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Literature summary for 3.4.24.19 extracted from

  • Pollard, R.D.; Blesso, C.N.; Zabalawi, M.; Fulp, B.; Gerelus, M.; Zhu, X.; Lyons, E.W.; Nuradin, N.; Francone, O.L.; Li, X.A.; Sahoo, D.; Thomas, M.J.; Sorci-Thomas, M.G.
    Procollagen C-endopeptidase enhancer protein 2 (PCPE2) reduces atherosclerosis in mice by enhancing scavenger receptor class B1 (SR-BI)-mediated high-density lipoprotein (HDL)-cholesteryl ester uptake (2015), J. Biol. Chem., 290, 15496-15511 .
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
additional information both PCPE1 and PCPE2 are located in the extracellular matrix, where they facilitate bone morphogenetic protein 1 (BMP1) cleavage of C-terminal procollagen propeptides. PCPE2 and PCPE1 have different tissue distributions and heparin-binding affinities, suggesting a functional divergence. PCPE2 is heavily expressed in heart tissue in contrast to PCPE1. Both PCPE1 and PCPE2 have two CUB (Complement C1r/C1s, Uegf, Bmp1) domains separated by a short linker region, with each domain consisting of about 110 residues containing a beta-sandwich fold that mediates a variety of protein-protein interactions. Phenotype of PCPE2-/- mice, overview Mus musculus
procollagen C-endopeptidase enhancer protein 1 PCPE1, a glycoprotein located in the extracellular matrix, enhances the cleavage of C-terminal procollagen by bone morphogenetic protein 1 (BMP1) Mus musculus
procollagen C-endopeptidase enhancer protein 2 PCPE2, a 52-kDa glycoprotein located in the extracellular matrix, enhances the cleavage of C-terminal procollagen by bone morphogenetic protein 1 (BMP1). PCPE2 is not essential for in vivo pro-apoA-I processing. PCPE2 confers atheroprotection to apoA-I by enhancing BMP1-mediated catalytic cleavage, converting pro-apoA-I to mature apoA-I, and stimulating ABCA1-mediated cholesterol flux, but pro-apoA-I processing is not altered in the case of PCPE2 deficiency Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Mus musculus
-
-
extracellular matrix
-
 Mus musculus 31012
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pro-apoA-I + H2O Mus musculus
-
 apoA-I + apoA-I propeptide
-
 ?
procollagen + H2O Mus musculus
-
 collagen + collagen propeptide
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P98063
-
-

Source Tissue

Source Tissue Comment Organism Textmining
connective tissue aortic root Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pro-apoA-I + H2O
-
 Mus musculus apoA-I + apoA-I propeptide
-
 ?
procollagen + H2O
-
 Mus musculus collagen + collagen propeptide
-
 ?

Synonyms

Synonyms Comment Organism
BMP1
-
 Mus musculus
bone morphogenetic protein 1
-
 Mus musculus

General Information

General Information Comment Organism
physiological function BMP1, in addition to catalyzing procollagen processing, removes the apoA-I six-amino acid propeptide. BMP1-PCPE2 processing of the apoA-I propeptide might stimulate nHDL assembly. PCPE2 enhances the BMP1-mediated cleavage of propeptides from procollagen. PCPE2 confers atheroprotection to apoA-I by enhancing BMP1-mediated catalytic cleavage, converting pro-apoA-I to mature apoA-I, and stimulating ABCA1-mediated cholesterol flux, but pro-apoA-I processing is not altered in the case of PCPE2 deficiency Mus musculus