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Q27459 (ACE1_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 95. 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·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:CBG16374
OrganismCaenorhabditis briggsae [Reference proteome]
Taxonomic identifier6238 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Rapidly hydrolyzes choline released into the synapse.

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 By similarity.

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_processneurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell 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_functionacetylcholinesterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 620589Acetylcholinesterase 1
PRO_0000008609

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...) Potential
Glycosylation2721N-linked (GlcNAc...) Potential
Glycosylation4861N-linked (GlcNAc...) Potential
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
Q27459 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 69D73CD3996E11FC

FASTA62071,501
        10         20         30         40         50         60 
MRYSLLFFIF LPCVITAVDL IHLHDGSPLF GEEVLSQTGK PLTRFLGIPF AEPPIGNLRF 

        70         80         90        100        110        120 
RKPKPKQPWR IPFNATTPPN SCIQSEDTYF GDFYGSTMWN PNTKLSEDCL YLNVYVPGKV 

       130        140        150        160        170        180 
DPNKKLAVMI WVYGGGFWSG TSTLDVYDGR ILTVEENVIL VAMNYRVSIF GFLYMNRSEA 

       190        200        210        220        230        240 
PGNMGMWDQL LAMKWVHKNI DLFGGDTSRI TLFGESAGAA SVSIHMLSQK SAPYFHRAII 

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

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

       370        380        390        400        410        420 
VADFFSKSEF IKDRQTWIKG VKDLLPRQIL KCQLTLAAVL HEYEPQDLPI SAQNWLNAMD 

       430        440        450        460        470        480 
KMLGDYHFTC SVNEMALAHT KHGGDTFYYY FTHRATQQTW PEWMGVLHGY EINFIFGEPF 

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

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

       610        620 
FEQYKRYQTY RQSDSETCGG 

« Hide

References

« Hide 'large scale' references
[1]"Sequence comparison of ACE-1, the gene encoding acetylcholinesterase of class A, in the two nematodes Caenorhabditis elegans and Caenorhabditis briggsae."
Grauso M., Culetto E., Berge J.-B., Toutant J.-P., Arpagaus M.
DNA Seq. 6:217-227(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics."
Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. expand/collapse author list , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H.
PLoS Biol. 1:166-192(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AF16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U41846 Genomic DNA. Translation: AAB41269.1.
HE600961 Genomic DNA. Translation: CAP34096.1.
RefSeqXP_002643631.1. XM_002643585.1.

3D structure databases

ProteinModelPortalQ27459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6238.CBG16374.

Protein family/group databases

MEROPSS09.979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaCBG16374; CBG16374; CBG16374.
GeneID8585625.
KEGGcbr:CBG16374.

Organism-specific databases

CTD8585625.
WormBaseCBG16374; CBP03902; WBGene00036330; Cbr-ace-1.

Phylogenomic databases

eggNOGCOG2272.
HOGENOMHOG000091866.
KOK01049.
OMASFNAPWA.
OrthoDBEOG789C9R.

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...

Entry information

Entry nameACE1_CAEBR
AccessionPrimary (citable) accession number: Q27459
Secondary accession number(s): A8XNK7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 22, 2014
This is version 95 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