Lamp1 encodes lysosome-associated membrane glycoprotein 1 (LAMP-1, CD107a), a heavily N- and O-glycosylated single-pass type I membrane protein that is, with LAMP-2, the most abundant protein of the lysosomal and late endosomal limiting membrane. Its large luminal region of two beta-prism domains forms a glycocalyx lining the lysosome, and its short cytoplasmic tail carries a tyrosine-based lysosomal sorting signal; the protein cycles through the plasma membrane and is enriched on lysosome-related organelles such as cytolytic granules, melanosomes, phagolysosomes and autolysosomes. Its best-defined molecular activity, shown for the human orthologue, is direct inhibition of the lysosomal cation/proton leak channel TMEM175, which allows the lysosomal lumen to reach the low pH needed for hydrolase activity. Lamp1 also binds and stabilizes the lysosomal peptide transporter TAPL/ABCB9, and in natural killer cells supports perforin delivery to lytic granules and protects the cells from their own granule contents when exposed on the surface after degranulation. Lamp1-null mice are viable and fertile with near-normal lysosomes, whereas Lamp1/Lamp2 double deficiency is embryonic lethal with autophagic vacuole accumulation, indicating largely redundant functions with LAMP-2.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000421 autophagosome membrane | IDA PMID:31006538 Intrinsically Disordered Protein TEX264 Mediates ER-phagy. | UNDECIDED | Summary: Autophagosome membrane. Reason: Lamp1 is acquired by autophagosomes upon fusion with late endosomes/lysosomes, so Lamp1-positive autophagic membranes are amphisomes/autolysosomes rather than nascent autophagosomes. The cited TEX264 paper is abstract-only in cache and does not mention Lamp1, so whether the assay resolved autophagosomes from autolysosomes cannot be checked; the autolysosome row (IDA, PMID:26284655) captures the supported location. |
| GO:0000421 autophagosome membrane | IEA GO_REF:0000117 | UNDECIDED | Summary: Autophagosome membrane. Reason: Lamp1 is acquired by autophagosomes upon fusion with late endosomes/lysosomes, so Lamp1-positive autophagic membranes are amphisomes/autolysosomes rather than nascent autophagosomes. The cited TEX264 paper is abstract-only in cache and does not mention Lamp1, so whether the assay resolved autophagosomes from autolysosomes cannot be checked; the autolysosome row (IDA, PMID:26284655) captures the supported location. |
| GO:0005515 protein binding | IPI PMID:16674683 Amelogenin, a major structural protein in mineralizing ename... | REMOVE | Summary: Protein binding with amelogenin (AMELX). Reason: Bare protein binding is uninformative under the protein-binding policy; the cached abstract does not describe the interaction and no more specific function can be assigned from it. |
| GO:0005515 protein binding | IPI PMID:21194361 The lysosomal polypeptide transporter TAPL: more than a hous... | REMOVE | Summary: Protein binding with human TAPL/ABCB9 (review article). Reason: Bare protein binding is uninformative under the protein-binding policy; the TAPL interaction is captured by GO:0019904 (PMID:22641697) and protein stabilization rows. Removal does not dispute the interaction. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | MODIFY | Summary: Cytoplasm by Ensembl orthology. Reason: Cytoplasm is true but uninformative for a lysosomal membrane protein; MODIFY to lysosomal membrane (GO:0005765, part_of cytoplasm). Proposed replacements: lysosomal membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005737 cytoplasm | ISO PMID:21266579 Raftlin is involved in the nucleocapture complex to induce p... | MODIFY | Summary: Cytoplasm by orthology to a human LAMP1 IDA (raftlin study). Reason: Cytoplasm is true but uninformative for a lysosomal membrane protein; MODIFY to lysosomal membrane (GO:0005765, part_of cytoplasm). The human source used LAMP1 as an organelle marker. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P11279 · LAMP1 SUPPORTS TRANSFER Human LAMP1 cytoplasmic (organellar) staining is sound; the term is too coarse. Proposed replacements: lysosomal membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:10787428 Localization of the murine Niemann-Pick C1 protein to two di... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:10787428 a fraction of which colocalize with LAMP1-positive compartments |
| GO:0005764 lysosome | IDA PMID:11486041 Intact lysosome transport and phagosome function despite kin... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:11486041 lysosomes were localized by labeling with anti-LAMP-1 antibody |
| GO:0005764 lysosome | IDA PMID:11854359 Dynamics of major histocompatibility complex class II compar... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:11854359 enlarging class II- and Lamp 1-positive vesicles in B cells |
| GO:0005764 lysosome | IDA PMID:12925704 Impaired membrane resealing and autoimmune myositis in synap... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:12925704 indicating that both wild-type and mutated forms of Syt VII are targeted normally to lysosomes |
| GO:0005764 lysosome | IDA PMID:14627652 Emerging role for autophagy in the removal of aggresomes in ... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:14643301 Accelerated antigen presentation and elicitation of humoral ... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:15006695 Sialin expression in the CNS implicates extralysosomal funct... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:15294975 Endoplasmic reticulum-associated degradation-induced dissoci... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:15588329 Membrane trafficking and mitochondrial abnormalities precede... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:15588329 Batp1 signal exhibited some overlap with the lysosomal marker, Lamp1 |
| GO:0005764 lysosome | IDA PMID:16249233 Distribution and dynamics of Lamp1-containing endocytic orga... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:16249233 Distribution and dynamics of Lamp1-containing endocytic organelles in fibroblasts deficient in BLOC-3 |
| GO:0005764 lysosome | IDA PMID:16415873 The Unc93b1 mutation 3d disrupts exogenous antigen presentat... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:16542649 Palmitoyl protein thioesterase 1 (PPT1) deficiency causes en... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:17185018 Lysosomal accumulation of SCMAS (subunit c of mitochondrial ... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:17185018 co-localized with the lysosomal/endosomal marker, Lamp 1 |
| GO:0005764 lysosome | IDA PMID:18477453 Glypican-3 inhibits Hedgehog signaling during development by... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:23926254 Goofy coordinates the acuity of olfactory signaling. | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:23926254 Lamp-1 (lysosome marker) |
| GO:0005764 lysosome | IDA PMID:24029230 Haploinsufficiency of SAMD9L, an endosome fusion facilitator... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. The cached record is abstract-only and does not name Lamp1; the curator saw the full text, and Lamp1 lysosomal localization is independently established, so the row is accepted. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005764 lysosome | IDA PMID:24035762 Christianson syndrome protein NHE6 modulates TrkB endosomal ... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:24035762 expansion of the LAMP-1 compartment |
| GO:0005764 lysosome | IDA PMID:26432893 Novel Role of TRPML2 in the Regulation of the Innate Immune ... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:26432893 no co-localization with the lysosomal marker LAMP1 was observed |
| GO:0005764 lysosome | IDA PMID:26965651 CCC- and WASH-mediated endosomal sorting of LDLR is required... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:26965651 as well as, to some extent, in LAMP1+ lysosomes |
| GO:0005764 lysosome | IDA PMID:31637311 Loss of spatacsin impairs cholesterol trafficking and calciu... | ACCEPT | Summary: Lamp1 detected on lysosomes (Lamp1 used as lysosomal marker). Reason: Lysosome is a root organelle term and is informative (projects/ORGANELLES.md); it is kept beside the lysosomal membrane rows rather than modified. In these papers Lamp1 is used as the lysosomal marker, so the immunostaining directly shows Lamp1 in lysosomes. Supporting Evidence: PMID:31637311 Staining of cholesterol with filipin and late endosomes/lysosomes by the marker LAMP1 |
| GO:0005764 lysosome | IEA GO_REF:0000120 | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO GO_REF:0000008 | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO GO_REF:0000096 | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO GO_REF:0000119 | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO GO_REF:0000119 | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO PMID:15292400 Alfy, a novel FYVE-domain-containing protein associated with... | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO PMID:22792322 The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62,... | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO PMID:23269685 Role for phospholipid flippase complex of ATP8A1 and CDC50A ... | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005764 lysosome | ISO PMID:23704327 The giant spectrin βV couples the molecular motors to photot... | ACCEPT | Summary: Lysosome, transferred from orthologous LAMP1 or by keyword mapping. Reason: The organelle claim holds: Lamp1 is a lysosomal membrane protein in mouse (many IDA rows in this review). Lysosome is a root organelle term and is informative (projects/ORGANELLES.md). Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005765 lysosomal membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Lysosomal membrane, inherited across the LAMP family. Reason: Lamp1 is a type I transmembrane glycoprotein and one of the most abundant proteins of the lysosomal limiting membrane; this is the core location where its TMEM175-inhibitory activity acts. The PAINT node places this at the LAMP family root; Lamp1 itself (MGI:96745) is among the descendant evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000897064 · PTN000897064 SUPPORTS TRANSFER LAMP family node; LAMP1/LAMP2/LAMP3 experimental lysosomal membrane localization, including mouse Lamp1, seeds the IBD. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:27663661 are the most abundant protein components in lysosome membranes |
| GO:0005765 lysosomal membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Lysosomal membrane. Reason: Lamp1 is a type I transmembrane glycoprotein and one of the most abundant proteins of the lysosomal limiting membrane; this is the core location where its TMEM175-inhibitory activity acts. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005765 lysosomal membrane | ISO GO_REF:0000119 | ACCEPT | Summary: Lysosomal membrane. Reason: Lamp1 is a type I transmembrane glycoprotein and one of the most abundant proteins of the lysosomal limiting membrane; this is the core location where its TMEM175-inhibitory activity acts. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005765 lysosomal membrane | ISO GO_REF:0000119 | ACCEPT | Summary: Lysosomal membrane. Reason: Lamp1 is a type I transmembrane glycoprotein and one of the most abundant proteins of the lysosomal limiting membrane; this is the core location where its TMEM175-inhibitory activity acts. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005765 lysosomal membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Lysosomal membrane. Reason: Lamp1 is a type I transmembrane glycoprotein and one of the most abundant proteins of the lysosomal limiting membrane; this is the core location where its TMEM175-inhibitory activity acts. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane PMID:22147702 Large vacuoles were stained by the antibody against LAMP-1, a major component of the lysosomal membrane |
| GO:0005768 endosome | IDA PMID:10787428 Localization of the murine Niemann-Pick C1 protein to two di... | MODIFY | Summary: Lamp1 in endosomal compartments. Reason: Correct but general for a type I membrane protein; MODIFY to endosome membrane (GO:0010008, part_of endosome), which the gene already carries. Proposed replacements: endosome membrane Supporting Evidence: PMID:10787428 a fraction of which colocalize with LAMP1-positive compartments file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005768 endosome | IDA PMID:11182090 Disruption of ClC-3, a chloride channel expressed on synapti... | MODIFY | Summary: Lamp1 in endosomal compartments. Reason: Correct but general for a type I membrane protein; MODIFY to endosome membrane (GO:0010008, part_of endosome), which the gene already carries. The cached record is abstract-only; the location is independently established. Proposed replacements: endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005768 endosome | IDA PMID:31637311 Loss of spatacsin impairs cholesterol trafficking and calciu... | MODIFY | Summary: Lamp1 in endosomal compartments. Reason: Correct but general for a type I membrane protein; MODIFY to endosome membrane (GO:0010008, part_of endosome), which the gene already carries. Proposed replacements: endosome membrane Supporting Evidence: PMID:31637311 Staining of cholesterol with filipin and late endosomes/lysosomes by the marker LAMP1 file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:12446704 Small GTPase Rah/Rab34 is associated with membrane ruffles a... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:14668490 Mammalian late vacuole protein sorting orthologues participa... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: PMID:14668490 late endosomal and lysosomal compartments positive for LAMP1 or CD63 file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:15294975 Endoplasmic reticulum-associated degradation-induced dissoci... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:16249233 Distribution and dynamics of Lamp1-containing endocytic orga... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: PMID:16249233 Distribution and dynamics of Lamp1-containing endocytic organelles in fibroblasts deficient in BLOC-3 file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:16415873 The Unc93b1 mutation 3d disrupts exogenous antigen presentat... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:17620357 Slc11a1, formerly Nramp1, is expressed in dendritic cells an... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: PMID:17620357 Slc11a1 protein is expressed in DCs and localizes to Lamp1-positive vesicles file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:18477453 Glypican-3 inhibits Hedgehog signaling during development by... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IDA PMID:24841562 The late endosomal p14-MP1 (LAMTOR2/3) complex regulates foc... | MODIFY | Summary: Lamp1 on late endosomes. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: PMID:24841562 LAMP1-positive late endosomes collapse to the perinuclear region upon Arl8b knockdown file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | IEA GO_REF:0000107 | MODIFY | Summary: Late endosome by Ensembl orthology. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | ISO GO_REF:0000008 | MODIFY | Summary: Late endosome by orthology to human LAMP1. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P11279 · LAMP1 SUPPORTS TRANSFER Human LAMP1 late endosome localization is sound and transfers; only the granularity is refined. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | ISO GO_REF:0000119 | MODIFY | Summary: Late endosome by orthology to human LAMP1. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P11279 · LAMP1 SUPPORTS TRANSFER Human LAMP1 late endosome localization is sound and transfers; only the granularity is refined. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005770 late endosome | ISO PMID:15292400 Alfy, a novel FYVE-domain-containing protein associated with... | MODIFY | Summary: Late endosome by orthology to human LAMP1. Reason: Correct but general: Lamp1 is a single-pass type I membrane protein, so its late endosomal localization is in the limiting membrane. MODIFY to late endosome membrane (GO:0031902, a part_of descendant of late endosome), which the gene already carries. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P11279 · LAMP1 SUPPORTS TRANSFER Human LAMP1 late endosome localization is sound and transfers; only the granularity is refined. Proposed replacements: late endosome membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0005771 multivesicular body | IDA PMID:11854359 Dynamics of major histocompatibility complex class II compar... | KEEP AS NON CORE | Summary: Lamp1 in multivesicular MHC class II compartments of B cells. Reason: Multivesicular bodies are late endocytic compartments whose limiting membrane carries Lamp1; real, as precise as the evidence allows, non-core. Supporting Evidence: PMID:11854359 multivesicular prelysosomal compartments (early MIICs; references 4 and 5) containing lysosomal proteins |
| GO:0005771 multivesicular body | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Multivesicular body. Reason: Multivesicular bodies are late endocytic compartments whose limiting membrane carries Lamp1; real, as precise as the evidence allows, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane |
| GO:0005771 multivesicular body | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Multivesicular body by orthology to rat Lamp1. Reason: Multivesicular bodies are late endocytic compartments whose limiting membrane carries Lamp1; real, as precise as the evidence allows, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane |
| GO:0005829 cytosol | IEA GO_REF:0000108 | REMOVE | Summary: Cytosol inferred automatically from the Golgi to lysosome transport annotation. Reason: Lamp1 is a type I transmembrane protein whose bulk is luminal and whose 12-residue tail faces the cytoplasm; it is not a soluble cytosolic protein. The GO_REF:0000108 inter-ontology rule (transport process implies cytosol) is wrong for this membrane cargo, and the process row it derives from is itself over-annotated here. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0005886 plasma membrane | EXP PMID:23847195 Surface CD107a/LAMP-1 protects natural killer cells from deg... | KEEP AS NON CORE | Summary: Plasma membrane (surface CD107a). Reason: Lamp1 transits the plasma membrane and appears on the surface of NK/cytotoxic cells after granule exocytosis; real but peripheral to its lysosomal function. Supporting Evidence: PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Plasma membrane. Reason: Lamp1 transits the plasma membrane and appears on the surface of NK/cytotoxic cells after granule exocytosis; real but peripheral to its lysosomal function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000897064 · PTN000897064 SUPPORTS TRANSFER LAMP family node; surface LAMP pools are documented for several members including mouse Lamp1. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Plasma membrane (surface CD107a). Reason: Lamp1 transits the plasma membrane and appears on the surface of NK/cytotoxic cells after granule exocytosis; real but peripheral to its lysosomal function. Supporting Evidence: PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0005886 plasma membrane | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Plasma membrane (surface CD107a). Reason: Lamp1 transits the plasma membrane and appears on the surface of NK/cytotoxic cells after granule exocytosis; real but peripheral to its lysosomal function. Supporting Evidence: PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0007042 lysosomal lumen acidification | IEA GO_REF:0000107 | ACCEPT | Summary: Lysosomal lumen acidification via TMEM175 inhibition. Reason: By inhibiting TMEM175 proton leak, LAMP proteins enable the lysosomal lumen to reach a lower pH. In mouse, Lamp1 loss alone does not change lysosomal pH, consistent with LAMP-2 redundancy, so this is a shared LAMP function. Supporting Evidence: PMID:37390818 This LAMP inhibition mitigates the proton conduction of TMEM175 and facilitates lysosomal acidification to a lower pH environment crucial for optimal hydrolase activity file:mouse/Lamp1/Lamp1-uniprot.txt acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity |
| GO:0007042 lysosomal lumen acidification | ISO GO_REF:0000119 | ACCEPT | Summary: Lysosomal lumen acidification via TMEM175 inhibition. Reason: By inhibiting TMEM175 proton leak, LAMP proteins enable the lysosomal lumen to reach a lower pH. In mouse, Lamp1 loss alone does not change lysosomal pH, consistent with LAMP-2 redundancy, so this is a shared LAMP function. Supporting Evidence: PMID:37390818 This LAMP inhibition mitigates the proton conduction of TMEM175 and facilitates lysosomal acidification to a lower pH environment crucial for optimal hydrolase activity file:mouse/Lamp1/Lamp1-uniprot.txt acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity |
| GO:0007042 lysosomal lumen acidification | ISS GO_REF:0000024 | ACCEPT | Summary: Lysosomal lumen acidification via TMEM175 inhibition. Reason: By inhibiting TMEM175 proton leak, LAMP proteins enable the lysosomal lumen to reach a lower pH. In mouse, Lamp1 loss alone does not change lysosomal pH, consistent with LAMP-2 redundancy, so this is a shared LAMP function. Supporting Evidence: PMID:37390818 This LAMP inhibition mitigates the proton conduction of TMEM175 and facilitates lysosomal acidification to a lower pH environment crucial for optimal hydrolase activity file:mouse/Lamp1/Lamp1-uniprot.txt acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity |
| GO:0007283 spermatogenesis | TAS PMID:18689890 Comparative analysis of testis protein evolution in rodents. | REMOVE | Summary: Spermatogenesis, traceable author statement from a rodent testis protein evolution study. Reason: PMID:18689890 compares evolution rates of testis-expressed ESTs; the cached full text does not mention Lamp1 and makes no statement about a Lamp1 role in spermatogenesis. Lamp1-deficient mice are viable and fertile. No evidence of participation. Supporting Evidence: PMID:10212251 LAMP-1-deficient mice are viable and fertile |
| GO:0008021 synaptic vesicle | IDA PMID:15073168 AP-3-dependent mechanisms control the targeting of a chlorid... | UNDECIDED | Summary: Lamp1 reported in a synaptic vesicle context (ClC-3 targeting study). Reason: The cached record is abstract-only and does not mention Lamp1, so the assay cannot be inspected. Lamp1 is a lysosomal membrane protein and is not an established synaptic vesicle constituent; whether this row reflects genuine synaptic vesicle localization or co-fractionating endolysosomal membrane cannot be judged without the full text. |
| GO:0008200 ion channel inhibitor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Ion channel inhibitor activity toward TMEM175. Reason: LAMP proteins directly bind and inhibit the lysosomal cation/proton leak channel TMEM175, lowering lysosomal pH (shown for human LAMP-1/LAMP-2). The luminal and transmembrane regions are conserved in mouse Lamp1, and UniProt records the activity by similarity. This is the best-defined molecular activity of Lamp1. Supporting Evidence: PMID:37390818 LAMP-1 and LAMP-2 directly interact with and inhibit the activity of the lysosomal cation channel TMEM175 file:mouse/Lamp1/Lamp1-uniprot.txt acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity |
| GO:0008200 ion channel inhibitor activity | ISO GO_REF:0000119 | ACCEPT | Summary: Ion channel inhibitor activity toward TMEM175. Reason: LAMP proteins directly bind and inhibit the lysosomal cation/proton leak channel TMEM175, lowering lysosomal pH (shown for human LAMP-1/LAMP-2). The luminal and transmembrane regions are conserved in mouse Lamp1, and UniProt records the activity by similarity. This is the best-defined molecular activity of Lamp1. Supporting Evidence: PMID:37390818 LAMP-1 and LAMP-2 directly interact with and inhibit the activity of the lysosomal cation channel TMEM175 file:mouse/Lamp1/Lamp1-uniprot.txt acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity |
| GO:0008200 ion channel inhibitor activity | ISS GO_REF:0000024 | ACCEPT | Summary: Ion channel inhibitor activity toward TMEM175. Reason: LAMP proteins directly bind and inhibit the lysosomal cation/proton leak channel TMEM175, lowering lysosomal pH (shown for human LAMP-1/LAMP-2). The luminal and transmembrane regions are conserved in mouse Lamp1, and UniProt records the activity by similarity. This is the best-defined molecular activity of Lamp1. Supporting Evidence: PMID:37390818 LAMP-1 and LAMP-2 directly interact with and inhibit the activity of the lysosomal cation channel TMEM175 file:mouse/Lamp1/Lamp1-uniprot.txt acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity |
| GO:0009897 external side of plasma membrane | IDA PMID:16973387 Cellular mechanisms of fatal early-onset autoimmunity in mic... | KEEP AS NON CORE | Summary: Lamp1 (CD107a) on the external side of the T-cell plasma membrane, as a degranulation marker. Reason: Lamp1 transits the plasma membrane and appears on the surface of NK/cytotoxic cells after granule exocytosis; real but peripheral to its lysosomal function. After granule fusion the luminal domain faces the extracellular side, consistent with the type I topology. Supporting Evidence: PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein |
| GO:0009986 cell surface | IDA PMID:16674683 Amelogenin, a major structural protein in mineralizing ename... | KEEP AS NON CORE | Summary: Lamp1 detected at the cell surface. Reason: Lamp1 transits the plasma membrane and appears on the surface of NK/cytotoxic cells after granule exocytosis; real but peripheral to its lysosomal function. The cached record is abstract-only; the surface pool is independently established. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0009986 cell surface | IDA PMID:16760431 BLOC-1 complex deficiency alters the targeting of adaptor pr... | KEEP AS NON CORE | Summary: Lamp1 detected at the cell surface. Reason: Lamp1 transits the plasma membrane and appears on the surface of NK/cytotoxic cells after granule exocytosis; real but peripheral to its lysosomal function. The cached record is abstract-only; the surface pool is independently established. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0010008 endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Endosome membrane. Reason: Lamp1 cycles through endosomal membranes en route to lysosomes. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0010008 endosome membrane | ISO GO_REF:0000119 | ACCEPT | Summary: Endosome membrane. Reason: Lamp1 cycles through endosomal membranes en route to lysosomes. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0010008 endosome membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Endosome membrane. Reason: Lamp1 cycles through endosomal membranes en route to lysosomes. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0010008 endosome membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Endosome membrane. Reason: Lamp1 cycles through endosomal membranes en route to lysosomes. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0016020 membrane | IEA GO_REF:0000002 | MODIFY | Summary: Membrane from InterPro mapping. Reason: Membrane is correct but general; the specific membrane is the lysosomal membrane (GO:0005765), already carried. Proposed replacements: lysosomal membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Single-pass type I membrane protein file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0019899 enzyme binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Enzyme binding (ABCB9/TAPL) by Ensembl orthology. Reason: Lamp1 binds the ATP-binding cassette transporter TAPL/ABCB9 (an ATPase) and is reported to bind FURIN; enzyme binding is true but uninformative, and the functional consequence (TAPL stabilization) is captured by the protein stabilization rows. Non-core. Supporting Evidence: PMID:22641697 A proteomic approach allowed identification of the lysosome-associated membrane proteins LAMP-1 and LAMP-2B as the most abundant interaction partners file:mouse/Lamp1/Lamp1-uniprot.txt Interacts with ABCB9; this interaction strongly stabilizes ABCB9 and protects ABCB9 against lysosomal degradation |
| GO:0019899 enzyme binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Enzyme binding (ABCB9/TAPL) by orthology to human LAMP1. Reason: Lamp1 binds the ATP-binding cassette transporter TAPL/ABCB9 (an ATPase) and is reported to bind FURIN; enzyme binding is true but uninformative, and the functional consequence (TAPL stabilization) is captured by the protein stabilization rows. Non-core. Supporting Evidence: PMID:22641697 A proteomic approach allowed identification of the lysosome-associated membrane proteins LAMP-1 and LAMP-2B as the most abundant interaction partners file:mouse/Lamp1/Lamp1-uniprot.txt Interacts with ABCB9; this interaction strongly stabilizes ABCB9 and protects ABCB9 against lysosomal degradation |
| GO:0019904 protein domain specific binding | IPI PMID:22641697 The lysosomal polypeptide transporter TAPL is stabilized by ... | KEEP AS NON CORE | Summary: Lamp1 binds the TMD0 domain of TAPL/ABCB9. Reason: The interaction was mapped to the TMD0 domain of TAPL, so a domain-specific binding term is accurate; it underlies TAPL stabilization, a non-core function. Supporting Evidence: PMID:22641697 The interaction interface with LAMP was mapped to the four-transmembrane helices constituting the N-terminal domain of TAPL (TMD0) PMID:22641697 A proteomic approach allowed identification of the lysosome-associated membrane proteins LAMP-1 and LAMP-2B as the most abundant interaction partners |
| GO:0030425 dendrite | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: dendrite by orthology to rat Lamp1. Reason: Rat Lamp1 was observed in dendrite; Lamp1-positive lysosomes and lysosome-related organelles occur in these cellular regions in mouse as well. Peripheral context, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0030670 phagocytic vesicle membrane | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Phagocytic vesicle membrane. Reason: Maturing phagosomes acquire Lamp1 on their membrane; peripheral. Supporting Evidence: PMID:22190682 acquires LAMP1 by fusing with LAMP1-containing Golgi-derived vesicles |
| GO:0030672 synaptic vesicle membrane | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: Synaptic vesicle membrane by orthology to rat Lamp1 (SynGO). Reason: The rat source rests on synaptic vesicle fraction proteomics/imaging. Lamp1 is a lysosomal and late endosomal membrane protein; detection in vesicle fractions does not separate synaptic vesicles from co-purifying endolysosomal membranes, and no functional role on synaptic vesicles is known. Transfer of this compartment to mouse as an is_active_in claim overstates the evidence. Propagation Review Root cause: SOURCE WEAK OR INFERRED Failure modes: SOURCE EVIDENCE WEAK Sources checked: RGD:2989 · Lamp1 SOURCE WEAK OR INFERRED Rat Lamp1 SynGO EXP/IDA (PMID:17110340) is fraction-based; contamination with endolysosomal membranes not excluded. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0031902 late endosome membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Late endosome membrane. Reason: Lamp1 resides in the limiting membrane of late endosomes as well as lysosomes. Consistent with the PAINT LAMP family node. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000897064 · PTN000897064 SUPPORTS TRANSFER LAMP family node; LAMP1/LAMP2 late endosome membrane localization is experimentally supported in human and mouse. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0031902 late endosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Late endosome membrane. Reason: Lamp1 resides in the limiting membrane of late endosomes as well as lysosomes. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane |
| GO:0031902 late endosome membrane | ISO GO_REF:0000119 | ACCEPT | Summary: Late endosome membrane. Reason: Lamp1 resides in the limiting membrane of late endosomes as well as lysosomes. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane |
| GO:0031902 late endosome membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Late endosome membrane. Reason: Lamp1 resides in the limiting membrane of late endosomes as well as lysosomes. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane |
| GO:0031982 vesicle | IDA PMID:10787428 Localization of the murine Niemann-Pick C1 protein to two di... | MODIFY | Summary: Lamp1-positive vesicular compartments colocalizing with NPC1. Reason: Vesicle is uninformative; the Lamp1-positive compartments in this study are late endosomes/lysosomes. MODIFY to late endosome membrane (GO:0031902, a descendant of vesicle via cytoplasmic vesicle). Proposed replacements: late endosome membrane Supporting Evidence: PMID:10787428 a fraction of which colocalize with LAMP1-positive compartments file:mouse/Lamp1/Lamp1-uniprot.txt Late endosome membrane |
| GO:0035752 lysosomal lumen pH elevation | ISO GO_REF:0000119 | MODIFY | Summary: Lysosomal lumen pH elevation by orthology to human LAMP1. Reason: Direction is inverted. LAMP1 inhibits TMEM175 and so opposes proton leak and pH elevation; disrupting the LAMP-TMEM175 interaction alkalinizes lysosomes. The human source annotation is no longer present for P11279. Sign correction to lysosomal lumen acidification (GO:0007042), which the gene already carries. Propagation Review Root cause: SOURCE STALE OR MISSING Failure modes: REGULATORY SIGN INVERSION Sources checked: UniProtKB:P11279 · LAMP1 SOURCE STALE OR MISSING No current GO:0035752 annotation on human LAMP1 in QuickGO; the current human evidence (PMID:37390818) supports acidification, the opposite sign. Proposed replacements: lysosomal lumen acidification Supporting Evidence: PMID:37390818 This LAMP inhibition mitigates the proton conduction of TMEM175 and facilitates lysosomal acidification to a lower pH environment crucial for optimal hydrolase activity PMID:37390818 Disrupting the LAMP-TMEM175 interaction alkalinizes the lysosomal pH |
| GO:0042383 sarcolemma | IDA PMID:14506282 Dysferlin interacts with annexins A1 and A2 and mediates sar... | KEEP AS NON CORE | Summary: Lamp1 at the sarcolemma during membrane repair. Reason: Abstract-only record; lysosomal exocytosis delivers Lamp1 to the plasma membrane during wound repair, so a sarcolemmal pool is plausible and the curator saw the full text. Peripheral. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt This protein shuttles between lysosomes, endosomes, and the plasma membrane |
| GO:0042470 melanosome | IDA PMID:11266470 Rab27a regulates the peripheral distribution of melanosomes ... | KEEP AS NON CORE | Summary: Lamp1 on melanosomes in melanocytes. Reason: Lamp1 is present on melanosomes, a lysosome-related organelle; peripheral. Supporting Evidence: PMID:11266470 punctate cytoplasmic structures which also contained the melanosome-resident proteins silver and LAMP-1 |
| GO:0043025 neuronal cell body | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: neuronal cell body by orthology to rat Lamp1. Reason: Rat Lamp1 was observed in neuronal cell body; Lamp1-positive lysosomes and lysosome-related organelles occur in these cellular regions in mouse as well. Peripheral context, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0043323 positive regulation of natural killer cell degranulation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: NK-cell granule function by orthology to human LAMP1 (PMID:23632890). Reason: In NK cells LAMP1 supports perforin delivery to lytic granules and granule movement (human RNAi), and mouse Lamp1-deficient NK cells suffer degranulation-associated apoptosis. These are context-specific roles of a lysosome-related organelle protein: non-core. Supporting Evidence: PMID:23632890 LAMP1 silencing causes inhibition of NK-cell cytotoxicity PMID:23632890 Reduction of LAMP1 expression affects the movement of lytic granules and results in decreased levels of perforin, but not granzyme B, in the granules PMID:23847195 deficiency of CD107a/LAMP-1 in mice resulted in increased NK cell apoptosis upon target cell-induced degranulation |
| GO:0043323 positive regulation of natural killer cell degranulation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: NK-cell granule function by orthology to human LAMP1 (PMID:23632890). Reason: In NK cells LAMP1 supports perforin delivery to lytic granules and granule movement (human RNAi), and mouse Lamp1-deficient NK cells suffer degranulation-associated apoptosis. These are context-specific roles of a lysosome-related organelle protein: non-core. Supporting Evidence: PMID:23632890 LAMP1 silencing causes inhibition of NK-cell cytotoxicity PMID:23632890 Reduction of LAMP1 expression affects the movement of lytic granules and results in decreased levels of perforin, but not granzyme B, in the granules PMID:23847195 deficiency of CD107a/LAMP-1 in mice resulted in increased NK cell apoptosis upon target cell-induced degranulation |
| GO:0044194 cytolytic granule | IDA PMID:19915045 Impaired NK cytolytic activity and enhanced tumor growth in ... | MODIFY | Summary: Lamp1 in NK/CTL cytolytic granules. Reason: Correct but general for a transmembrane protein; MODIFY to cytolytic granule membrane (GO:0101004, part_of cytolytic granule), already carried. Abstract-only record; location independently established. Proposed replacements: cytolytic granule membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Cytolytic granule membrane PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis |
| GO:0044194 cytolytic granule | IDA PMID:32839608 The NK cell granule protein NKG7 regulates cytotoxic granule... | MODIFY | Summary: Lamp1 in NK/CTL cytolytic granules. Reason: Correct but general for a transmembrane protein; MODIFY to cytolytic granule membrane (GO:0101004, part_of cytolytic granule), already carried. Abstract-only record; location independently established. Proposed replacements: cytolytic granule membrane Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Cytolytic granule membrane PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis |
| GO:0044754 autolysosome | IDA PMID:26284655 In Vivo Evidence for Lysosome Depletion and Impaired Autopha... | KEEP AS NON CORE | Summary: Lamp1 on autolysosomes in Spg11 knockout Purkinje cells. Reason: Autolysosomes form by autophagosome-lysosome fusion and carry Lamp1; peripheral to the core activity. Supporting Evidence: PMID:26284655 the vesicular structures positive for both Lamp1 and p62 represent autolysosomes |
| GO:0045335 phagocytic vesicle | IMP PMID:22190682 Salmonella acquires lysosome-associated membrane protein 1 (... | MODIFY | Summary: Lamp1 recruited to Salmonella-containing phagosomes in macrophages. Reason: The location is real (imaging of Lamp1 on SCP), but as a transmembrane protein Lamp1 sits in the phagosome membrane: MODIFY to phagocytic vesicle membrane (GO:0030670, part_of phagocytic vesicle), which the gene also carries. The IMP code reflects Salmonella sipC and host Syntaxin6 perturbations, which cannot establish Lamp1 location; the location itself is a direct observation. Proposed replacements: phagocytic vesicle membrane Supporting Evidence: PMID:22190682 acquires LAMP1 by fusing with LAMP1-containing Golgi-derived vesicles |
| GO:0045954 positive regulation of natural killer cell mediated cytotoxicity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: NK-cell granule function by orthology to human LAMP1 (PMID:23632890). Reason: In NK cells LAMP1 supports perforin delivery to lytic granules and granule movement (human RNAi), and mouse Lamp1-deficient NK cells suffer degranulation-associated apoptosis. These are context-specific roles of a lysosome-related organelle protein: non-core. Supporting Evidence: PMID:23632890 LAMP1 silencing causes inhibition of NK-cell cytotoxicity PMID:23632890 Reduction of LAMP1 expression affects the movement of lytic granules and results in decreased levels of perforin, but not granzyme B, in the granules PMID:23847195 deficiency of CD107a/LAMP-1 in mice resulted in increased NK cell apoptosis upon target cell-induced degranulation |
| GO:0045954 positive regulation of natural killer cell mediated cytotoxicity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: NK-cell granule function by orthology to human LAMP1 (PMID:23632890). Reason: In NK cells LAMP1 supports perforin delivery to lytic granules and granule movement (human RNAi), and mouse Lamp1-deficient NK cells suffer degranulation-associated apoptosis. These are context-specific roles of a lysosome-related organelle protein: non-core. Supporting Evidence: PMID:23632890 LAMP1 silencing causes inhibition of NK-cell cytotoxicity PMID:23632890 Reduction of LAMP1 expression affects the movement of lytic granules and results in decreased levels of perforin, but not granzyme B, in the granules PMID:23847195 deficiency of CD107a/LAMP-1 in mice resulted in increased NK cell apoptosis upon target cell-induced degranulation |
| GO:0048102 autophagic cell death | ISO GO_REF:0000096 | REMOVE | Summary: Autophagic cell death by orthology to rat Lamp1. Reason: The rat source (RGD IDA, PMID:18690537) used increased lamp1 immunostaining as a marker of autophagy in dying oocytes of atretic follicles. Marker upregulation is not participation; Lamp1 executes no step of autophagic cell death. Over-propagated ISO of a marker-based source. Propagation Review Root cause: SOURCE BAD Failure modes: ROLE CONFLATION Sources checked: RGD:2989 · Lamp1 SOURCE BAD Rat Lamp1 IDA (PMID:18690537) reflects lamp1 used as an autophagy/lysosome marker in dying oocytes. Supporting Evidence: PMID:18690537 a large increase of lamp1 and acid phosphatase characteristic of autophagy |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm. Reason: Lamp1-positive late endosomes/lysosomes cluster perinuclearly; a descriptive location of its organelles, non-core. Supporting Evidence: PMID:24841562 LAMP1-positive late endosomes collapse to the perinuclear region upon Arl8b knockdown |
| GO:0048471 perinuclear region of cytoplasm | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm. Reason: Lamp1-positive late endosomes/lysosomes cluster perinuclearly; a descriptive location of its organelles, non-core. Supporting Evidence: PMID:24841562 LAMP1-positive late endosomes collapse to the perinuclear region upon Arl8b knockdown |
| GO:0048471 perinuclear region of cytoplasm | ISO PMID:16249233 Distribution and dynamics of Lamp1-containing endocytic orga... | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm. Reason: Lamp1-positive late endosomes/lysosomes cluster perinuclearly; a descriptive location of its organelles, non-core. Supporting Evidence: PMID:24841562 LAMP1-positive late endosomes collapse to the perinuclear region upon Arl8b knockdown |
| GO:0050821 protein stabilization | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Protein stabilization. Reason: Lamp1 (with LAMP-2) binds TAPL/ABCB9 and retains it on the endosomal limiting membrane; in LAMP-deficient cells TAPL half-life drops five-fold. Real, Lamp1 contributes binding/retention, but non-core and shared with LAMP-2. Supporting Evidence: PMID:22641697 in LAMP-deficient cells, the half-life of TAPL is decreased by a factor of five file:mouse/Lamp1/Lamp1-uniprot.txt Interacts with ABCB9; this interaction strongly stabilizes ABCB9 and protects ABCB9 against lysosomal degradation |
| GO:0050821 protein stabilization | IMP PMID:22641697 The lysosomal polypeptide transporter TAPL is stabilized by ... | KEEP AS NON CORE | Summary: LAMP proteins stabilize TAPL/ABCB9. Reason: Lamp1 (with LAMP-2) binds TAPL/ABCB9 and retains it on the endosomal limiting membrane; in LAMP-deficient cells TAPL half-life drops five-fold. Real, Lamp1 contributes binding/retention, but non-core and shared with LAMP-2. Supporting Evidence: PMID:22641697 in LAMP-deficient cells, the half-life of TAPL is decreased by a factor of five |
| GO:0061474 phagolysosome membrane | IDA PMID:23395172 HRG1 is essential for heme transport from the phagolysosome ... | KEEP AS NON CORE | Summary: Lamp1 on phagolysosome membranes of macrophages during erythrophagocytosis. Reason: Phagolysosomes acquire Lamp1 by fusion with lysosomes; peripheral. Supporting Evidence: PMID:23395172 Hrg1 and Lamp1 protein strongly colocalized on the phagolysosomal membrane |
| GO:0072594 establishment of protein localization to organelle | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Establishment of protein localization to organelle. Reason: LAMP1 on TGN-derived transport vesicles, with AP-1, is needed for perforin delivery to lytic granules; LAMP family proteins are themselves sorted to lysosomes. Non-core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000897064 · PTN000897064 SUPPORTS TRANSFER LAMP family node seeded by LAMP1/LAMP2 experimental data (human perforin trafficking; LAMP2 roles). Supporting Evidence: PMID:23632890 the interaction between AP-1 sorting complex and LAMP1 on the surface of the transport vesicles is important for perforin trafficking to lytic granules |
| GO:0072594 establishment of protein localization to organelle | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Establishment of protein localization to organelle (perforin to lytic granules). Reason: LAMP1 on TGN-derived transport vesicles, with AP-1, is needed for perforin delivery to lytic granules; LAMP family proteins are themselves sorted to lysosomes. Non-core. Supporting Evidence: PMID:23632890 the interaction between AP-1 sorting complex and LAMP1 on the surface of the transport vesicles is important for perforin trafficking to lytic granules file:mouse/Lamp1/Lamp1-uniprot.txt Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule |
| GO:0072594 establishment of protein localization to organelle | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Establishment of protein localization to organelle (perforin to lytic granules). Reason: LAMP1 on TGN-derived transport vesicles, with AP-1, is needed for perforin delivery to lytic granules; LAMP family proteins are themselves sorted to lysosomes. Non-core. Supporting Evidence: PMID:23632890 the interaction between AP-1 sorting complex and LAMP1 on the surface of the transport vesicles is important for perforin trafficking to lytic granules file:mouse/Lamp1/Lamp1-uniprot.txt Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule |
| GO:0090160 Golgi to lysosome transport | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Golgi to lysosome transport by Ensembl orthology. Reason: Golgi to lysosome transport is vesicle-mediated movement of material from the Golgi to the lysosome. LAMP1 is itself a cargo of this route, and being transported is not participation. Its contribution to perforin delivery (AP-1 interaction on transport vesicles) is better captured by establishment of protein localization to organelle (GO:0072594), kept as non-core. Supporting Evidence: PMID:23632890 the interaction between AP-1 sorting complex and LAMP1 on the surface of the transport vesicles is important for perforin trafficking to lytic granules |
| GO:0090160 Golgi to lysosome transport | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Golgi to lysosome transport by orthology to human LAMP1. Reason: Golgi to lysosome transport is vesicle-mediated movement of material from the Golgi to the lysosome. LAMP1 is itself a cargo of this route, and being transported is not participation. Its contribution to perforin delivery (AP-1 interaction on transport vesicles) is better captured by establishment of protein localization to organelle (GO:0072594), kept as non-core. Propagation Review Root cause: SOURCE BAD Failure modes: ROLE CONFLATION Sources checked: UniProtKB:P11279 · LAMP1 SOURCE BAD Human IMP (PMID:23632890) shows perforin mis-sorting; the term frames LAMP1 as transport machinery rather than cargo/sorting partner. Supporting Evidence: PMID:23632890 the interaction between AP-1 sorting complex and LAMP1 on the surface of the transport vesicles is important for perforin trafficking to lytic granules |
| GO:0097208 alveolar lamellar body | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: alveolar lamellar body by orthology to rat Lamp1. Reason: Rat Lamp1 was observed in alveolar lamellar body; Lamp1-positive lysosomes and lysosome-related organelles occur in these cellular regions in mouse as well. Peripheral context, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0098794 postsynapse | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: postsynapse by orthology to rat Lamp1. Reason: Rat Lamp1 was observed in postsynapse; Lamp1-positive lysosomes and lysosome-related organelles occur in these cellular regions in mouse as well. Peripheral context, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0098978 glutamatergic synapse | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: glutamatergic synapse by orthology to rat Lamp1. Reason: Rat Lamp1 was observed in glutamatergic synapse; Lamp1-positive lysosomes and lysosome-related organelles occur in these cellular regions in mouse as well. Peripheral context, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt SUBCELLULAR LOCATION: Lysosome membrane |
| GO:0101004 cytolytic granule membrane | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Cytolytic granule membrane. Reason: Cytolytic granules are lysosome-related secretory organelles of NK cells and CTLs and Lamp1 is a major membrane protein of them; context-specific, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Cytolytic granule membrane PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis |
| GO:0101004 cytolytic granule membrane | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Cytolytic granule membrane. Reason: Cytolytic granules are lysosome-related secretory organelles of NK cells and CTLs and Lamp1 is a major membrane protein of them; context-specific, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Cytolytic granule membrane PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis |
| GO:0101004 cytolytic granule membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cytolytic granule membrane. Reason: Cytolytic granules are lysosome-related secretory organelles of NK cells and CTLs and Lamp1 is a major membrane protein of them; context-specific, non-core. Supporting Evidence: file:mouse/Lamp1/Lamp1-uniprot.txt Cytolytic granule membrane PMID:23847195 the lysosomal-associated membrane proteins (LAMPs) appear on the cell surface after CG exocytosis |
| GO:0140507 granzyme-mediated programmed cell death signaling pathway | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Granzyme-mediated programmed cell death signaling pathway by Ensembl orthology. Reason: The granzyme-mediated death pathway runs in the target cell after granzyme entry. LAMP1 acts in the effector NK cell, supporting perforin loading of lytic granules and granule movement; it executes no step of the target-cell signaling pathway. The NK-cell cytotoxicity rows capture its contribution. Supporting Evidence: PMID:23632890 LAMP1 silencing causes inhibition of NK-cell cytotoxicity PMID:23632890 Reduction of LAMP1 expression affects the movement of lytic granules and results in decreased levels of perforin, but not granzyme B, in the granules |
| GO:1902513 regulation of organelle transport along microtubule | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: NK-cell granule function by orthology to human LAMP1 (PMID:23632890). Reason: In NK cells LAMP1 supports perforin delivery to lytic granules and granule movement (human RNAi), and mouse Lamp1-deficient NK cells suffer degranulation-associated apoptosis. These are context-specific roles of a lysosome-related organelle protein: non-core. Supporting Evidence: PMID:23632890 LAMP1 silencing causes inhibition of NK-cell cytotoxicity PMID:23632890 Reduction of LAMP1 expression affects the movement of lytic granules and results in decreased levels of perforin, but not granzyme B, in the granules PMID:23847195 deficiency of CD107a/LAMP-1 in mice resulted in increased NK cell apoptosis upon target cell-induced degranulation |
| GO:1902513 regulation of organelle transport along microtubule | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: NK-cell granule function by orthology to human LAMP1 (PMID:23632890). Reason: In NK cells LAMP1 supports perforin delivery to lytic granules and granule movement (human RNAi), and mouse Lamp1-deficient NK cells suffer degranulation-associated apoptosis. These are context-specific roles of a lysosome-related organelle protein: non-core. Supporting Evidence: PMID:23632890 LAMP1 silencing causes inhibition of NK-cell cytotoxicity PMID:23632890 Reduction of LAMP1 expression affects the movement of lytic granules and results in decreased levels of perforin, but not granzyme B, in the granules PMID:23847195 deficiency of CD107a/LAMP-1 in mice resulted in increased NK cell apoptosis upon target cell-induced degranulation |
| GO:1902600 proton transmembrane transport | ISO GO_REF:0000119 | MODIFY | Summary: Proton transmembrane transport by orthology to human LAMP1. Reason: Lamp1 is not a proton transporter; it binds TMEM175 and reduces its proton conduction. The relationship is regulatory (inhibitory), so the row is corrected laterally to regulation of proton transport (GO:0010155); GO has no negative-regulation child. The human source row is no longer present. Propagation Review Root cause: SOURCE STALE OR MISSING Failure modes: ROLE CONFLATION Sources checked: UniProtKB:P11279 · LAMP1 SOURCE STALE OR MISSING No current GO:1902600 annotation on human LAMP1 in QuickGO; human evidence shows inhibition of TMEM175 proton conduction, not transport by LAMP1. Proposed replacements: regulation of proton transport Supporting Evidence: PMID:37390818 This LAMP inhibition mitigates the proton conduction of TMEM175 and facilitates lysosomal acidification to a lower pH environment crucial for optimal hydrolase activity |
Loading supporting content…
Download this section (compressed HTML)Q: Does mouse Lamp1 inhibit mouse Tmem175 to the same extent as the human proteins, and why does Lamp1 loss alone leave lysosomal pH unchanged in mouse tissues (LAMP-2 compensation versus a minor contribution)?
Suggested experts: Youxing Jiang, Paul Saftig
Q: Should GO add a child of ion channel inhibitor activity for inhibition of lysosomal proton/cation leak channels, and a negative regulation of proton transport term, to describe LAMP-TMEM175 regulation precisely?
Q: Is Lamp1 a genuine synaptic vesicle membrane constituent or a co-fractionating endolysosomal contaminant in synaptic vesicle preparations?
Experiment: Measure lysosomal pH and Tmem175 currents in Lamp1/Lamp2 double-deficient mouse fibroblasts rescued with wild-type Lamp1 or Lamp1 mutants that cannot bind Tmem175, with and without Tmem175 deletion.
Hypothesis: Lamp1 lowers lysosomal pH in mouse cells through direct Tmem175 inhibition, and this activity is redundant with Lamp2.
Type: genetic rescue / lysosomal patch clamp / ratiometric pH imaging
Experiment: Compare degranulation-associated perforin binding and apoptosis of Lamp1-/- NK cells reconstituted with hinge-glycosylation mutants of Lamp1.
Hypothesis: The glycosylated hinge of surface Lamp1 shields NK cells from perforin after degranulation.
Type: NK-cell reconstitution / cytotoxicity and apoptosis assay
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)