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ADAMTS-like protein 1 (ADAMTSL1)
- Target
- ADAMTSL1
- Molecular classification
- Extracellular matrix glycoprotein, ADAMTS-like family (a disintegrin and metalloproteinase with thrombospondin motif-like protein), Immunoglobulin superfamily domain containing
01
Overview
ADAMTS-like protein 1 (ADAMTSL1), also known as punctin-1, is a "secreted extracellular matrix glycoprotein" and member of the ADAMTS–like family that lacks metalloproteinase and disintegrin-like domains but contains multiple thrombospondin type 1 repeats and immunoglobulin-like domains. It participates in extracellular matrix assembly and microfibril organization, with its function and proper secretion dependent on specific post-translational modifications, including C-mannosylation and O-fucosylation. Pathogenic variants in ADAMTSL1 can cause multisystem developmental disorders, with evidence suggesting roles in ocular, craniofacial, and various connective tissue manifestations. While the protein is involved in extracellular matrix biology, it is not an established therapeutic target such as a druggable receptor, enzyme, or transporter[1][2][3][4].
- Other names
- ADAMTS-like protein 1ADAMTSL1ADAMTSR1C9orf94UNQ528/PRO1071ADAMTSL-1FLJ35283Punctin-1punctinpunctin-1PUNCTINADAM-TS related protein 1
02
Biological functions
Extracellular matrix organization and assemblyMicrofibril organizationPossible modulation of extracellular matrix remodeling through substrate sheddingPost-translational modification-dependent protein secretion
03
Disease associations
Developmental disorders (e.g., congenital glaucoma, craniofacial/dental, auditory, brain, renal, and limb anomalies)Connective tissue disordersTumor aggressiveness (role in cancer progression is suggested but not well established)Immune disorders (e.g., systemic lupus erythematosus based on locus association)
04
Safety considerations
Genetic mutations may result in dominant negative effects, impacting protein secretion and potentially leading to multisystem developmental phenotypesDisruption of post-translational modifications (C-mannosylation, O-fucosylation) can cause intracellular protein retention/dysfunction
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