The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Gene/Protein Identity: UniProt A0A8C9H4D2 | Piliocolobus tephrosceles (Ugandan red Colobus)
No published studies specifically characterize OLFML2A from Piliocolobus tephrosceles. This report therefore relies on functional annotation inferred from (1) conserved domain architecture (Olfactomedin-like domain, IPR003112, IPR050605, PF02191) documented in UniProt, and (2) experimental and bioinformatic evidence from OLFML2A orthologs in humans and cattle, as well as closely related olfactomedin family members (OLFML2B, OLFML3, OLFM2). The functional predictions presented below represent the most defensible inferences based on evolutionary conservation within the olfactomedin protein family.
OLFML2A belongs to the olfactomedin-like (OLFML) subfamily of the broader olfactomedin (OLF) protein family. The olfactomedin domain-containing protein family comprises over 200 members across diverse species and is characterized by a conserved C-terminal olfactomedin domain (approximately 250 amino acids) with distinctive structural features including signal peptides, DExGLW and CG sequences, cysteine residues, and N-glycosylation sites (wang2021olfml2bisa pages 1-4).
Based on structural homology to characterized family members, OLFML proteins typically contain:
- An N-terminal coiled-coil region (CC domain)
- A C-terminal olfactomedin-like domain (OLF domain)
The olfactomedin domain confers the capacity for protein-protein interactions and is essential for the extracellular regulatory functions of these proteins (yu2025olfml3promotesirg1 pages 1-2, toedebusch2021microgliaderivedolfactomedinlike3 pages 1-2).
OLFML2A is not an enzyme and does not possess catalytic activity or substrate specificity. Instead, it functions as a matricellular regulatory glycoprotein. Matricellular proteins are defined as secreted, extracellular proteins that modulate cell behavior by binding to structural matrix proteins, cell surface receptors, cytokines, and proteases, without directly contributing to mechanical ECM integrity (cardenasleon2022matricellularproteinsin pages 1-2).
Studies of human OLFML2A provide the most direct functional insights:
Cell Proliferation and Survival: In triple-negative breast cancer (TNBC) cells, OLFML2A silencing by shRNA significantly inhibited cell proliferation and migration while inducing apoptosis and promoting S-phase cell cycle arrest (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6). Microarray analysis revealed that OLFML2A knockdown significantly altered expression of 1,140 genes involved in DNA synthesis, chromosome alignment, microtubule dynamics, cytoskeletal organization, cell movement, cell cycle progression, and apoptosis (gao2022genechipexpressionprofiling pages 1-6).
Migration and Invasion: OLFML2A depletion decreased both migration (via wound-healing assays) and invasion (via transwell assays) of TNBC cells, implicating the protein in promoting motile and invasive cellular phenotypes (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6).
Epithelial-Mesenchymal Transition (EMT): OLFML2A knockdown suppressed EMT progression in TNBC, a critical process for cancer metastasis (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6). This is consistent with observations in the related protein OLFML2B, which promotes EMT, metastasis, and invasion in lung adenocarcinoma and squamous cell carcinoma (wang2021olfml2bisa pages 1-4).
Rather than serving as a structural scaffold, OLFML2A appears to function as a signaling mediator and regulator of cell-extracellular matrix (ECM) interactions. Related olfactomedin family proteins modulate focal adhesion pathways, axon guidance, and ECM remodeling (lluch2025defectiveolfactomedin2connects pages 1-2, cardenasleon2022matricellularproteinsin pages 1-2).
Based on family-level classification and functional studies of related proteins, OLFML2A is predicted to be secreted into the extracellular space where it associates with the extracellular matrix (ECM). This inference is supported by multiple lines of evidence:
Matricellular Protein Classification: Olfactomedin family proteins are recognized as matricellular proteins that are secreted and bind to ECM components, cell surface receptors, and other extracellular signaling molecules (cardenasleon2022matricellularproteinsin pages 1-2).
Surfaceome Evidence: In systematic surfaceome CRISPR screens designed to identify cell surface and extracellular proteins, the related protein OLFML3 was identified as a surface-associated host factor, confirming extracellular localization for this family member (mei2021surfaceomecrisprscreen pages 1-2).
Glycoprotein Characteristics: The olfactomedin domain contains conserved N-glycosylation sites, consistent with processing through the secretory pathway (yu2025olfml3promotesirg1 pages 1-2, wang2021olfml2bisa pages 1-4).
Site of Function: OLFML2A likely exerts its biological effects in the extracellular matrix, where it mediates cell-ECM interactions, influences cell surface receptor signaling, and participates in paracrine communication between cells.
OLFML2A participates in multiple interconnected signaling pathways that converge on the regulation of cell proliferation, migration, survival, and differentiation.
OLFML2A was identified as a key regulatory protein acting downstream of the AP-1 transcription factor complex in human TNBC. Specifically, OLFML2A is necessary for the anti-tumor effects of T-5224, a selective inhibitor of the c-Fos/AP-1 DNA binding activity (zhao2021olfml2aisnecessary pages 1-2, zhao2021olfml2aisnecessary pages 2-3). ChIP-qPCR analysis confirmed that AP-1 directly binds to the OLFML2A promoter, establishing OLFML2A as a direct transcriptional target of AP-1 (zhao2021olfml2aisnecessary pages 2-3). This pathway is particularly relevant in cancer contexts where AP-1 family members (including Fra-1 and c-Jun) are overexpressed and drive invasion and metastasis (zhao2021olfml2aisnecessary pages 1-2).
Gene expression profiling following OLFML2A knockdown revealed significant upregulation of G2/M DNA damage checkpoint regulation and p53 signaling pathways, indicating that OLFML2A normally suppresses these tumor-suppressive mechanisms in TNBC cells (gao2022genechipexpressionprofiling pages 1-6). OLFML2A appears to promote cell cycle progression by regulating genes involved in DNA synthesis, chromosome alignment, and microtubule organization (gao2022genechipexpressionprofiling pages 1-6).
OLFML2A depletion inhibits integrin signaling pathways, which are critical for cell-ECM adhesion, migration, and survival (gao2022genechipexpressionprofiling pages 1-6). This is consistent with the broader role of olfactomedin family proteins in mediating cell adhesion processes. Related family member OLFM2 has been shown to regulate focal adhesion and axon guidance pathways in adipocytes (lluch2025defectiveolfactomedin2connects pages 1-2).
OLFML2A knockdown suppressed hepatocyte growth factor (HGF) and nerve growth factor (NGF) signaling pathways, both of which are tumor-promoting pathways involved in cell survival, proliferation, and motility (gao2022genechipexpressionprofiling pages 1-6).
While direct mechanistic studies of OLFML2A and TGF-β were not retrieved in this literature search, a review article noted that OLFML2A is a novel TGF-β regulator that induces smooth muscle differentiation (toedebusch2021microgliaderivedolfactomedinlike3 pages 1-2). This connection is consistent with observations in related family members: OLFML3 is a direct TGF-β target gene in microglia, and OLFM2 is induced by TGF-β to drive smooth muscle cell proliferation and differentiation (toedebusch2021microgliaderivedolfactomedinlike3 pages 1-2, lluch2025defectiveolfactomedin2connects pages 1-2).
OLFML2A promotes EMT in breast cancer cells (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6). EMT is a developmental and pathological program involving loss of epithelial characteristics, acquisition of mesenchymal features, and increased migratory and invasive capacity. The related protein OLFML2B similarly promotes EMT in lung cancer (wang2021olfml2bisa pages 1-4).
The olfactomedin domain is highly conserved across vertebrate species, suggesting that functional roles identified in human and cattle OLFML2A are likely conserved in the P. tephrosceles ortholog.
In a genome-wide association study of lactation persistency and milk production traits in Holstein cattle, OLFML2A was identified as a candidate gene associated with milk fat yield (pedrosa2021genomewideassociationanalyses pages 1-2). This finding suggests a conserved role for OLFML2A in lipid metabolism and/or tissue function across mammalian species, though the precise molecular mechanism remains to be elucidated.
A genome-wide microarray study of familial Chiari malformation type I (a brain malformation) identified a missense variant in OLFML2A (rs7874348) as significantly associated with disease risk (avsar2020genomewideidentificationof pages 1-4). This provides additional evidence that OLFML2A plays a conserved physiological role in vertebrate development and tissue homeostasis.
Based on the available evidence, OLFML2A in Piliocolobus tephrosceles is predicted to be a secreted, extracellular glycoprotein belonging to the olfactomedin-like subfamily. It functions as a non-enzymatic matricellular regulatory protein that modulates cell behavior through interactions with the extracellular matrix, cell surface receptors, and signaling molecules.
High OLFML2A expression is associated with poor prognosis in triple-negative breast cancer (TNBC) patients (zhao2021olfml2aisnecessary pages 1-2). Multiple clinical databases confirm this negative prognostic association. OLFML2A has been proposed as a potential therapeutic target in TNBC, particularly in tumors with high AP-1 activity (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6). Targeting both AP-1 and OLFML2A through agents such as T-5224 may represent a synergistic therapeutic strategy for this clinically challenging breast cancer subtype (zhao2021olfml2aisnecessary pages 1-2).
Similarly, the related protein OLFML2B has been proposed as a prognostic biomarker and immunotherapy response predictor in lung adenocarcinoma and squamous cell carcinoma (wang2021olfml2bisa pages 1-4).
No species-specific data: No publications directly characterize OLFML2A from Piliocolobus tephrosceles. All functional inferences are based on mammalian orthologs.
Limited direct localization data: While family-level evidence strongly supports secreted/extracellular localization, direct experimental verification of OLFML2A subcellular localization by immunofluorescence or fractionation was not found in the retrieved literature.
Mechanism of action unclear: The precise molecular mechanisms by which OLFML2A regulates downstream signaling pathways remain incompletely understood. Identification of direct binding partners and receptors for OLFML2A would strengthen mechanistic understanding.
Context-dependent functions: Most functional studies of OLFML2A have been conducted in cancer contexts. The normal physiological roles of OLFML2A in non-transformed tissues require further investigation.
| Aspect | OLFML2A-specific evidence | Inference from related olfactomedin family members | Evidence strength / interpretation |
|---|---|---|---|
| Verified identity | Target protein is annotated in UniProt as OLFML2A from Piliocolobus tephrosceles and contains Olfactomedin-like / OLF domains; human literature also uses the same symbol/name “olfactomedin-like 2A” in breast cancer and disease-association studies (zhao2021olfml2aisnecessary pages 1-2, avsar2020genomewideidentificationof pages 1-4) | OLFML proteins are recognized as a subfamily within the broader olfactomedin family that includes OLFML1/2A/2B/3 (wang2021olfml2bisa pages 1-4) | High confidence that the queried protein belongs to the OLFML2A/olfactomedin-like family; species-specific functional data for P. tephrosceles are lacking |
| Protein family / structural domains | OLFML2A is identified as an olfactomedin-domain-containing protein in Chiari malformation genetics work (avsar2020genomewideidentificationof pages 1-4) | OLFML3 is described as a glycoprotein with an N-terminal coiled-coil region and C-terminal OLF-like domain; OLFML family proteins are glycoproteins within the OLF family, whose members share a conserved C-terminal olfactomedin domain (yu2025olfml3promotesirg1 pages 1-2, wang2021olfml2bisa pages 1-4) | Moderate confidence for domain architecture by homology; direct structural characterization for OLFML2A itself was not found |
| Molecular class | OLFML2A is treated in functional cancer studies as a regulatory protein affecting proliferation, apoptosis, migration, invasion, and EMT rather than as an enzyme or transporter (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6) | Reviews of matricellular proteins describe extracellular regulatory proteins that bind matrix proteins, receptors, cytokines, or proteases; olfactomedin-like proteins are discussed in this extracellular/matricellular context, and OLFM2 is explicitly called a pleiotropic glycoprotein and scaffold-like mediator (cardenasleon2022matricellularproteinsin pages 1-2, lluch2025defectiveolfactomedin2connects pages 1-2) | Best current interpretation: non-enzymatic glycoprotein / likely matricellular regulator rather than catalyst; no substrate-specific enzymatic activity reported |
| Enzymatic activity / substrate specificity | No evidence in the OLFML2A papers for catalytic activity, reaction chemistry, or substrate transport; studies focus on transcriptional regulation and cell phenotypes after knockdown (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6) | Related family literature likewise emphasizes signaling, adhesion, migration, immune modulation, and protein-protein interactions rather than enzyme function (yu2025olfml3promotesirg1 pages 1-2, lluch2025defectiveolfactomedin2connects pages 1-2, cardenasleon2022matricellularproteinsin pages 1-2) | High confidence that OLFML2A is not currently known as an enzyme; substrate specificity is not established |
| Subcellular localization | Direct localization for OLFML2A was not experimentally established in the retrieved OLFML2A papers; supplemental material points to Human Protein Atlas expression resources for protein distribution (gao2022genechipexpressionprofiling pages 1-6) | Matricellular proteins are secreted into the extracellular matrix; surfaceome-focused screening included extracellular/plasma-membrane-associated proteins, and OLFML3 was identified in that framework; OLFML family proteins are described as extracellular or cell-surface-associated glycoproteins (cardenasleon2022matricellularproteinsin pages 1-2, mei2021surfaceomecrisprscreen pages 1-2, wang2021olfml2bisa pages 1-4) | Moderate confidence that OLFML2A is secreted/extracellular ECM-associated by family-level inference, but direct localization evidence for this specific protein remains limited |
| Primary biological role | In triple-negative breast cancer (TNBC), OLFML2A is required for robust cell proliferation, migration, invasion, and survival; its silencing induces apoptosis, cell-cycle arrest, and suppresses EMT (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6) | Related OLF proteins regulate cell proliferation/migration and tissue remodeling: OLFML3 controls macrophage migration/phagocytosis and mitochondrial immune function, while OLFM2 regulates adipocyte differentiation and focal adhesion-related programs (yu2025olfml3promotesirg1 pages 1-2, lluch2025defectiveolfactomedin2connects pages 1-2) | Strongest evidence supports a role as a context-dependent extracellular/signaling regulator of cell behavior rather than a structural scaffold alone |
| Cell adhesion / ECM-linked functions | OLFML2A knockdown in TNBC altered pathways including integrin signaling, cytoskeleton, cell movement, and EMT-associated programs (gao2022genechipexpressionprofiling pages 1-6) | Matricellular proteins act through matrix and receptor interactions; olfactomedin family proteins are broadly linked to cell adhesion and ECM-mediated signaling; OLFM2 modulates focal adhesion pathways (cardenasleon2022matricellularproteinsin pages 1-2, lluch2025defectiveolfactomedin2connects pages 1-2) | Moderate-to-strong evidence for ECM/adhesion-linked regulatory function |
| EMT / invasion | OLFML2A silencing decreases EMT progression and reduces migration/invasion in TNBC cells (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6) | OLFML2B is associated with EMT, metastasis, immune-suppressive tumor microenvironment, and poor prognosis in lung cancer (wang2021olfml2bisa pages 1-4) | Strong cancer-context evidence that OLFML2A-family proteins can promote invasive phenotypes |
| Cell proliferation / survival | OLFML2A knockdown suppresses TNBC proliferation and promotes apoptosis; GeneChip analysis highlighted effects on DNA synthesis, chromosome alignment, microtubules, cytoskeleton, and checkpoint pathways (gao2022genechipexpressionprofiling pages 1-6) | OLFM2 deficiency impairs adipocyte differentiation and downregulates cell-cycle genes; OLFML3 affects inflammatory survival phenotypes in vivo (lluch2025defectiveolfactomedin2connects pages 1-2, yu2025olfml3promotesirg1 pages 1-2) | Strong for growth/survival regulation, especially in transformed cells |
| Signaling pathways: AP-1 | OLFML2A was identified as a key regulatory protein downstream of AP-1 in TNBC and is required for the anti-tumor effect of the AP-1 inhibitor T-5224 (zhao2021olfml2aisnecessary pages 1-2) | AP-1/Fra-1 is a major driver of EMT and metastasis in cancer broadly, fitting the OLFML2A-TNBC phenotype (zhao2021olfml2aisnecessary pages 1-2) | Strong direct evidence for AP-1-linked regulation in breast cancer |
| Signaling pathways: p53 / DNA damage checkpoint / HGF / NGF / integrin | OLFML2A knockdown was reported to activate G2/M DNA damage checkpoint regulation and p53 signaling while inhibiting integrin, HGF, NGF, and other tumor-promoting pathways in TNBC cells (gao2022genechipexpressionprofiling pages 1-6) | Related family members also connect to inflammation, migration, and extracellular communication pathways (yu2025olfml3promotesirg1 pages 1-2, wang2021olfml2bisa pages 1-4) | Moderate-to-strong evidence, but mainly from one transcriptomic perturbation study |
| Signaling pathways: TGF-beta | No direct OLFML2A-TGF-beta mechanistic paper was retrieved here | Related literature summarized in an ophthalmic review states that OLFML2A is a novel TGF-beta regulator that induces smooth muscle differentiation; OLFML3 is a direct TGF-beta target gene in microglia (toedebusch2021microgliaderivedolfactomedinlike3 pages 1-2) | Low-to-moderate confidence for OLFML2A-TGF-beta involvement within this evidence set because the direct primary study was not retrieved |
| Disease / phenotype associations | High OLFML2A expression is associated with poor prognosis in TNBC; independent genetic association studies implicate OLFML2A variants in Chiari malformation type I; cattle GWAS nominate OLFML2A as a candidate gene for milk fat yield (zhao2021olfml2aisnecessary pages 1-2, avsar2020genomewideidentificationof pages 1-4, pedrosa2021genomewideassociationanalyses pages 1-2) | Related family members are implicated in lung cancer (OLFML2B), antiviral immunity and acute lung injury (OLFML3), and obesity/adipocyte dysfunction (OLFM2) (wang2021olfml2bisa pages 1-4, yu2025olfml3promotesirg1 pages 1-2, lluch2025defectiveolfactomedin2connects pages 1-2) | Human disease association is strongest for cancer; non-cancer traits currently remain association-based rather than mechanistically resolved |
| Real-world / current applications | OLFML2A is being discussed as a potential therapeutic target and prognostic biomarker in TNBC, especially in AP-1-high disease contexts (zhao2021olfml2aisnecessary pages 1-2, gao2022genechipexpressionprofiling pages 1-6) | Family-level applications include biomarker/prognostic studies for OLFML2B in lung cancer and mechanistic targeting concepts for olfactomedin proteins in inflammation and metabolism (wang2021olfml2bisa pages 1-4, yu2025olfml3promotesirg1 pages 1-2, lluch2025defectiveolfactomedin2connects pages 1-2) | Translational potential is emerging, but no established clinical assay or approved therapy targeting OLFML2A was identified |
| Key caveat for annotation of the Ugandan red colobus protein | No publication directly characterizes A0A8C9H4D2 OLFML2A in Piliocolobus tephrosceles; therefore, functional annotation must rely primarily on conserved domain architecture and mammalian ortholog data (zhao2021olfml2aisnecessary pages 1-2, avsar2020genomewideidentificationof pages 1-4) | Family evidence consistently supports a secreted/extracellular, non-enzymatic regulatory role for OLFML proteins (yu2025olfml3promotesirg1 pages 1-2, cardenasleon2022matricellularproteinsin pages 1-2, wang2021olfml2bisa pages 1-4) | Most defensible annotation: secreted/extracellular olfactomedin-like glycoprotein involved in ECM/cell-signaling regulation, with likely roles in adhesion, migration, and proliferation |
Table: This table summarizes the best-supported characteristics of OLFML2A, combining direct evidence for OLFML2A with carefully marked family-based inferences from related olfactomedin proteins. It is useful for functional annotation because species-specific data for the Ugandan red colobus protein are limited.
This report synthesizes evidence from 11 primary sources spanning cancer biology (zhao2021olfml2aisnecessary pages 1-2, zhao2021olfml2aisnecessary pages 2-3, gao2022genechipexpressionprofiling pages 1-6, wang2021olfml2bisa pages 1-4), livestock genetics (pedrosa2021genomewideassociationanalyses pages 1-2), human disease genetics (avsar2020genomewideidentificationof pages 1-4), immunology (yu2025olfml3promotesirg1 pages 1-2, mei2021surfaceomecrisprscreen pages 1-2), metabolic biology (lluch2025defectiveolfactomedin2connects pages 1-2), matricellular protein biology (cardenasleon2022matricellularproteinsin pages 1-2), and developmental neurobiology (toedebusch2021microgliaderivedolfactomedinlike3 pages 1-2). The synthesis prioritizes authoritative primary research and recent reviews (2020-2025) as requested.
References
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