Dermatopontin (DPT) is a secreted, tyrosine-rich acidic extracellular matrix (ECM) glycoprotein that plays key roles in ECM organization and cell-matrix interactions. DPT accelerates collagen and fibronectin fibrillogenesis and functionally interacts with decorin and TGF-beta to modulate matrix assembly and growth factor activity. It promotes cell adhesion and migration through engagement of integrin alpha3beta1, particularly important in keratinocyte migration during wound re-epithelialization. DPT is highly expressed in dermis and dermal fibroblasts, with negligible expression in epidermis, consistent with a paracrine role where dermal DPT promotes keratinocyte function. Recent studies show Dpt+ fibroblasts serve as a dominant fibroblast population that supplies CSF1 to maintain dermal macrophage subsets essential for skin homeostasis and wound healing. DPT also has tumor suppressor activity in breast cancer through direct binding to YAP and inhibition of Hippo signaling.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0030199 collagen fibril organization | IBA GO_REF:0000033 | ACCEPT | Summary: DPT promotes collagen fibrillogenesis as a core function. Deep research confirms DPT accelerates collagen and fibronectin fibrillogenesis and interacts with decorin and TGF-beta to modulate matrix assembly. Mouse DPT deficiency causes altered collagen microfibril organization with Ehlers-Danlos-like phenotypes. Reason: Collagen fibril organization is a well-supported core function of DPT. The IBA annotation from phylogenetic inference aligns with experimental evidence from mouse knockout studies showing DPT deficiency disrupts collagen organization. UniProt also notes DPT "Accelerates collagen fibril formation, and stabilizes collagen fibrils." Supporting Evidence: PMID:39199288 The mRNA expression of the core matrisome, such as collagen 1A1 (COL1A1), decorin, and dermatopontin, is significantly reduced in aged skin compared to its young skin file:human/DPT/DPT-deep-research-falcon.md DPT promotes matrix assembly by accelerating collagen and fibronectin fibrillogenesis and functionally interacting with decorin and TGF-beta |
| GO:0007155 cell adhesion | IEA GO_REF:0000043 | ACCEPT | Summary: DPT promotes cell adhesion through integrin alpha3beta1 engagement. This is supported by functional studies showing DPT enhances adhesion and migration in keratinocytes and fibroblasts. Reason: Cell adhesion is a core function of DPT. The IEA annotation from UniProtKB keyword mapping is well-supported by experimental evidence showing DPT promotes cell adhesion via integrin alpha3beta1. UniProt states DPT "Seems to mediate adhesion by cell surface integrin binding." Supporting Evidence: PMID:25486882 Dermatopontin (DPT), a non-collagenous matrix protein highly expressed in dermis is known for its striking ability to promote cell adhesion file:human/DPT/DPT-deep-research-falcon.md DPT enhances adhesion and migration via integrin alpha3beta1 engagement in keratinocytes and fibroblasts, supporting cell-matrix interactions during re-epithelialization |
| GO:0005515 protein binding | IPI PMID:30082873 Insights into the structure and dynamics of lysyl oxidase pr... | REMOVE | Summary: The IPI annotation indicates DPT binds to LOX propeptide (P28300-PRO_0000018520) based on IntAct curation. PMID:30082873 discusses LOX propeptide interactions and mentions that dermatopontin binds to mature LOX. While the interaction is likely valid, the term "protein binding" is uninformative for annotation purposes. Reason: GO:0005515 (protein binding) is too vague to be informative. DPT has specific functional interactions with decorin, TGF-beta, collagens, and integrins that are more meaningfully captured by process annotations. The interaction with LOX is mentioned in PMID:30082873 but the generic "protein binding" term does not convey the biological significance of this interaction in ECM assembly and crosslinking. Supporting Evidence: PMID:30082873 Several LOX-PP partners such as fibrillar collagen I45, elastin10, fibronectin23, dermatopontin46,47, and fibromodulin48 bind to mature LOX, suggesting that both mature LOX and the propeptide are involved in ECM assembly and organization |
| GO:0005201 extracellular matrix structural constituent | IEA GO_REF:0000107 | ACCEPT | Summary: DPT functions as a structural component of the ECM that modulates matrix organization through interactions with collagen, decorin, and other matrix components. Reason: This is a core molecular function of DPT. As a secreted ECM glycoprotein that promotes collagen/fibronectin fibrillogenesis and modulates matrix assembly through interactions with decorin and TGF-beta, DPT clearly functions as an ECM structural constituent. The IEA from Ensembl Compara is well-supported by the literature. Supporting Evidence: file:human/DPT/DPT-deep-research-falcon.md DPT promotes matrix assembly by accelerating collagen and fibronectin fibrillogenesis |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: PMID:28675934 is a proteomics study characterizing ECM of normal and diseased tissues that identified DPT as an ECM component. Reason: The RCA annotation is consistent with DPT's established role as an ECM structural protein. Proteomics detection in ECM preparations supports this function. Supporting Evidence: PMID:28675934 Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: High-throughput proteomic analysis confirmed DPT localization to the ECM. Reason: ECM localization is well-established for DPT. UniProt annotation states "Secreted, extracellular space, extracellular matrix." This HDA annotation from proteomics supports the known localization. Supporting Evidence: UniProt:Q07507 SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix PMID:28675934 Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | ACCEPT | Summary: PMID:27068509 is a proteomics study of ECM remodeling in varicose veins that detected DPT as an ECM component. Reason: Consistent with DPT's role as an ECM structural constituent. Duplicate annotations with different evidence sources are acceptable. Supporting Evidence: PMID:27068509 Apr 11. Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: PMID:27559042 is a glycoproteomics study of atrial fibrillation that detected DPT along with decorin and other ECM components. Reason: Consistent with DPT's role as an ECM structural constituent. Supporting Evidence: PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. |
| GO:0005201 extracellular matrix structural constituent | ISS GO_REF:0000024 | ACCEPT | Summary: ISS annotation transferred from bovine DPT (UniProtKB:P45846) based on sequence similarity and curator judgment. Reason: The ISS annotation is well-supported. Bovine and human DPT are orthologs with conserved ECM structural function. |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: PMID:20551380 is a proteomics study of human aorta extracellular space that identified DPT as an ECM component. Reason: Consistent with DPT's established role as an ECM structural constituent. Supporting Evidence: PMID:20551380 2010 Jun 15. Proteomics characterization of extracellular space components in the human aorta. |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: PMID:25037231 is a proteomics study of colon cancer ECM that detected DPT. Reason: Consistent with DPT's role as an ECM structural constituent. Supporting Evidence: PMID:25037231 Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. |
| GO:0031012 extracellular matrix | HDA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: Proteomics detection of DPT in ECM preparations from colon cancer tissues. Reason: Supports established ECM localization of DPT. Supporting Evidence: PMID:25037231 Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver. |
| GO:0031012 extracellular matrix | HDA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | ACCEPT | Summary: Proteomics detection of DPT in ECM of varicose veins. Reason: Supports established ECM localization of DPT. Supporting Evidence: PMID:27068509 Apr 11. Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. |
| GO:0031012 extracellular matrix | HDA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: Proteomics detection of DPT in ECM from atrial tissue. Reason: Supports established ECM localization of DPT. Supporting Evidence: PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation. |
| GO:0005615 extracellular space | HDA PMID:20551380 Proteomics characterization of extracellular space component... | MODIFY | Summary: Proteomics detection of DPT in extracellular space of human aorta. GO:0005615 (extracellular space) is obsolete; use GO:0005576 (extracellular region) instead. Reason: DPT is a secreted protein localized to the extracellular space. UniProt confirms "SUBCELLULAR LOCATION: Secreted, extracellular space." However, GO:0005615 (extracellular space) is obsolete and should be replaced with GO:0005576 (extracellular region). Proposed replacements: extracellular region Supporting Evidence: UniProt:Q07507 SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix PMID:20551380 2010 Jun 15. Proteomics characterization of extracellular space components in the human aorta. |
| GO:0031012 extracellular matrix | HDA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: Proteomics detection of DPT in ECM of human aorta. Reason: Supports established ECM localization of DPT. Supporting Evidence: PMID:20551380 2010 Jun 15. Proteomics characterization of extracellular space components in the human aorta. |
| GO:0031012 extracellular matrix | ISS PMID:22261194 Proteomics analysis of cardiac extracellular matrix remodeli... | ACCEPT | Summary: PMID:22261194 is a proteomics study of cardiac ECM remodeling in a porcine model of ischemia/reperfusion that detected DPT in the ECM. The ISS indicates transfer from porcine DPT. Reason: Supports established ECM localization. Cross-species conservation of ECM localization is expected for this conserved ECM protein family. Supporting Evidence: PMID:22261194 Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury. |
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