3.4.21.B27: proprotein convertase 7
This is an abbreviated version!
For detailed information about proprotein convertase 7, go to the full flat file.
Word Map on EC 3.4.21.B27
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3.4.21.B27
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furin
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tmprss6
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endoproteases
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pcsks
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medicine
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pafah1b2
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hemochromatosis
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furin-like
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pnpla3
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mbtps1
- 3.4.21.B27
- furin
- tmprss6
- endoproteases
-
pcsks
- medicine
- pafah1b2
- hemochromatosis
-
furin-like
-
pnpla3
-
mbtps1
Reaction
cleaves proteins typically at sites marked by the consensus Arg-Xaa-(Lys/Arg)-Arg sequence =
Synonyms
furin, LPC, lymphoma PC, PC-7, PC7, PC7A, PC7B, PCSK7, Proprotein convertase, proprotein convertase 7, proprotein convertase PCSK7, proprotein convertase subtilisin/kexin type 7, rPC7, S08.077, SPC7, subtilisin-like proprotein convertase 7
ECTree
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General Information
General Information on EC 3.4.21.B27 - proprotein convertase 7
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evolution
malfunction
metabolism
physiological function
additional information
the enzyme is a member of the subtilisin/kexin family of pro-protein convertases
evolution
four of nine conserved proprotein convertases (PCs), including furin, Pace4, PC5A/B, and PC7, cleave substrates after the minimal dibasic recognition motif (K/R)-(X)n-(K/R)Y, where n is 0, 2, 4, or 6 and X can be any amino acid. In 152 PC sequences examined across species, the catalytic sites are 95% identical
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cells silenced for proprotein convertase 7 have substantially reduced MHC class I surface levels caused by high instability and significantly delayed surface accumulation of these molecules
malfunction
an enzyme PC7 chimera, in which the transmembrane domain and the cytosolic tail are replaced by that of the convertase furin, loses its ability to cleave the transferrin receptor
malfunction
enzyme loss of function suppresses markers for anterior patterning of neural tissues and early eye development
malfunction
inhibiting the enzyme in zebrafish results in various developmental defects and dysregulation of gene expressions, phenotypes, overview
malfunction
the PLC motif in the cytosolic tail of proprotein convertase 7 (PC7) is dispensable for endosomal activity, but is specifically required for trans-Golgi network (TGN) recycling and to rescue proactivin-A cleavage in furin-depleted B16-F1 melanoma cells. In sharp contrast, PC7 complements furin in cleaving Notch1 independently of PLC-mediated TGN access
when iron is limiting, human transferrin receptor TfR1 levels increase at least in part by way of the down-regulation of PC7 enzyme expression
metabolism
all proprotein convertase (PC) activity detected in the trans-Golgi network/endosomal system of B16-F1 cells is mediated by furin, but not by endogenous PC7. Enzyme PC7 can rescue proActivin-A cleavage in furin-depleted B16-F1 melanoma cells
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proprotein convertase 7 is required for normal MHC class I surface levels in the context of a defective peptide-loading complex
physiological function
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proprotein convertase PC7 enhances the activation of the epidermal growth factor receptor pathway through processing of the epidermal growth factor precursor
physiological function
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proprotein convertase PC7 enhances the activation of the epidermal growth factor receptor pathway through processing of the epidermal growth factor precursor
physiological function
the enzyme cleaves many pro-proteins to release their active proteins, including members of the bone morphogenetic protein (BMP) family of signaling molecules. The enzyme is required during embryonic development of eyes and brain, overview
physiological function
the enzyme is essential for zebrafish development and regulates the expression and proteolytic cleavage of transforming growth factor beta1a
physiological function
the enzyme is involved in the regulation of systemic iron homeostasis via shedding of human transferrin receptor 1, TfR1, as its unique mechanism. Shedding of hTfR1 by the enzyme requires endocytosis into acidic clathrin-coated vesicles, enzyme transmembrane domain and cytosolic tail are critical for hTfR1 shedding in the endosomes
physiological function
the enzyme is involved in the regulation of systemic iron homeostasis via shedding of soluble human transferrin receptor 1, TfR1, as its unique mechanism. But the enzyme is not involved in hepcidin regulation by influencing solube hemojuvelin level
physiological function
CRISPR editing reveals that both furin and PC7 are functional in B16-F1 cells and able to substitute for each other during Notch1 and ADAM10 precursor processing
physiological function
morula compaction and inner cell mass formation depend on PC7 and the related proteases Furin and Pace4. These proteases jointly regulate cell-cell adhesion mediated by E-cadherin processing during blastocyst formation
additional information
a PLC motif in the cytosolic tail of PC7 is dispensable for endosomal activity, but it is specifically required for trans-Golgi network recycling and to rescue proActivin-A cleavage in furin-depleted B16-F1 melanoma cells