Acetylcholinesterase 1 precursor - Caenorhabditis briggsae

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Q27459 (ACE1_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. History...

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

Documents (1) |

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:	CBG16374

Organism

Caenorhabditis briggsae [Reference proteome]

Taxonomic identifier

6238 [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	Inferred 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 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 By similarity.
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	neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell 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_function	acetylcholinesterase activity Inferred from electronic annotation. Source: EC carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
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_0000008609

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...) Potential

Glycosylation

272

N-linked (GlcNAc...) Potential

Glycosylation

486

N-linked (GlcNAc...) Potential

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

Q27459 [UniParc].

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

620

71,501

        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' referencesShow '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. 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.
RefSeq	XP_002643631.1. XM_002643585.1.
3D structure databases
ProteinModelPortal	Q27459.
ModBase	Search...
Protein-protein interaction databases
STRING	6238.CBG16374.
Protein family/group databases
MEROPS	S09.979.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	CBG16374; CBG16374; CBG16374.
GeneID	8585625.
KEGG	cbr:CBG16374.
Organism-specific databases
CTD	8585625.
WormBase	CBG16374; CBP03902; WBGene00036330; Cbr-ace-1.
Phylogenomic databases
eggNOG	COG2272.
HOGENOM	HOG000091866.
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...

Entry information

Entry name

ACE1_CAEBR

Accession

Primary (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:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

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

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents