PCOLCE

Protein-coding gene in humans

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)^[1]

Band	7q22.1	Start	100,602,363 bp^[1]
Band	7q22.1	End	100,608,175 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5 G2\|5 76.59 cM	Start	137,603,365 bp^[2]
Band	5 G2\|5 76.59 cM	End	137,612,046 bp^[2]

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

belly 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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Procollagen C-endopeptidase enhancer 1 is an enzyme that in humans is encoded by the PCOLCE gene.^[5]^[6]^[7]

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.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000106333 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000029718 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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): 253–256. doi:10.1006/geno.1996.0043. PMID 8824813.
^ 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): 1060–1073. doi:10.1101/gr.8.10.1060. PMC 310788. PMID 9799793.
^ ^a ^b "Entrez Gene: PCOLCE procollagen C-endopeptidase enhancer".

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. doi:10.1016/S0021-9258(18)47191-8. 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. Bibcode:2002PNAS...9916899M. 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" (PDF). J. Biol. Chem. 282 (23): 16924–16933. doi:10.1074/jbc.M701610200. PMID 17446170. Archived from the original on 2018-07-23.