SERPINE2

Today, SERPINE2 has gained unprecedented relevance in various areas, whether in the world of work, in everyday life or in the academic field. Its influence has become palpable in practically all aspects of our society, generating a significant impact on the way we relate, work and function in the digital environment. This is why it is vitally important to understand and analyze in a deep and critical way the role that SERPINE2 plays in our daily lives, as well as the challenges and opportunities that its presence entails. In this article, we will explore the different aspects related to SERPINE2 and how its presence continues to have a relevant impact on today's society.

Protein-coding gene in the species Homo sapiens

SERPINE2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4DY0, 4DY7
Identifiers
Aliases	SERPINE2, GDN, GDNPF, PI-7, PI7, PN-1, PN1, PNI, serpin family E member 2
External IDs	OMIM: 177010; MGI: 101780; HomoloGene: 21247; GeneCards: SERPINE2; OMA:SERPINE2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q36.1 Start 223,975,045 bp[1] End 224,039,318 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1 C4|1 40.97 cM Start 79,771,914 bp[2] End 79,838,897 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in decidua cartilage tissue stromal cell of endometrium ventral tegmental area tibia paraflocculus of cerebellum spinal ganglia external globus pallidus trigeminal ganglion superior vestibular nucleus Top expressed in seminal vesicula tunica media of zone of aorta calvaria stroma of bone marrow cumulus cell olfactory epithelium tibiofemoral joint body of femur ventral tegmental area ciliary body More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding glycosaminoglycan binding peptidase inhibitor activity heparin binding serine-type endopeptidase inhibitor activity signaling receptor binding Cellular component extracellular vesicle extrinsic component of external side of plasma membrane platelet alpha granule extracellular matrix cytosol neuromuscular junction extracellular region extracellular space collagen-containing extracellular matrix Biological process negative regulation of phosphatidylinositol 3-kinase signaling negative regulation of cell growth seminal vesicle epithelium development secretory granule organization innervation mating plug formation nervous system development detection of mechanical stimulus involved in sensory perception multicellular organism development regulation of cell migration long-term potentiation regulation of timing of cell differentiation cell differentiation negative regulation of proteolysis negative regulation of protein catabolic process negative regulation of plasminogen activation cerebellar granular layer morphogenesis negative regulation of cell population proliferation secretion by cell negative regulation of sodium ion transport negative regulation of smoothened signaling pathway negative regulation of protein processing positive regulation of astrocyte differentiation negative regulation of platelet activation response to wounding regulation of synaptic transmission, glutamatergic negative regulation of peptidase activity negative regulation of blood coagulation blood coagulation negative regulation of platelet aggregation negative regulation of endopeptidase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5270 20720 Ensembl ENSG00000135919 ENSMUSG00000026249 UniProt P07093 Q07235 RefSeq (mRNA) NM_001136528 NM_001136530 NM_006216 NM_009255 RefSeq (protein) NP_001130000 NP_001130002 NP_006207 NP_033281 Location (UCSC) Chr 2: 223.98 – 224.04 Mb Chr 1: 79.77 – 79.84 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Glia-derived nexin is a protein that in humans is encoded by the SERPINE2 gene.^[5][6]

See also

• Serpin

References

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000135919 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000026249 – 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. ^ Carter RE, Cerosaletti KM, Burkin DJ, Fournier RE, Jones C, Greenberg BD, Citron BA, Festoff BW (Oct 1995). "The gene for the serpin thrombin inhibitor (PI7), protease nexin I, is located on human chromosome 2q33-q35 and on syntenic regions in the mouse and sheep genomes". Genomics. 27 (1): 196–9. doi:10.1006/geno.1995.1025. PMID 7665170.
6. ^ "Entrez Gene: SERPINE2 serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 2".

Further reading

• Naldini L, Tamagnone L, Vigna E, et al. (1993). "Extracellular proteolytic cleavage by urokinase is required for activation of hepatocyte growth factor/scatter factor". EMBO J. 11 (13): 4825–33. doi:10.1002/j.1460-2075.1992.tb05588.x. PMC 556958. PMID 1334458.
• Gloor S, Odink K, Guenther J, et al. (1987). "A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins". Cell. 47 (5): 687–93. doi:10.1016/0092-8674(86)90511-8. PMID 2877744. S2CID 35327577.
• Sommer J, Gloor SM, Rovelli GF, et al. (1988). "cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily". Biochemistry. 26 (20): 6407–10. doi:10.1021/bi00394a016. PMID 3427015.
• Scott RW, Bergman BL, Bajpai A, et al. (1985). "Protease nexin. Properties and a modified purification procedure". J. Biol. Chem. 260 (11): 7029–34. doi:10.1016/S0021-9258(18)88883-4. PMID 3997857.
• Magnaldo T, Bernerd F, Darmon M (1995). "Galectin-7, a human 14-kDa S-lectin, specifically expressed in keratinocytes and sensitive to retinoic acid". Dev. Biol. 168 (2): 259–71. doi:10.1006/dbio.1995.1078. PMID 7729568.
• Donovan FM, Vaughan PJ, Cunningham DD (1994). "Regulation of protease nexin-1 target protease specificity by collagen type IV". J. Biol. Chem. 269 (25): 17199–205. doi:10.1016/S0021-9258(17)32540-1. PMID 8006028.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Nykjaer A, Conese M, Christensen EI, et al. (1997). "Recycling of the urokinase receptor upon internalization of the uPA:serpin complexes". EMBO J. 16 (10): 2610–20. doi:10.1093/emboj/16.10.2610. PMC 1169872. PMID 9184208.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Li Y, Lu YY (2002). "Applying a highly specific and reproducible cDNA RDA method to clone garlic up-regulated genes in human gastric cancer cells". World J. Gastroenterol. 8 (2): 213–6. doi:10.3748/wjg.v8.i2.213. PMC 4658353. PMID 11925594.
• Grabham PW, Monard D, Gallimore PH, Grand RJ (1991). "Modulation of Human Neurite Outgrowth by Serine Proteases: A Comparison of the Interaction of Thrombin and Prothrombin with Glia-Derived Nexin". The European Journal of Neuroscience. 3 (7): 663–668. doi:10.1111/j.1460-9568.1991.tb00852.x. PMID 12106474. S2CID 216379.
• Crisp RJ, Knauer MF, Knauer DJ (2003). "Protease nexin 1 is a potent urinary plasminogen activator inhibitor in the presence of collagen type IV". J. Biol. Chem. 277 (49): 47285–91. doi:10.1074/jbc.M204813200. PMID 12356769.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Petrovic D, Milanez T, Kobal J, et al. (2003). "Prothrombotic gene polymorphisms and atherothrombotic cerebral infarction". Acta Neurol. Scand. 108 (2): 109–13. doi:10.1034/j.1600-0404.2003.00126.x. PMID 12859287. S2CID 25978032.
• Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Sci. 13 (10): 2819–24. doi:10.1110/ps.04682504. PMC 2286551. PMID 15340161.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Kim JA, Tran ND, Li Z, et al. (2006). "Brain endothelial hemostasis regulation by pericytes". J. Cereb. Blood Flow Metab. 26 (2): 209–17. doi:10.1038/sj.jcbfm.9600181. PMID 16015279.
• Navaneetham D, Jin L, Pandey P, et al. (2006). "Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2". J. Biol. Chem. 280 (43): 36165–75. doi:10.1074/jbc.M504990200. PMID 16085935.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

External links

• The MEROPS online database for peptidases and their inhibitors: I04.021
• SERPINE2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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