA53235.1.
PIRS48724.
UniGeneOcu.2012.

3D structure databases

ProteinModelPortalQ29499.
SMRQ29499. Positions 6-578.
ModBaseSearch...

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG008839.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACES_RABIT
AccessionPrimary (citable) accession number: Q29499
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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