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Literature summary for 3.1.1.32 extracted from

  • Kunduri, G.; Yuan, C.; Parthibane, V.; Nyswaner, K.; Kanwar, R.; Nagashima, K.; Britt, S.; Mehta, N.; Kotu, V.; Porterfield, M.; Tiemeyer, M.; Dolph, P.; Acharya, U.; Acharya, J.
    Phosphatidic acid phospholipase A1 mediates ER-Golgi transit of a family of G protein-coupled receptors (2014), J. Cell Biol., 206, 79-96.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene CG8552, expression of a 31-kb genomic enzyme fragment modified to carry a V5 epitope at the N-terminus, i.e. V5-N-PAPLA1, the recombinant protein is transiently expressed and fully functional in the Drosophila S2 cell line and rescues all the phenotype of a null mutant Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
additional information construction of a gene CG8552 null mutant Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Drosophila melanogaster 5829
-

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster M9MRD9 isozyme b; gene CG8552 or papla1
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Drosophila melanogaster Q9VLS7 isozyme a; gene CG8552 or papla1
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Drosophila melanogaster X2JDJ3 isozyme D; gene CG8552 or papla1
-

Source Tissue

Source Tissue Comment Organism Textmining
head
-
Drosophila melanogaster
-
male accessory gland
-
Drosophila melanogaster
-
additional information the enzyme protein shows strong colocalization with the Sec23 protein in a number of tissues, including oocyte and male accessory gland Drosophila melanogaster
-
oocyte
-
Drosophila melanogaster
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Synonyms

Synonyms Comment Organism
PAPLA1
-
Drosophila melanogaster
phosphatidic acid phospholipase A1
-
Drosophila melanogaster

General Information

General Information Comment Organism
malfunction in enzyme mutants, in the absence of transport to the Golgi, rhodopsin 1 is aberrantly glycosylated and is mislocalized. These defects lead to decreased levels of the protein and decreased sensitivity of the photoreceptors to light. Several GPCRs, including other rhodopsins and Bride of sevenless, are similarly affected, phenotypes, overview Drosophila melanogaster
physiological function the cytosolic enzyme is necessary for transit of selective transmembrane receptor cargo by the COPII coat for anterograde trafficking in Drosophila melanogaster. The enzme interacts with the coat protein II (COPII), the COPII coated vesicular system transports newly synthesized secretory and membrane proteins from the endoplasmic reticulum to the Golgi complex. The enzyme is required for the transport of rhodopsin 1, an N-glycosylated G protein-coupled receptor, from the endoplasmic reticulum to the Golgi complex, but the active site of PAPLA1 is not necessary for Rh1 maturation. The enzyme acts downstream of the rhodopsin 1 chaperone NinaA and upstream of the Golgi-resident protein dMPPE Drosophila melanogaster