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P38433 (ACE1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase 1

Short name=AChE 1
EC=3.1.1.7
Gene names
Name:ace-1
ORF Names:W09B12.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.

Catalytic activity

Acetylcholine + H2O = choline + acetate.

Subunit structure

Oligomer composed of disulfide-linked homodimers By similarity.

Subcellular location

Cell junctionsynapse By similarity. Secreted By similarity. Cell membrane; Peripheral membrane protein By similarity. Note: May be secreted or membrane associated via a non-catalytic subunit.

Developmental stage

Detected at all stages. Found to be more abundant in larval stages than in embryos or adults.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

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

Inferred from direct assay PubMed 10891266PubMed 7835425Ref.1. Source: WormBase

acetylcholine catabolic process in synaptic cleft

Inferred from sequence or structural similarity PubMed 10891266. Source: WormBase

choline metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of locomotion

Inferred from genetic interaction PubMed 10438595PubMed 12911746. Source: WormBase

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcell

Inferred from direct assay PubMed 10891266. Source: WormBase

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular region

Inferred from direct assay Ref.1. Source: WormBase

membrane

Inferred from direct assay Ref.1. Source: WormBase

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylcholinesterase activity

Inferred from direct assay PubMed 10891266Ref.1. Source: WormBase

cholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

identical protein binding

Inferred from physical interaction PubMed 10891266PubMed 11580201. Source: WormBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 620589Acetylcholinesterase 1
PRO_0000008610

Sites

Active site2161Acyl-ester intermediate By similarity
Active site3461Charge relay system By similarity
Active site4681Charge relay system By similarity

Amino acid modifications

Glycosylation741N-linked (GlcNAc...) Ref.3
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Ref.3
Glycosylation5361N-linked (GlcNAc...) Potential
Disulfide bond82 ↔ 109 By similarity
Disulfide bond270 ↔ 286 By similarity
Disulfide bond430 ↔ 558 By similarity
Disulfide bond618Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
P38433 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 61D78C4899F55C65

FASTA62071,433
        10         20         30         40         50         60 
MRNSLLFFIF LPSTILAVDL IHLHDGSPLF GEEVLSQTGK PLTRFQGIPF AEPPVGNLRF 

        70         80         90        100        110        120 
KKPKPKQPWR IPLNATTPPN SCIQSEDTYF GDFYGSTMWN ANTKLSEDCL YLNVYVPGKV 

       130        140        150        160        170        180 
DPNKKLAVMV WVYGGGFWSG TATLDVYDGR ILTVEENVIL VAMNYRVSIF GFLYMNRPEA 

       190        200        210        220        230        240 
PGNMGMWDQL LAMKWVHKNI DLFGGDLSRI TLFGESAGAA SVSIHMLSPK SAPYFHRAII 

       250        260        270        280        290        300 
QSGSATSPWA IEPRDVALAR AVILYNAMKC GNMSLINPDY DRILDCFQRA DADALRENEW 

       310        320        330        340        350        360 
APVREFGDFP WVPVVDGDFL LENAQTSLKQ GNFKKTQLLA GSNRDESIYF LTYQLPDIFP 

       370        380        390        400        410        420 
VADFFTKTDF IKDRQLWIKG VKDLLPRQIL KCQLTLAAVL HEYEPQDLPV TPRDWINAMD 

       430        440        450        460        470        480 
KMLGDYHFTC SVNEMALAHT KHGGDTYYYY FTHRASQQTW PEWMGVLHGY EINFIFGEPL 

       490        500        510        520        530        540 
NQKRFNYTDE ERELSNRFMR YWANFAKTGD PNKNEDGSFT QDVWPKYNSV SMEYMNMTVE 

       550        560        570        580        590        600 
SSYPSMKRIG HGPRRKECAF WKAYLPNLMA AVADVGDPYL VWKQQMDKWQ NEYITDWQYH 

       610        620 
FEQYKRYQTY RQSDSETCGG 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequence, gene structure, and in vitro expression of ace-1, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans."
Arpagaus M., Fedon Y., Cousin X., Chatonnet A., Berge J.-B., Fournier D., Toutant J.-P.
J. Biol. Chem. 269:9957-9965(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Bristol N2.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74 AND ASN-486, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75331 mRNA. Translation: CAA53080.1.
FO081067 Genomic DNA. Translation: CCD68912.1.
PIRA54413.
T29347.
RefSeqNP_510660.1. NM_078259.6.
UniGeneCel.19718.

3D structure databases

ProteinModelPortalP38433.
SMRP38433. Positions 35-571, 573-604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.W09B12.1.1.

Protein family/group databases

MEROPSS09.979.

Proteomic databases

PaxDbP38433.
PRIDEP38433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaW09B12.1.1; W09B12.1.1; W09B12.1.
W09B12.1.2; W09B12.1.2; W09B12.1.
GeneID181706.
KEGGcel:CELE_W09B12.1.
UCSCW09B12.1.1. c. elegans.

Organism-specific databases

CTD181706.
WormBaseW09B12.1; CE07569; WBGene00000035; ace-1.

Phylogenomic databases

eggNOGCOG2272.
HOGENOMHOG000091866.
InParanoidP38433.
KOK01049.
OMAWEAFADI.
PhylomeDBP38433.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF00135. 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...

Other

NextBio915022.

Entry information

Entry nameACE1_CAEEL
AccessionPrimary (citable) accession number: P38433
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase