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Serpin peptidase inhibitor, clade B (ovalbumin), member 8 (HGNC Symbol)
Entrez gene summary
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 well-conserved a 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-8 (PI8; SERPINB8) 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]
Phobius predicted membrane proteins SPOCTOPUS predicted secreted proteins Predicted intracellular proteins Plasma proteins Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
P50452 [Direct mapping] Serpin B8 A0A024R2B1 [Target identity:100%; Query identity:100%] Serpin peptidase inhibitor, clade B (Ovalbumin), member 8, isoform CRA_a
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SPOCTOPUS predicted secreted proteins Predicted intracellular proteins Plasma proteins Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
