Acetylcholinesterase 1 precursor - Caenorhabditis elegans

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P38433 (ACE1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acetylcholinesterase 1
Short name=AChE 1
EC=3.1.1.7

Gene names

Name:	ace-1
ORF Names:	W09B12.1

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	620 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 junction › synapse 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 process	Neurotransmitter degradation
Cellular component	Cell junction Cell membrane Membrane Secreted Synapse
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 10438595 PubMed 12911746. Source: WormBase
Cellular_component	cell 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_function	acetylcholinesterase activity Inferred from direct assay PubMed 10891266 Ref.1. Source: WormBase carboxylesterase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

Potential

Chain

32 – 620

589

Acetylcholinesterase 1

PRO_0000008610

Sites

Active site

216

Acyl-ester intermediate By similarity

Active site

346

Charge relay system By similarity

Active site

468

Charge relay system By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Ref.3

Glycosylation

272

N-linked (GlcNAc...) Potential

Glycosylation

486

N-linked (GlcNAc...) Ref.3

Glycosylation

536

N-linked (GlcNAc...) Potential

Disulfide bond

82 ↔ 109

By similarity

Disulfide bond

270 ↔ 286

By similarity

Disulfide bond

430 ↔ 558

By similarity

Disulfide bond

618

Interchain By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P38433 [UniParc].

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

620

71,433

        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' referencesShow '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, 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.
PIR	A54413. T29347.
RefSeq	NP_510660.1. NM_078259.6.
UniGene	Cel.19718.
3D structure databases
ProteinModelPortal	P38433.
SMR	P38433. Positions 35-571.
ModBase	Search...
Protein-protein interaction databases
STRING	6239.W09B12.1.1.
Protein family/group databases
MEROPS	S09.979.
Proteomic databases
PaxDb	P38433.
PRIDE	P38433.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	W09B12.1.1; W09B12.1.1; W09B12.1. W09B12.1.2; W09B12.1.2; W09B12.1.
GeneID	181706.
KEGG	cel:CELE_W09B12.1.
UCSC	W09B12.1.1. c. elegans.
Organism-specific databases
CTD	181706.
WormBase	W09B12.1; CE07569; WBGene00000035; ace-1.
Phylogenomic databases
eggNOG	COG2272.
GeneTree	ENSGT00700000104419.
HOGENOM	HOG000091866.
InParanoid	P38433.
KO	K01049.
OMA	GNDAFFY.
Family and domain databases
InterPro	IPR014788. AChE_tetra. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view]
Pfam	PF00135. COesterase. 1 hit. [Graphical view]
PRINTS	PR00878. CHOLNESTRASE.
ProDom	PD415333. AChE_tetra. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	915022.

Entry information

Entry name

ACE1_CAEEL

Accession

Primary (citable) accession number: P38433

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents