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P37136 (ACES_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. 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·Alt products·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
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. Catalytic forms H (GPI-anchor dimer) and T (asymmetric collagen-tailed), which differ in their C-terminus, account for all types of known ACHE forms. 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 junctionsynapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.

Isoform H: Cell membrane; Lipid-anchorGPI-anchor; Extracellular side.

Tissue specificity

Has been found in central nervous system and muscle. Found in embryonic liver and spleen but not in adult liver.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetylcholine catabolic process

Inferred from direct assay PubMed 1133098PubMed 126256PubMed 14646156PubMed 16052514PubMed 2731551PubMed 334962PubMed 3655326PubMed 4008917PubMed 6854006PubMed 8737018. Source: RGD

acetylcholine metabolic process

Inferred from mutant phenotype PubMed 16628397. Source: RGD

choline metabolic process

Inferred from direct assay PubMed 1133098PubMed 8737018. Source: RGD

neuron death

Inferred from mutant phenotype PubMed 11403956. Source: RGD

positive regulation of axonogenesis

Inferred from mutant phenotype PubMed 12799140. Source: RGD

positive regulation of dendrite morphogenesis

Inferred from mutant phenotype PubMed 12799140. Source: RGD

synapse assembly

Inferred from mutant phenotype PubMed 12799140. Source: RGD

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 1133098. Source: RGD

anchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

axon

Inferred from direct assay PubMed 1133098. Source: RGD

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from direct assay PubMed 2731551. Source: RGD

cytoplasm

Inferred from direct assay PubMed 16052514. Source: RGD

dendrite

Inferred from direct assay PubMed 1133098. Source: RGD

endoplasmic reticulum lumen

Inferred from direct assay PubMed 1133098. Source: RGD

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuromuscular junction

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuron projection

Inferred from direct assay PubMed 16052514. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 1133098. Source: RGD

nuclear envelope

Inferred from direct assay PubMed 1133098. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 16052514. Source: RGD

plasma membrane

Inferred from direct assay PubMed 2731551. Source: RGD

postsynaptic membrane

Inferred from direct assay PubMed 3655326. Source: RGD

presynaptic membrane

Inferred from direct assay PubMed 3655326. Source: RGD

rough endoplasmic reticulum

Inferred from direct assay PubMed 2731551. Source: RGD

synapse

Inferred from direct assay PubMed 1133098. Source: RGD

   Molecular_functionacetylcholine binding

Inferred from direct assay PubMed 1133098PubMed 126256PubMed 14646156PubMed 2731551PubMed 3655326PubMed 4008917PubMed 8737018. Source: RGD

acetylcholinesterase activity

Inferred from direct assay PubMed 1133098PubMed 126256PubMed 14646156PubMed 16052514PubMed 2731551PubMed 334962PubMed 3655326PubMed 4008917PubMed 6854006Ref.1PubMed 8737018. Source: RGD

choline binding

Inferred from direct assay PubMed 1133098. Source: RGD

cholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform T (identifier: P37136-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform H (identifier: P37136-2)

The sequence of this isoform differs from the canonical sequence as follows:
     575-614: DTLDEAERQW...YSKQERCSDL → ATEVPCTCPS...FLLHSGLRWL
Isoform R (identifier: P37136-3)

The sequence of this isoform differs from the canonical sequence as follows:
     575-614: DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQERCSDL → GRRGVGKQGMHKAARVGRTGERKGGKHRM
Note: May be not functional.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 614583Acetylcholinesterase
PRO_0000008590

Sites

Active site2341Acyl-ester intermediate By similarity
Active site3651Charge relay system By similarity
Active site4781Charge relay system By similarity

Amino acid modifications

Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation4951N-linked (GlcNAc...) Potential
Disulfide bond100 ↔ 127 By similarity
Disulfide bond288 ↔ 303 By similarity
Disulfide bond440 ↔ 560 By similarity
Disulfide bond611Interchain By similarity

Natural variations

Alternative sequence575 – 61440DTLDE…RCSDL → ATEVPCTCPSPAHGEAAPRP GPALSLSLLFFLFLLHSGLR WL in isoform H.
VSP_001458
Alternative sequence575 – 61440DTLDE…RCSDL → GRRGVGKQGMHKAARVGRTG ERKGGKHRM in isoform R.
VSP_001459

Sequences

Sequence LengthMass (Da)Tools
Isoform T [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 2EDAE7D46282E7C0

FASTA61468,196
        10         20         30         40         50         60 
MRPPWYPLHT PSLASPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG IRLKAPGGPV 

        70         80         90        100        110        120 
SAFLGIPFAE PPVGSRRFMP PEPKRPWSGI LDATTFQNVC YQYVDTLYPG FEGTEMWNPN 

       130        140        150        160        170        180 
RELSEDCLYL NVWTPYPRPT SPTPVLIWIY GGGFYSGASS LDVYDGRFLA QVEGTVLVSM 

       190        200        210        220        230        240 
NYRVGTFGFL ALPGSREAPG NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV 

       250        260        270        280        290        300 
GMHILSLPSR SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL 

       310        320        330        340        350        360 
ISCLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPDALINTG DFQDLQVLVG 

       370        380        390        400        410        420 
VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ ASDLAAEAVV LHYTDWLHPE 

       430        440        450        460        470        480 
DPAHLRDAMS AVVGDHNVVC PVAQLAGRLA AQGARVYAYI FEHRASTLTW PLWMGVPHGY 

       490        500        510        520        530        540 
EIEFIFGLPL DPSLNYTVEE RIFAQRLMQY WTNFARTGDP NDPRDSKSPR WPPYTTAAQQ 

       550        560        570        580        590        600 
YVSLNLKPLE VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 

       610 
QFDHYSKQER CSDL 

« Hide

Isoform H [UniParc].

Checksum: DA2CB2026B1FFE38
Show »

FASTA61667,582
Isoform R [UniParc].

Checksum: 16115C6C19815CFA
Show »

FASTA60366,268

References

[1]"Cloning and expression of a rat acetylcholinesterase subunit: generation of multiple molecular forms and complementarity with a Torpedo collagenic subunit."
Legay C., Bon S., Vernier P., Coussen F., Massoulie J.
J. Neurochem. 60:337-346(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM T).
[2]"Expression of a cDNA encoding the glycolipid-anchored form of rat acetylcholinesterase."
Legay C., Bon S., Massoulie J.
FEBS Lett. 315:163-166(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H AND R).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S50879 mRNA. Translation: AAB24586.1.
X70140 mRNA. Translation: CAA49717.1.
X70141 mRNA. Translation: CAA49718.1.
PIRJH0811.
RefSeqNP_742006.1. NM_172009.1. [P37136-1]
UniGeneRn.105879.

3D structure databases

ProteinModelPortalP37136.
SMRP37136. Positions 36-608.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP37136.
ChEMBLCHEMBL3199.

Protein family/group databases

MEROPSS09.979.

Proteomic databases

PRIDEP37136.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83817.
KEGGrno:83817.

Organism-specific databases

CTD43.
RGD69313. Ache.

Phylogenomic databases

HOVERGENHBG008839.
KOK01049.
PhylomeDBP37136.

Gene expression databases

GenevestigatorP37136.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR014788. 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]
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616425.
PROP37136.

Entry information

Entry nameACES_RAT
AccessionPrimary (citable) accession number: P37136
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 102 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