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Literature summary for 3.1.1.7 extracted from

  • Jiang, X.C.; Jiang, X.Y.; Liu, S.
    Molecular characterization and expression analysis of two acetylcholinesterase genes from the small white butterfly Pieris rapae (Lepidoptera Pieridae) (2018), J. Insect Sci., 18, 1-9 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene ace1, cloning from RNA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, Prace1 is distributed on genomic scaffold 156, Prace1 consists of three exons and two introns, quantitative real-time PCR expression analysis Pieris rapae
gene ace2, cloning from RNA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, Prace2 is distributed on genomic scaffold 430, Prace2 consists of six exons and five introns, quantitative real-time PCR expression analysis Pieris rapae

Protein Variants

Protein Variants Comment Organism
G324A naturally occuring mutation, conserved, associated with insecticide insensitivity Pieris rapae
S291G naturally occuring mutation, conserved, associated with insecticide insensitivity Pieris rapae
S431F naturally occuring mutation, conserved, associated with insecticide insensitivity Pieris rapae

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular isozyme PrAChE1 has a predicted signal peptide at its N-terminus, suggesting that the protein might be secreted into the extracellular fluid Pieris rapae
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extracellular isozyme PrAChE2 has a predicted signal peptide at their N-terminus, suggesting that the protein might be secreted into the extracellular fluid Pieris rapae
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Organism

Organism UniProt Comment Textmining
Pieris rapae A0A1U9X1Z7 i.e. Artogeia rapae, captured from an experimental cabbage (Brassica pekinensis) field in Anhui Agricultural University, Hefei, Anhui, China in May 2017
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Pieris rapae A0A385HWF0 i.e. Artogeia rapae, captured from an experimental cabbage (Brassica pekinensis) field in Anhui Agricultural University, Hefei, Anhui, China in May 2017
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Source Tissue

Source Tissue Comment Organism Textmining
head larval Pieris rapae
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larva fifth-instar larval stage Pieris rapae
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additional information isozymes Prace1 and Prace2 are highly expressed at the fifth-instar larval stage and in the larval head, and the transcriptional levels of Prace1 are significantly higher than those of Prace2 in all of the tested life stages and tissues, expression profiles of the two Prace genes at different developmental stages, overview Pieris rapae
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Subunits

Subunits Comment Organism
? x * 71700, about, isozyme PrAChE2, sequence calculation Pieris rapae
? x * 78400, about, isozyme PrAChE1, sequence calculation Pieris rapae

Synonyms

Synonyms Comment Organism
AcE1
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Pieris rapae
ACE2
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Pieris rapae
AChE
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Pieris rapae
Prace1
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Pieris rapae
Prace2
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Pieris rapae
PrAChE1
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Pieris rapae
PrAChE2
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Pieris rapae

pI Value

Organism Comment pI Value Maximum pI Value
Pieris rapae isozyme PrAChE1, sequence calculation
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5.3
Pieris rapae isozyme PrAChE1, sequence calculation
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6.1

General Information

General Information Comment Organism
evolution isozymes PrAChE1 and PrAChE2 both have features typical of AChEs, including the catalytic triad, choline-binding sites, an oxyanion hole, an acyl pocket, a peripheral anionic subsite, an FGESAG motif and 14 conserved aromatic amino acids. Phylogenetic analysis shows that Prace1 and Prace2 are clustered into two distinct groups: ace1 and ace2, respectively Pieris rapae
physiological function acetylcholinesterases (AChEs) are essential for the hydrolysis of the neurotransmitter acetylcholine and play crucial roles in the termination of neurotransmission Pieris rapae