DOLPP1 (dolichyldiphosphatase 1; dolichyl pyrophosphate phosphatase 1; EC 3.6.1.43) is a multi-pass endoplasmic reticulum membrane enzyme of the PAP2 / lipid-phosphatase superfamily. It hydrolyzes dolichyl diphosphate (dolichyl-PP) to dolichyl phosphate (dolichyl-P) plus inorganic phosphate, acting on dolichyl diphosphate at a high rate and on dolichyl monophosphate much more weakly, and does not act on phosphatidate. During N-linked protein glycosylation, the lipid-linked oligosaccharide is transferred from dolichyl-PP-oligosaccharide to nascent glycoproteins by oligosaccharyltransferase, releasing dolichyl-PP into the ER. By dephosphorylating this released dolichyl-PP, DOLPP1 regenerates the dolichyl-P glycan-carrier pool (the salvage arm of dolichyl-phosphate synthesis) and is thereby required for efficient N-glycosylation and for maintaining optimal levels of dolichol-linked oligosaccharides.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005789 endoplasmic reticulum membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Correct core localization. DOLPP1 is an ER membrane multi-pass protein and its substrate dolichyl-PP is released into the ER, so the enzyme acts in the ER membrane. Consistent with UniProt subcellular location and the four predicted TM helices. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Endoplasmic reticulum membrane |
| GO:0006487 protein N-linked glycosylation | IBA GO_REF:0000033 | ACCEPT | Summary: Correct core biological role. By recycling dolichyl-PP released after oligosaccharyl transfer, DOLPP1 regenerates the dolichyl-P carrier pool and is required for efficient N-glycosylation. Phylogenetic (IBA) support is consistent with the conserved dolichyldiphosphatase family role. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Required for efficient N-glycosylation. Necessary for |
| GO:0047874 dolichyldiphosphatase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Correct core molecular function. GO:0047874 (dolichyldiphosphatase activity) exactly matches the UniProt catalytic activity (di-trans,poly-cis-dolichyl diphosphate + H2O = di-trans,poly-cis-dolichyl phosphate + phosphate + H+; RHEA:14385; EC 3.6.1.43). This is the representative core function of the gene. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Reaction=a di-trans,poly-cis-dolichyl diphosphate + H2O = a di- |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Same correct ER membrane localization as the IBA annotation, transferred electronically from the mouse ortholog (Q9JMF7) and UniProt-SubCell. This is the gene's own correct location; the electronic support is redundant with, not in conflict with, the curated view. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Endoplasmic reticulum membrane |
| GO:0047874 dolichyldiphosphatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Same correct core molecular function as the IBA/ISS/TAS annotations, transferred electronically (with RHEA:14385 and EC:3.6.1.43 mappings from the mouse ortholog). Redundant but correct; retained as the core catalytic function. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl |
| GO:0006487 protein N-linked glycosylation | IEA GO_REF:0000107 | ACCEPT | Summary: Same correct N-glycosylation role as the IBA/ISS annotations, transferred electronically from the mouse ortholog (Q9JMF7). Redundant but correct; retained. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Required for efficient N-glycosylation. Necessary for |
| GO:0043048 dolichyl monophosphate biosynthetic process | TAS Reactome:R-HSA-446199 | ACCEPT | Summary: Appropriate. The direct product of DOLPP1 is dolichyl phosphate (dolichyl monophosphate), formed by dephosphorylation of dolichyl-PP; this salvage reaction is one route to dolichyl-P. Reactome curates DOLPP1 within the "Synthesis of dolichyl-phosphate" pathway, so this process annotation captures the enzyme's product-forming role. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Hydrolyzes dolichyl pyrophosphate at a very high rate and dolichyl |
| GO:0047874 dolichyldiphosphatase activity | TAS Reactome:R-HSA-446200 | ACCEPT | Summary: Correct core molecular function, curated by Reactome (reaction "DOLPP1 dephosphorylates DOLDP to DOLP"). Consistent with the UniProt catalytic activity and EC 3.6.1.43. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Reaction=a di-trans,poly-cis-dolichyl diphosphate + H2O = a di- |
| GO:0047874 dolichyldiphosphatase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Same correct core molecular function, inferred by sequence similarity to the mouse ortholog Q9JMF7. Redundant with the IBA/IEA/TAS calls for this term but correct; retained. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Reaction=a di-trans,poly-cis-dolichyl diphosphate + H2O = a di- |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-446200 | ACCEPT | Summary: Correct ER membrane localization, curated by Reactome. Consistent with the UniProt subcellular location and multi-pass membrane topology. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Same correct ER membrane localization, inferred by sequence similarity to the mouse ortholog Q9JMF7. Redundant with the IBA/IEA/TAS calls but correct; retained. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Endoplasmic reticulum membrane |
| GO:0006487 protein N-linked glycosylation | ISS GO_REF:0000024 | ACCEPT | Summary: Same correct N-glycosylation role, inferred by sequence similarity to the mouse ortholog Q9JMF7. Redundant with the IBA/IEA calls but correct; retained as a core biological role. Supporting Evidence: file:human/DOLPP1/DOLPP1-uniprot.txt Required for efficient N-glycosylation. Necessary for |
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