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Literature summary for 1.14.11.4 extracted from

  • Heard, M.E.; Besio, R.; Weis, M.; Rai, J.; Hudson, D.M.; Dimori, M.; Zimmerman, S.M.; Kamykowski, J.A.; Hogue, W.R.; Swain, F.L.; Burdine, M.S.; Mackintosh, S.G.; Tackett, A.J.; Suva, L.J.; Eyre, D.R.; Morello, R.
    Sc65-null mice provide evidence for a novel endoplasmic reticulum complex regulating collagen lysyl hydroxylation (2016), PLoS Genet., 12, e1006002 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.4

Cloned(Commentary)

Cloned (Comment) Organism
transient transfection of HA-tagged LH1 in 714 mouse embryonic fibroblasts Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
additional information the endoplasmic reticulum complex including SC65 and prolyl 3-hydroxylase 3affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility, while it has no effect on prolyl 3-hydroxylation. CRTAP, a non-enzymic member of the Leprecan family of proteins which includes Synaptonemal Complex 65 (SC65) and the prolyl 3-hydroxylases (P3H1, P3H2 and P3H3), is an essential third subunit of a complex with prolyl 3-hydroxylase 1 (aka LEPRECAN) and cyclophilin B (CYPB) in the endoplasmic reticulum, forming the so-called collagen prolyl 3-hydroxylation complex Mus musculus
SC65 directly interacts with lysyl-hydroxylase 1, LH1 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Mus musculus 5783
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
[procollagen]-L-lysine + 2-oxoglutarate + O2 Mus musculus
-
 [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
 ?
[procollagen]-L-lysine + 2-oxoglutarate + O2 Mus musculus 714
-
 [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9R0E2
-
-
Mus musculus 714 Q9R0E2
-
-

Source Tissue

Source Tissue Comment Organism Textmining
bone
-
 Mus musculus
-
fibroblast skin and embryonic Mus musculus
-
osteoblast primary calvarial Mus musculus
-
skin
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[procollagen]-L-lysine + 2-oxoglutarate + O2
-
 Mus musculus [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
 ?
[procollagen]-L-lysine + 2-oxoglutarate + O2
-
 Mus musculus 714 [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
LH1
-
 Mus musculus
lysyl-hydroxylase 1
-
 Mus musculus
Plod1
-
 Mus musculus

General Information

General Information Comment Organism
malfunction mice with loss of function of Leprel2 (encoding P3H3) have the same loss of tissue type I collagen lysine-hydroxylation as that observed in the Sc65 knockout mice. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility, while it has no effect on prolyl 3-hydroxylation. Sc65KO mouse generation and confirmation of bone loss phenotype, overview Mus musculus
metabolism the endoplasmic reticulum complex including SC65 and prolyl 3-hydroxylase 3 affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. The prolyl-hydroxylase complex in the endoplasmic reticulum controls lysyl-hydroxylase activity during collagen synthesis. SC65/LH1/P3H3 are interlinked within a protein complex in the endoplasmic reticulum Mus musculus
physiological function in the endoplasmic reticulum, specific proline and lysine residues of newly translated procollagen chains are modified by prolyl- and lysyl-hydroxylases, respectively. These enzymes share a highly conserved catalytic 2-oxoglutarate, ascorbate- and Fe(II)-dependent dioxygenase domain Mus musculus