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P38433

- ACE1_CAEEL

UniProt

P38433 - ACE1_CAEEL

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Protein
Acetylcholinesterase 1
Gene
ace-1, W09B12.1
Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei216 – 2161Acyl-ester intermediate By similarity
Active sitei346 – 3461Charge relay system By similarity
Active sitei468 – 4681Charge relay system By similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: WormBase
  2. cholinesterase activity Source: RefGenome
  3. identical protein binding Source: WormBase

GO - Biological processi

  1. acetylcholine catabolic process Source: WormBase
  2. acetylcholine catabolic process in synaptic cleft Source: WormBase
  3. choline metabolic process Source: RefGenome
  4. regulation of locomotion Source: WormBase
  5. synaptic transmission, cholinergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

ReactomeiREACT_183754. Synthesis of PC.

Protein family/group databases

MEROPSiS09.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase 1 (EC:3.1.1.7)
Short name:
AChE 1
Gene namesi
Name:ace-1
ORF Names:W09B12.1
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome X

Organism-specific databases

WormBaseiW09B12.1; CE07569; WBGene00000035; ace-1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cell Source: WormBase
  2. cell junction Source: UniProtKB-KW
  3. extracellular region Source: WormBase
  4. membrane Source: WormBase
  5. plasma membrane Source: UniProtKB-SubCell
  6. synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131 Reviewed prediction
Add
BLAST
Chaini32 – 620589Acetylcholinesterase 1
PRO_0000008610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
Disulfide bondi82 ↔ 109 By similarity
Disulfide bondi270 ↔ 286 By similarity
Glycosylationi272 – 2721N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi430 ↔ 558 By similarity
Glycosylationi486 – 4861N-linked (GlcNAc...)1 Publication
Glycosylationi536 – 5361N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi618 – 618Interchain By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP38433.
PRIDEiP38433.

Expressioni

Developmental stagei

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

Interactioni

Subunit structurei

Oligomer composed of disulfide-linked homodimers By similarity.

Protein-protein interaction databases

STRINGi6239.W09B12.1.1.

Structurei

3D structure databases

ProteinModelPortaliP38433.
SMRiP38433. Positions 19-571.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00740000115241.
HOGENOMiHOG000091866.
InParanoidiP38433.
KOiK01049.
OMAiWEAFADI.
PhylomeDBiP38433.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00878. CHOLNESTRASE.
ProDomiPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38433-1 [UniParc]FASTAAdd to Basket

« Hide

MRNSLLFFIF LPSTILAVDL IHLHDGSPLF GEEVLSQTGK PLTRFQGIPF    50
AEPPVGNLRF KKPKPKQPWR IPLNATTPPN SCIQSEDTYF GDFYGSTMWN 100
ANTKLSEDCL YLNVYVPGKV DPNKKLAVMV WVYGGGFWSG TATLDVYDGR 150
ILTVEENVIL VAMNYRVSIF GFLYMNRPEA PGNMGMWDQL LAMKWVHKNI 200
DLFGGDLSRI TLFGESAGAA SVSIHMLSPK SAPYFHRAII QSGSATSPWA 250
IEPRDVALAR AVILYNAMKC GNMSLINPDY DRILDCFQRA DADALRENEW 300
APVREFGDFP WVPVVDGDFL LENAQTSLKQ GNFKKTQLLA GSNRDESIYF 350
LTYQLPDIFP VADFFTKTDF IKDRQLWIKG VKDLLPRQIL KCQLTLAAVL 400
HEYEPQDLPV TPRDWINAMD KMLGDYHFTC SVNEMALAHT KHGGDTYYYY 450
FTHRASQQTW PEWMGVLHGY EINFIFGEPL NQKRFNYTDE ERELSNRFMR 500
YWANFAKTGD PNKNEDGSFT QDVWPKYNSV SMEYMNMTVE SSYPSMKRIG 550
HGPRRKECAF WKAYLPNLMA AVADVGDPYL VWKQQMDKWQ NEYITDWQYH 600
FEQYKRYQTY RQSDSETCGG 620
Length:620
Mass (Da):71,433
Last modified:October 1, 1994 - v1
Checksum:i61D78C4899F55C65
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75331 mRNA. Translation: CAA53080.1.
FO081067 Genomic DNA. Translation: CCD68912.1.
PIRiA54413.
T29347.
RefSeqiNP_510660.1. NM_078259.6.
UniGeneiCel.19718.

Genome annotation databases

EnsemblMetazoaiW09B12.1.1; W09B12.1.1; WBGene00000035.
W09B12.1.2; W09B12.1.2; WBGene00000035.
GeneIDi181706.
KEGGicel:CELE_W09B12.1.
UCSCiW09B12.1.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75331 mRNA. Translation: CAA53080.1 .
FO081067 Genomic DNA. Translation: CCD68912.1 .
PIRi A54413.
T29347.
RefSeqi NP_510660.1. NM_078259.6.
UniGenei Cel.19718.

3D structure databases

ProteinModelPortali P38433.
SMRi P38433. Positions 19-571.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6239.W09B12.1.1.

Protein family/group databases

MEROPSi S09.979.

Proteomic databases

PaxDbi P38433.
PRIDEi P38433.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai W09B12.1.1 ; W09B12.1.1 ; WBGene00000035 .
W09B12.1.2 ; W09B12.1.2 ; WBGene00000035 .
GeneIDi 181706.
KEGGi cel:CELE_W09B12.1.
UCSCi W09B12.1.1. c. elegans.

Organism-specific databases

CTDi 181706.
WormBasei W09B12.1 ; CE07569 ; WBGene00000035 ; ace-1.

Phylogenomic databases

eggNOGi COG2272.
GeneTreei ENSGT00740000115241.
HOGENOMi HOG000091866.
InParanoidi P38433.
KOi K01049.
OMAi WEAFADI.
PhylomeDBi P38433.

Enzyme and pathway databases

Reactomei REACT_183754. Synthesis of PC.

Miscellaneous databases

NextBioi 915022.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00878. CHOLNESTRASE.
ProDomi PD415333. AChE_tetra. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiACE1_CAEEL
AccessioniPrimary (citable) accession number: P38433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: September 3, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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