SERPINB10

Serpin peptidase inhibitor, clade B (ovalbumin), member 10 is a protein that in humans is encoded by the SERPINB10 gene.[5]

SERPINB10
Identifiers
Aliases	SERPINB10, PI-10, PI10, serpin family B member 10
External IDs	OMIM: 602058 MGI: 2138648 HomoloGene: 68430 GeneCards: SERPINB10
Gene location (Human) Chr. Chromosome 18 (human)[1] Band 18q22.1 Start 63,897,174 bp[1] End 63,936,111 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 E2.1 Start 107,529,003 bp[2] End 107,549,271 bp[2]
Gene ontology Molecular function • peptidase inhibitor activity • serine-type endopeptidase inhibitor activity Cellular component • cytoplasm • extracellular • cell membrane • secretory granule membrane • ficolin-1-rich granule membrane • cell nucleus Biological process • negative regulation of peptidase activity • negative regulation of endopeptidase activity • neutrophil degranulation • negative regulation of apoptotic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5273	241197
Ensembl	ENSG00000242550	ENSMUSG00000092572
UniProt	P48595	Q8K1K6
RefSeq (mRNA)	NM_005024	NM_001160307 NM_198028
RefSeq (protein)	NP_005015	NP_001153779 NP_932145
Location (UCSC)	Chr 18: 63.9 – 63.94 Mb	Chr 1: 107.53 – 107.55 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6] 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.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000242550 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000092572 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Serpin peptidase inhibitor, clade B (ovalbumin), member 10".
6. Huber R, Carrell RW (November 1989). "Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins". Biochemistry. 28 (23): 8951–66. doi:10.1021/bi00449a001. PMID 2690952.
7. • Bartuski AJ, Kamachi Y, Schick C, Overhauser J, Silverman GA (August 1997). "Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3". Genomics. 43 (3): 321–8. doi:10.1006/geno.1997.4827. PMID 9268635.

Further reading

• Chuang TL, Schleef RR (April 1999). "Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10". The Journal of Biological Chemistry. 274 (16): 11194–8. doi:10.1074/jbc.274.16.11194. PMID 10196205.
• Lindskog C, Korsgren O, Pontén F, Eriksson JW, Johansson L, Danielsson A (May 2012). "Novel pancreatic beta cell-specific proteins: antibody-based proteomics for identification of new biomarker candidates". Journal of Proteomics. 75 (9): 2611–20. doi:10.1016/j.jprot.2012.03.008. PMID 22465717.
• Schleef RR, Chuang TL (August 2000). "Protease inhibitor 10 inhibits tumor necrosis factor alpha -induced cell death. Evidence for the formation of intracellular high M(r) protease inhibitor 10-containing complexes". The Journal of Biological Chemistry. 275 (34): 26385–9. doi:10.1074/jbc.C000389200. PMID 10871600.
• Przygodzka P, Ramstedt B, Tengel T, Larsson G, Wilczynska M (April 2010). "Bomapin is a redox-sensitive nuclear serpin that affects responsiveness of myeloid progenitor cells to growth environment". BMC Cell Biology. 11: 30. doi:10.1186/1471-2121-11-30. PMC 2874763. PMID 20433722.
• Shioji G, Ezura Y, Nakajima T, Ohgaki K, Fujiwara H, Kubota Y, Ichikawa T, Inoue K, Shuin T, Habuchi T, Ogawa O, Nishimura T, Emi M (2005). "Nucleotide variations in genes encoding plasminogen activator inhibitor-2 and serine proteinase inhibitor B10 associated with prostate cancer". Journal of Human Genetics. 50 (10): 507–15. doi:10.1007/s10038-005-0285-1. PMID 16172807.
• Riewald M, Schleef RR (November 1995). "Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow". The Journal of Biological Chemistry. 270 (45): 26754–7. doi:10.1074/jbc.270.45.26754. PMID 7592909.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.