SERPINB10

Protein-coding gene in the species Homo sapiens
SERPINB10
Identifiers
AliasesSERPINB10, PI-10, PI10, serpin family B member 10
External IDsOMIM: 602058; MGI: 2138648; HomoloGene: 68430; GeneCards: SERPINB10; OMA:SERPINB10 - orthologs
Gene location (Human)
Chromosome 18 (human)
Chr.Chromosome 18 (human)[1]
Chromosome 18 (human)
Genomic location for SERPINB10
Genomic location for SERPINB10
Band18q22.1Start63,897,174 bp[1]
End63,936,111 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for SERPINB10
Genomic location for SERPINB10
Band1|1 E2.1Start107,456,757 bp[2]
End107,477,001 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 1: 107.46 – 107.48 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000242550 – Ensembl, May 2017
  2. ^ a b c 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.

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