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Target intelligence / Profile preview
Serpin family A member 11 (SERPINA11)
- Target
- SERPINA11
- Molecular classification
- Enzyme inhibitor, Serpin, Serine protease inhibitor, Clade A serpin (alpha-1 antiproteinase/antitrypsin family)
01
Overview
Serpin family A member 11 (SERPINA11) encodes a predicted extracellular serine protease inhibitor of the serpin superfamily, featuring a canonical serpin fold (3 β-sheets, 8-9 α-helices) and a reactive center loop typical of suicide (irreversible) protease inhibitors. The human protein sequence is ~422 amino acids with ~47 kDa molecular weight and shares 41% homology with the classical alpha-1 antitrypsin serpin (SERPINA1). While general functions of serpins include regulation of proteolytic cascades in coagulation, immune response, and inflammation, direct biological roles and disease associations for SERPINA11 remain poorly characterized with evidence mainly limited to rare genetic disorders. No drugs or clinical biomarker applications are currently available.
- Other names
- Serpin A11SERPINA11Antiproteinase-like 2Serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 11Serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 11
02
Mechanism of action
Not applicable; no drugs or direct modulators targeting SERPINA11 have been reported.
03
Biological functions
Protease inhibition (specifically inhibition of serine-type endopeptidases)Predicted to function in the extracellular regionOther possible functions shared by the serpin family include modulation of proteolytic cascades related to coagulation and inflammation, but exact functions of SERPINA11 are not well characterized
04
Disease associations
Genetic deficiency in SERPINA11 has been associated with a novel perinatal lethal serpinopathy, but this is rare and barely described in literatureRelated to Alpha-1-antitrypsin deficiency and Pericardial effusion by annotation proximity, but direct involvement is not establishedOther serpins can be involved in conformational diseases (“serpinopathies”) such as emphysema, thrombosis, and dementia, but SERPINA11-specific roles remain unclear
05
Safety considerations
Unknown in the clinical setting; safety challenges of the serpin family include risk of misfolding and polymerization, leading to "serpinopathies," but these are theoretical for SERPINA11Null mutations or instability could lead to rare, severe, and potentially lethal disease states, as in the case of the described perinatal lethal disorder, but such reports are extremely rare
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