PCSK6

From Wikipedia, the free encyclopedia

Proprotein convertase subtilisin/kexin type 6

Identifiers

PCSK6; PACE4; SPC4

External IDs

OMIM: 167405 MGI: 102897 HomoloGene: 20569

Gene ontology
Molecular Function:	• subtilase activity • calcium ion binding • peptidase activity
Cellular Component:	• endoplasmic reticulum
Biological Process:	• proteolysis • cell-cell signaling • zygotic determination of anterior/posterior axis, embryo • determination of left/right symmetry

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

XM_001130900 (mRNA)
XP_001130900 (protein)

XM_355911 (mRNA)
XP_355911 (protein)

Location

Chr 15: 99.66 - 99.85 Mb

Chr 7: 65.74 - 65.93 Mb

Pubmed search

[1]

[2]

Proprotein convertase subtilisin/kexin type 6, also known as PCSK6, is a human gene.^[1]

The protein encoded by this gene belongs to the subtilisin-like proprotein convertase family. The members of this family are proprotein convertases that process latent precursor proteins into their biologically active products. This encoded protein is a calcium-dependent serine endoprotease that can cleave precursor protein at their paired basic amino acid processing sites. Some of its substrates are - transforming growth factor beta related proteins, proalbumin, and von Willebrand factor. This gene is thought to play a role in tumor progression. Alternatively spliced transcript variants encoding different isoforms have been identified.^[1]

[edit] References

^ ^a ^b Entrez Gene: PCSK6 proprotein convertase subtilisin/kexin type 6.

[edit] Further reading

Bassi DE, Mahloogi H, Klein-Szanto AJ (2000). "The proprotein convertases furin and PACE4 play a significant role in tumor progression.". Mol. Carcinog. 28 (2): 63–9. PMID 10900462.
Moulard M, Decroly E (2001). "Maturation of HIV envelope glycoprotein precursors by cellular endoproteases.". Biochim. Biophys. Acta 1469 (3): 121–32. PMID 11063880.
Seidah NG, Prat A (2003). "Precursor convertases in the secretory pathway, cytosol and extracellular milieu.". Essays Biochem. 38: 79–94. PMID 12463163.
Kiefer MC, Tucker JE, Joh R, et al. (1992). "Identification of a second human subtilisin-like protease gene in the fes/fps region of chromosome 15.". DNA Cell Biol. 10 (10): 757–69. PMID 1741956.
Tsuji A, Higashine K, Hine C, et al. (1994). ""Identification of novel cDNAs encoding human kexin-like protease, PACE4 isoforms.".". Biochem. Biophys. Res. Commun. 204 (3): 1381–2. PMID 7980617.
Tsuji A, Higashine K, Hine C, et al. (1994). "Identification of novel cDNAs encoding human kexin-like protease, PACE4 isoforms.". Biochem. Biophys. Res. Commun. 200 (2): 943–50. doi:10.1006/bbrc.1994.1541. PMID 8179631.
Vollenweider F, Benjannet S, Decroly E, et al. (1996). "Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases.". Biochem. J. 314 ( Pt 2): 521–32. PMID 8670066.
Zhong M, Benjannet S, Lazure C, et al. (1997). "Functional analysis of human PACE4-A and PACE4-C isoforms: identification of a new PACE4-CS isoform.". FEBS Lett. 396 (1): 31–6. PMID 8906861.
Decroly E, Wouters S, Di Bello C, et al. (1997). "Identification of the paired basic convertases implicated in HIV gp160 processing based on in vitro assays and expression in CD4(+) cell lines.". J. Biol. Chem. 271 (48): 30442–50. PMID 8940009.
Inocencio NM, Sucic JF, Moehring JM, et al. (1997). "Endoprotease activities other than furin and PACE4 with a role in processing of HIV-I gp160 glycoproteins in CHO-K1 cells.". J. Biol. Chem. 272 (2): 1344–8. PMID 8995442.
Mori K, Kii S, Tsuji A, et al. (1997). "A novel human PACE4 isoform, PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus.". J. Biochem. 121 (5): 941–8. PMID 9192737.
Tsuji A, Hine C, Tamai Y, et al. (1997). "Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease.". J. Biochem. 122 (2): 438–52. PMID 9378725.
Moulard M, Chaloin L, Canarelli S, et al. (1998). "Retroviral envelope glycoprotein processing: structural investigation of the cleavage site.". Biochemistry 37 (13): 4510–7. doi:10.1021/bi972662f. PMID 9521771.
Nagahama M, Taniguchi T, Hashimoto E, et al. (1998). "Biosynthetic processing and quaternary interactions of proprotein convertase SPC4 (PACE4).". FEBS Lett. 434 (1-2): 155–9. PMID 9738469.
Viale A, Ortola C, Hervieu G, et al. (1999). "Cellular localization and role of prohormone convertases in the processing of pro-melanin concentrating hormone in mammals.". J. Biol. Chem. 274 (10): 6536–45. PMID 10037747.
Mori K, Imamaki A, Nagata K, et al. (1999). "Subtilisin-like proprotein convertases, PACE4 and PC8, as well as furin, are endogenous proalbumin convertases in HepG2 cells.". J. Biochem. 125 (3): 627–33. PMID 10050053.
Sucic JF, Moehring JM, Inocencio NM, et al. (1999). "Endoprotease PACE4 is Ca2+-dependent and temperature-sensitive and can partly rescue the phenotype of a furin-deficient cell strain.". Biochem. J. 339 ( Pt 3): 639–47. PMID 10215603.
Tsuji A, Yoshida S, Hasegawa S, et al. (2000). "Human subtilisin-like proprotein convertase, PACE4 (SPC4) gene expression is highly regulated through E-box elements in HepG2 and GH4C1 cells.". J. Biochem. 126 (3): 494–502. PMID 10467164.