PCOLCE

PCOLCE
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1UAP
Identifiers
Aliases	PCOLCE, PCPE, PCPE-1, PCPE1, procollagen C-endopeptidase enhancer
External IDs	OMIM: 600270; MGI: 105099; HomoloGene: 1946; GeneCards: PCOLCE; OMA:PCOLCE - orthologs
Gene location (Human) Chr. Chromosome 7 (human) Band 7q22.1 Start 100,602,363 bp End 100,608,175 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5 G2|5 76.59 cM Start 137,603,365 bp End 137,612,046 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium periodontal fiber canal of the cervix tendon of biceps brachii tibia cartilage tissue apex of heart gallbladder right coronary artery synovial membrane Top expressed in calvaria fossa efferent ductule molar vas deferens ankle umbilical cord external carotid artery body of femur stroma of bone marrow More reference expression data BioGPS More reference expression data
Gene ontology Molecular function heparin binding protein binding peptidase activator activity collagen binding extracellular matrix structural constituent Cellular component extracellular matrix extracellular exosome extracellular space extracellular region collagen-containing extracellular matrix Biological process multicellular organism development proteolysis positive regulation of peptidase activity cellular response to leukemia inhibitory factor Sources:Amigo / QuickGO
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: 137.6 – 137.61 Mb PubMed search
Wikidata
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Procollagen C-endopeptidase enhancer 1 is an enzyme that in humans is encoded by the PCOLCE gene.

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 activity.

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): 26280–26285. 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): 229–234. 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): 1384–1390. 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): 33864–33869. 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): 133–137. 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): 49820–49830. 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): 16899–16903. 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): 7199–7205. 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): 25982–25989. 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): 2121–2127. 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): 22616–22623. 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): 10786–10798. 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): 16924–16933. doi:10.1074/jbc.M701610200. PMID 17446170.