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Literature summary for 3.4.21.B26 extracted from

  • Hoac, B.; Susan-Resiga, D.; Essalmani, R.; Marcinkiweicz, E.; Seidah, N.G.; McKee, M.D.
    Osteopontin as a novel substrate for the proprotein convertase 5/6 (PCSK5) in bone (2018), Bone, 107, 45-55 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane proprotein convertase 5/6 (PC5/6) has two splice variants: soluble PC5/6A and membrane-bound PC5/6B Mus musculus 16020
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soluble proprotein convertase 5/6 (PC5/6) has two splice variants: soluble PC5/6A and membrane-bound PC5/6B Mus musculus
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
osteopontin + H2O Mus musculus Pcsk5/PCSK5 is temporally and spatially expressed with Opn/OPN (Spp1/SPP1) in osteoblasts and osteocytes, indicating that osteopontin could be a physiologically relevant substrate for PC5/6 or PC5/6-activated proteases in bone. Cleavage of osteopontin may modify the function of osteopontin in bone and/or modulate other enzymatic cleavages of osteopontin, leading to alterations in the bone phenotype ?
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Organism

Organism UniProt Comment Textmining
Mus musculus Q04592
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Source Tissue

Source Tissue Comment Organism Textmining
bone expressed during mouse development in many tissues including bone and tooth Mus musculus
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MC3T3-E1 cell
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Mus musculus
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MLO-Y4 cell
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Mus musculus
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osteoblast primary culture Mus musculus
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osteocyte
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Mus musculus
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tooth expressed during mouse development in many tissues including bone and tooth Mus musculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
osteopontin + H2O Pcsk5/PCSK5 is temporally and spatially expressed with Opn/OPN (Spp1/SPP1) in osteoblasts and osteocytes, indicating that osteopontin could be a physiologically relevant substrate for PC5/6 or PC5/6-activated proteases in bone. Cleavage of osteopontin may modify the function of osteopontin in bone and/or modulate other enzymatic cleavages of osteopontin, leading to alterations in the bone phenotype Mus musculus ?
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?
osteopontin + H2O the enzyme (PC5/6A) efficiently and completely cleaves human osteopontin into three distinct fragments migrating at about 50 kDa, about 18 kDa, and 16 kDa, with evidence for the predicted cleavage sites being at 168RSKSKKFR175-/- and 241KQSR244-/-. PC5/6 also partially cleaves mouse osteopontin to release fragments of about 30 kDa and 29 kDa Mus musculus ?
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Synonyms

Synonyms Comment Organism
PC5/6A proprotein convertase 5/6 (PC5/6) has two splice variants: soluble PC5/6A and membrane-bound PC5/6B Mus musculus
PC5/6B proprotein convertase 5/6 (PC5/6) has two splice variants: soluble PC5/6A and membrane-bound PC5/6B Mus musculus
PCSK5
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Mus musculus
proprotein convertase 5/6
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Mus musculus

General Information

General Information Comment Organism
malfunction PC5/6-knockout mouse embryos show developmental abnormalities, and reduced overall mineralization Mus musculus
physiological function Pcsk5/PCSK5 is temporally and spatially expressed with Opn/OPN (Spp1/SPP1) in osteoblasts and osteocytes, indicating that osteopontin could be a physiologically relevant substrate for PC5/6 or PC5/6-activated proteases in bone. Cleavage of osteopontin may modify the function of osteopontin in bone and/or modulate other enzymatic cleavages of osteopontin, leading to alterations in the bone phenotype Mus musculus