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; OMA:SERPINB10 - orthologs
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 107,456,757 bp[2] End 107,477,001 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in bone marrow bone marrow cells testicle monocyte trabecular bone epithelium of bronchus olfactory zone of nasal mucosa stromal cell of endometrium blood bronchial epithelial cell Top expressed in lobe of liver granulocyte epidermis esophagus zone of skin lip bone marrow spleen white adipose tissue thymus More reference expression data BioGPS n/a
Gene ontology Molecular function peptidase inhibitor activity serine-type endopeptidase inhibitor activity Cellular component cytoplasm extracellular space plasma membrane secretory granule membrane ficolin-1-rich granule membrane 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: 107.46 – 107.48 Mb PubMed search [3] [4]
Wikidata
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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, 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.