Gene Ontology annotation through association of InterPro records with GO terms.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping.
UniProtKB entry for human PLD5 (Inactive phospholipase D5)
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Explicitly named "Inactive phospholipase D5" with caution note about lacking conserved active sites
"RecName: Full=Inactive phospholipase D5"
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Single-pass transmembrane protein, 536 amino acids
"TRANSMEM 69..89"
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Contains two PLD phosphodiesterase domains
"DOMAIN 215..242 ... PLD phosphodiesterase 1 ... DOMAIN 434..460 ... PLD phosphodiesterase 2"
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Expression enriched in brain and choroid plexus
"HPA; ENSG00000180287; Group enriched (brain, choroid plexus)."
Deep research report on PLD5 from Falcon/Edison Scientific Literature
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PLD5 lacks catalytic activity as a lipase due to missing HKD motifs
"PLD5 catalytic status: Authoritative reviews consistently report that human PLD5 lacks catalytic activity as a lipase because it lacks the requisite conserved HKD catalytic motifs; thus PLD5 is considered catalytically inactive within the classical PLD reaction framework"
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PLD5 may have non-lipase activity similar to PLD3/PLD4 which are nucleases
"some paralogs (e.g., PLD3) possess nuclease activity rather than phospholipase activity, underscoring divergent functions within the family"
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PLD5 overexpression promotes cancer cell proliferation
"PLD5 overexpression promotes proliferation, migration, invasion, and metastasis, whereas miR-145-5p mimics suppress these PLD5-driven oncogenic phenotypes"
Deep research report on PLD5 from OpenAI o3-deep-research
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PLD5 is a transmembrane protein with type II membrane topology
"PLD5 contains a short N-terminal segment, a single-pass transmembrane region, and a large C-terminal region comprising two PLD phosphodiesterase domains"
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PLD5 localizes to mitochondria in cultured cells
"Data from the Human Protein Atlas indicate PLD5 is primarily localized to mitochondria in cultured human cells"
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No enzymatic activity has been demonstrated for PLD5
"Little is known about PLD5, and it is even unclear if it is active as an enzyme"
Cyberian deep research on PLD5 function