PCOLCE

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

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] 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] 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 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 [3] [4]
Wikidata
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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]