PCOLCE

Procollagen C-endopeptidase enhancer
PDB rendering based on 1uap.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1UAP​
Identifiers
Symbols	PCOLCE ; PCPE; PCPE-1; PCPE1
External IDs	OMIM: 600270 MGI: 105099 HomoloGene: 1946 GeneCards: PCOLCE Gene
Gene ontology Molecular function • protein binding • collagen binding • heparin binding • peptidase activator activity Cellular component • extracellular space • extracellular matrix • extracellular exosome Biological process • proteolysis • multicellular organismal development • positive regulation of peptidase activity Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5118	18542
Ensembl	ENSG00000106333	ENSMUSG00000029718
UniProt	Q15113	Q61398
RefSeq (mRNA)	NM_002593	NM_008788
RefSeq (protein)	NP_002584	NP_032814
Location (UCSC)	Chr 7: 100.6 – 100.61 Mb	Chr 5: 137.61 – 137.61 Mb
PubMed search

Procollagen C-endopeptidase enhancer 1 is an enzyme that in humans is encoded by the PCOLCE gene.^[1][2][3]

Fibrillar collagen types I-III are synthesized as precursor molecules known as procollagens. These precursors contain amino- and carboxyl-terminal peptide extensions known as N- and C-propeptides, respectively, which are cleaved, upon secretion of procollagen from the cell, to yield the mature triple helical, highly structured fibrils. This gene encodes a glycoprotein which binds and drives the enzymatic cleavage of type I procollagen and heightens C-proteinase activity.^[3]

References

1. Takahara K, Osborne L, Elliott RW, Tsui LC, Scherer SW, Greenspan DS (Mar 1997). "Fine mapping of the human and mouse genes for the type I procollagen COOH-terminal proteinase enhancer protein". Genomics 31 (2): 253–6. doi:10.1006/geno.1996.0043. PMID 8824813.
2. Glockner G, Scherer S, Schattevoy R, Boright A, Weber J, Tsui LC, Rosenthal A (Dec 1998). "Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes". Genome Res 8 (10): 1060–73. doi:10.1101/gr.8.10.1060. PMC 310788. PMID 9799793.
3. "Entrez Gene: PCOLCE procollagen C-endopeptidase enhancer".

Further reading

• Takahara K, Kessler E, Biniaminov L, et al. (1994). "Type I procollagen COOH-terminal proteinase enhancer protein: identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE)". J. Biol. Chem. 269 (42): 26280–5. PMID 7523404.
• Scott IC, Clark TG, Takahara K, et al. (1999). "Structural organization and expression patterns of the human and mouse genes for the type I procollagen COOH-terminal proteinase enhancer protein". Genomics 55 (2): 229–34. doi:10.1006/geno.1998.5663. PMID 9933570.
• Mott JD, Thomas CL, Rosenbach MT, et al. (2000). "Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor". J. Biol. Chem. 275 (2): 1384–90. doi:10.1074/jbc.275.2.1384. PMID 10625689.
• Ricard-Blum S, Bernocco S, Font B, et al. (2002). "Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1". J. Biol. Chem. 277 (37): 33864–9. doi:10.1074/jbc.M205018200. PMID 12105202.
• Ligon AH, Scott IC, Takahara K, et al. (2002). "PCOLCE deletion and expression analyses in uterine leiomyomata". Cancer Genet. Cytogenet. 137 (2): 133–7. doi:10.1016/S0165-4608(02)00547-2. PMID 12393284.
• Steiglitz BM, Keene DR, Greenspan DS (2003). "PCOLCE2 encodes a functional procollagen C-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1". J. Biol. Chem. 277 (51): 49820–30. doi:10.1074/jbc.M209891200. PMID 12393877.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Bernocco S, Steiglitz BM, Svergun DI, et al. (2003). "Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein". J. Biol. Chem. 278 (9): 7199–205. doi:10.1074/jbc.M210857200. PMID 12486138.
• Liepinsh E, Banyai L, Pintacuda G, et al. (2003). "NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding". J. Biol. Chem. 278 (28): 25982–9. doi:10.1074/jbc.M302734200. PMID 12670942.
• 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.
• Petropoulou V, Garrigue-Antar L, Kadler KE (2005). "Identification of the minimal domain structure of bone morphogenetic protein-1 (BMP-1) for chordinase activity: chordinase activity is not enhanced by procollagen C-proteinase enhancer-1 (PCPE-1)". J. Biol. Chem. 280 (24): 22616–23. doi:10.1074/jbc.M413468200. PMID 15817489.
• Ge G, Zhang Y, Steiglitz BM, Greenspan DS (2006). "Mammalian tolloid-like 1 binds procollagen C-proteinase enhancer protein 1 and differs from bone morphogenetic protein 1 in the functional roles of homologous protein domains". J. Biol. Chem. 281 (16): 10786–98. doi:10.1074/jbc.M511111200. PMID 16507574.
• Blanc G, Font B, Eichenberger D, et al. (2007). "Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity". J. Biol. Chem. 282 (23): 16924–33. doi:10.1074/jbc.M701610200. PMID 17446170.