Proprotein convertase subtilisin/kexin type 7
Symbols PCSK7; FLJ23503; FLJ45329; LPC; PC7; PC8; SPC7
External IDs OMIM604872 MGI107421 HomoloGene37955 GeneCards: PCSK7 Gene
EC number 3.4.21.-
RNA expression pattern
PBB GE PCSK7 203118 at tn.png
More reference expression data
Species Human Mouse
Entrez 9159 18554
Ensembl ENSG00000160613 ENSMUSG00000035382
UniProt Q16549 Q3U920
RefSeq (mRNA) NM_004716 NM_008794.2
RefSeq (protein) NP_004707 NP_032820.2
Location (UCSC) Chr 11:
117.08 – 117.1 Mb
Chr 9:
45.71 – 45.74 Mb
PubMed search [1] [2]

Proprotein convertase subtilisin/kexin type 7 is an enzyme that in humans is encoded by the PCSK7 gene.[1][2][3]

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. It is structurally related to its family members, PACE and PACE4. This protein is concentrated in the trans-Golgi network, associated with the membranes, and is not secreted. It can process proalbumin and is thought to be responsible for the activation of HIV envelope glycoproteins gp160 and gp140. This gene has been implicated in the transcriptional regulation of housekeeping genes. Multiple alternatively spliced transcripts are described for this gene but their full length nature is not yet known. Downstream of this gene's map location at 11q23-q24, nucleotides that match part of this gene's 3' end are duplicated and inverted. A translocation breakpoint associated with lymphoma occurs between this gene and its inverted counterpart.[3]


Further reading

  • Seidah NG, Chrétien M, Day R (1995). "The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions". Biochimie 76 (3–4): 197–209. doi:10.1016/0300-9084(94)90147-3. PMID 7819324. 
  • Moulard M, Decroly E (2001). "Maturation of HIV envelope glycoprotein precursors by cellular endoproteases". Biochim. Biophys. Acta 1469 (3): 121–32. doi:10.1016/S0304-4157(00)00014-9. PMID 11063880. 
  • Tsuji A, Hine C, Mori K, et al. (1994). "A novel member, PC7, of the mammalian kexin-like protease family: homology to PACE4A, its brain-specific expression and identification of isoforms". Biochem. Biophys. Res. Commun. 202 (3): 1452–9. doi:10.1006/bbrc.1994.2094. PMID 8060327. 
  • 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. 
  • Meerabux J, Yaspo ML, Roebroek AJ, et al. (1996). "A new member of the proprotein convertase gene family (LPC) is located at a chromosome translocation breakpoint in lymphomas". Cancer Res. 56 (3): 448–51. PMID 8564950. 
  • 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. doi:10.1074/jbc.271.48.30442. PMID 8940009. 
  • Hallenberger S, Moulard M, Sordel M, et al. (1997). "The role of eukaryotic subtilisin-like endoproteases for the activation of human immunodeficiency virus glycoproteins in natural host cells". J. Virol. 71 (2): 1036–45. PMC 191154. PMID 8995623. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=191154. 
  • Decroly E, Benjannet S, Savaria D, Seidah NG (1997). "Comparative functional role of PC7 and furin in the processing of the HIV envelope glycoprotein gp160". FEBS Lett. 405 (1): 68–72. doi:10.1016/S0014-5793(97)00156-7. PMID 9094426. 
  • van de Loo JW, Creemers JW, Bright NA, et al. (1997). "Biosynthesis, distinct post-translational modifications, and functional characterization of lymphoma proprotein convertase". J. Biol. Chem. 272 (43): 27116–23. doi:10.1074/jbc.272.43.27116. PMID 9341152. 
  • 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. 
  • 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. 
  • 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. 
  • Lecointe N, Meerabux J, Ebihara M, et al. (1999). "Molecular analysis of an unstable genomic region at chromosome band 11q23 reveals a disruption of the gene encoding the alpha2 subunit of platelet-activating factor acetylhydrolase (Pafah1a2) in human lymphoma". Oncogene 18 (18): 2852–9. doi:10.1038/sj.onc.1202645. PMID 10362256. 
  • Wouters S, Decroly E, Vandenbranden M, et al. (1999). "Occurrence of an HIV-1 gp160 endoproteolytic activity in low-density vesicles and evidence for a distinct density distribution from endogenously expressed furin and PC7/LPC convertases". FEBS Lett. 456 (1): 97–102. doi:10.1016/S0014-5793(99)00938-2. PMID 10452538. 
  • Bhattacharjya S, Xu P, Zhong M, et al. (2000). "Inhibitory activity and structural characterization of a C-terminal peptide fragment derived from the prosegment of the proprotein convertase PC7". Biochemistry 39 (11): 2868–77. doi:10.1021/bi9923961. PMID 10715106. 
  • Creemers JW, van de Loo JW, Plets E, et al. (2001). "Binding of BiP to the processing enzyme lymphoma proprotein convertase prevents aggregation, but slows down maturation". J. Biol. Chem. 275 (49): 38842–7. doi:10.1074/jbc.M006758200. PMID 10964928. 
  • Grosset C, Chen CY, Xu N, et al. (2000). "A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex". Cell 103 (1): 29–40. doi:10.1016/S0092-8674(00)00102-1. PMID 11051545. 

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