SERPINB10

Serpin peptidase inhibitor, clade B (ovalbumin), member 10 is a is_associated_with::protein that in humans is encoded by the SERPINB10 is_associated_with::gene.

Function
The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989 [PubMed 2690952]). A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-10 (PI10; SERPINB10) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1 (MIM 107400), is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position (summary by Bartuski et al., 1997 [PubMed 9268635]).[supplied by OMIM, Jan 2010]. ##Evidence-Data-START## Transcript exon combination :: BC096217.3, U35459.1 [ECO:0000332] RNAseq introns             :: mixed/partial sample support                                ERS025084, ERS025087 [ECO:0000350] ##Evidence-Data-END##