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Information on EC 3.4.21.B25 - PACE4 proprotein convertase
for references in articles please use BRENDA:EC3.4.21.B25
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preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.B25 PACE4 proprotein convertase
The enzyme appears in viruses and cellular organisms
- 3.4.21.B25
-
convertases
- furin
-
prohormone
- endoproteases
-
furin-deficient
-
furin-like
- alpha1-pdx
-
dibasic
-
pro-proteins
- alpha1-antitrypsin
- portland
-
endoproteolysis
- diagnostics
- kexin
-
kexin-like
- ski-1
-
cys-rich
- medicine
-
subtilisin-related
Reaction Schemes
showreleases mature proteins from their proproteins by cleavage of Arg-Xaa-Yaa-Arg-Zaa bonds, where Xaa can be any amino acid and Yaa is Arg or Lys
Synonyms
pace4, pace-4, proprotein convertase pace4, paired basic amino acid-cleaving enzyme 4, xpace4, pace 4, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PACE 4
PACE-4
PACE4
paired basic amino acid-cleaving enzyme 4
paired basic amino-acid-cleaving enzyme-4
PCSK6
SPC4
subtilisin-like proprotein convertase 4
PACE4
-
-
PACE4
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
releases mature proteins from their proproteins by cleavage of Arg-Xaa-Yaa-Arg-Zaa bonds, where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
cleavage of C-N-linkage
hydrolysis of peptide bond
cleavage of C-N-linkage
-
-
hydrolysis of peptide bond
-
-
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CAS REGISTRY NUMBER
COMMENTARY
151662-24-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
anthrax toxin PA + H2O
?
-
Substrates: contains the sequence RKKR at the cleavage site
Products: -
Products: -
?
benzyloxycarbonyl-REKR-7-amido-4-trifluoromethylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
envelope glycoprotein gp160
?
Substrates: well activated by PaCE4
Products: -
Products: -
?
human immunodeficiency virus type 1 Vpr + H2O
?
Substrates: undergoes proteolytic processing at a very well conserved proprotein convertase cleavage site, R85QRR88-/-, proprotein convertases PC5 and PACE4 can efficiently process extracellular Vpr
Products: -
Products: -
?
L-pyroglutamyl-Arg-Thr-Lys-Arg-4-methylcoumaryl 7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-pyroglutamyl-RTKR-4-methylcoumarin 7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
low density lipoprotein receptor-elated protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
?
Substrates: -
Products: -
Products: -
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
pro-beta site APP cleaving enzyme + H2O
beta site APP cleaving enzyme + ?
-
Substrates: i.e. BACE, weak substrate
Products: -
Products: -
?
pro-branching morphogenesis protein 2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
proADAMTS-4 + H2O
?
Substrates: recombinant PACE4 activates proADAMTS-4 by removal of the prodomain
Products: -
Products: -
?
proADAMTS-5 + H2O
?
Substrates: recombinant PACE4 activates proADAMTS-5 by removal of the prodomain
Products: -
Products: -
?
prosomatostatin + H2O
somatostatin-14 + somatostatin-28
-
Substrates: enzyme cleaves at a dibasic Arg-Lys site
Products: -
Products: -
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin-7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
ir
tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
Vg1 + H2O
?
Substrates: Vg1 in a TgF beta-related growth factor localized to vegetal blastomers in Xenopus embryos
Products: -
Products: -
?
Xnr1 + H2O
?
Substrates: i.e. Nodal-related protein 1
Products: -
Products: -
?
Xnr2 + H2O
?
Substrates: i.e. Nodal-related protein 2
Products: -
Products: -
?
Xnr3 + H2O
?
Substrates: i.e. Nodal-related protein 3
Products: -
Products: -
?
insulin receptor isoform B zymogen + H2O
mature insulin receptor isoform B + ?
Substrates: maturation
Products: -
Products: -
?
insulin receptor isoform B zymogen + H2O
mature insulin receptor isoform B + ?
Substrates: -
Products: -
Products: -
?
preprohepcidin + H2O
?
Substrates: key role of the convertases furin, PACE4, PC5 and/or PC7 in the generation and secretion of active hepcidin
Products: -
Products: -
?
preprohepcidin + H2O
?
Substrates: key role of the convertases furin, PACE4, PC5 and/or PC7 in the generation and secretion of active hepcidin. PC7 processes this peptide at the cleavage site of preprohepcidin PMFQRRRRR-/-, resulting in a major 1305 Da N-terminal product. Two minor products with masses of 149 Da and 993 Da are also detected which correspond to the loss of one (PMFQRRRR) or two (PMFQRRR) C-terminal Arg, respectively
Products: -
Products: -
?
proform bone morphogenetic protein 6 + H2O
mature bone morphogenetic protein 6 + ?
-
Substrates: BMP6, the substrate is exclusively found in hypertrophic chondrocytes
Products: -
Products: -
?
proform bone morphogenetic protein 6 + H2O
mature bone morphogenetic protein 6 + ?
-
Substrates: BMP6, recombinantly expressed FLAG-tagged human substrate protein. The enzyme recognizes the sequence RTTR(371-374) of human BMP6 and cleaves proBMP6 at its C-terminus
Products: -
Products: -
?
prorenin receptor PRR + H2O
soluble prorenin receptor sPRR + fragment M8.9
Substrates: cleavage occurs after a conserved consensus motif RXXR-
Products: -
Products: -
?
prorenin receptor PRR + H2O
soluble prorenin receptor sPRR + fragment M8.9
Substrates: cleavage occurs after a conserved consensus motif RXXR-
Products: -
Products: -
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
-
Substrates: -
Products: -
Products: -
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
Substrates: -
Products: -
Products: -
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
-
Substrates: -
Products: -
Products: -
?
von Willebrand factor precursor + H2O
mature von Willebrand factor + ?
-
Substrates: cleavage requires both the P4 arginine and the P2 lysine
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme cleaves at sites with paired basic amino acid residues
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: profactor IX
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: Pseudomonas exotoxin A
Products: -
Products: -
?
additional information
?
-
-
Substrates: PACE4-CS recognizes the motifs X-Ala and X-Pro
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme binds tightly to heparin and anchors heparan sulfate proteoglycans at the extracellular matrix, role in spatiotemporal regulation of TGFbeta-related factors' biological activity
Products: -
Products: -
?
additional information
?
-
Substrates: substrate cleavage analysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate cleavage analysis
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with insulin receptor isoform A zymogen
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme requires basic residues in the -1, -2 and -4 position of the substrate sequence, can recognize RAAR and, to a much lesser extent, KR and RR
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in proteolytic activation of anthrax toxin PA
Products: -
Products: -
?
additional information
?
-
Substrates: does not cleave proopiomelanocortin, proglucagon, prosomatostatin and secretogranin in neuroendocrine cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the main substrates for PACE4 are membrane type matrix metalloproteinases
Products: -
Products: -
?
additional information
?
-
Substrates: PACE4 is identified as a proprotein convertase responsible for activation of aggrecanases in osteoarthritic and cytokine-stimulated cartilage
Products: -
Products: -
?
additional information
?
-
Substrates: PACE4 regulates the submandibular gland development via the activation of some growth/differentiation factors
Products: -
Products: -
?
additional information
?
-
Substrates: no cleavage of Xnr5, Derrière or ActivinB pro-proteins
Products: -
Products: -
?
additional information
?
-
Substrates: no cleavage of Xnr5, Derrière or ActivinB pro-proteins
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
human immunodeficiency virus type 1 Vpr + H2O
?
Substrates: undergoes proteolytic processing at a very well conserved proprotein convertase cleavage site, R85QRR88-/-, proprotein convertases PC5 and PACE4 can efficiently process extracellular Vpr
Products: -
Products: -
?
insulin receptor isoform B zymogen + H2O
mature insulin receptor isoform B + ?
Substrates: maturation
Products: -
Products: -
?
preprohepcidin + H2O
?
Substrates: key role of the convertases furin, PACE4, PC5 and/or PC7 in the generation and secretion of active hepcidin
Products: -
Products: -
?
pro-branching morphogenesis protein 2 + H2O
?
-
Substrates: -
Products: -
Products: -
?
proform bone morphogenetic protein 6 + H2O
mature bone morphogenetic protein 6 + ?
-
Substrates: BMP6, the substrate is exclusively found in hypertrophic chondrocytes
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme binds tightly to heparin and anchors heparan sulfate proteoglycans at the extracellular matrix, role in spatiotemporal regulation of TGFbeta-related factors' biological activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in proteolytic activation of anthrax toxin PA
Products: -
Products: -
?
additional information
?
-
Substrates: PACE4 is identified as a proprotein convertase responsible for activation of aggrecanases in osteoarthritic and cytokine-stimulated cartilage
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,3',3'',3'''-(benzene-1,4-diyldimethanetriyl)tetrakis(4-hydroxy-2H-chromen-2-one)
-
3,3'-(1,3-benzodioxol-5-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
3,3'-(2,3-dihydro-1H-inden-5-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
A23187
-
if reticulocalbin-3 binds to proPACE4 transiently during its biosynthesis, this Ca2+-specific ionophore can block the maturation of proPACE4 to PACE4, accumulation of the proPaCE4-recticulocalbin-3 complex in the cells
alpha1-antitrypsin variant PDX
-
50% inhibition above 0.00002 mM, forms a complex with the enzyme
-
alpha1-antitrypsin variant Portland
-
contains a minimal consensus sequence (Arg-X-X-Arg) for efficient cleavage by furin in its reactive site loop
-
alpha1-antitrypsin variant RRRRSA
-
rat alpha-antitrypsin showing substitution of Arg-Arg-Arg-Arg for Ala-Val-Pro-Met352 at P4-P1 and Ala for Leu354 at P2'
-
alpha1-antitrypsin variant RRRRSL
-
rat alpha-antitrypsin showing substitution of Arg-Arg-Arg-Arg for Ala-Val-Pro-Met352 at P4-P1
-
antisense oligo 5
depletes XPACE4 to 5-10% of control levels; depletes XPACE4 to 5-10% of control levels
alpha1-antitrypsin variant RVRR
-
50% inhibition at 0.000005 mM, forms a complex with the enzyme
-
additional information
-
alpha1-proteinase inhibitor-Portland and alpha1-proteinase inhibitor-Pittsburgh have little effect on PACE4 activity
-
additional information
-
not inhibited by leupeptin and soybean trypsin inhibitor
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
reticulocalbin-3
-
efficiency of PACE4 secretion increases 2fold by coexpression with wild type reticulocalbin-3
-
additional information
-
selective and transient association of reticulocalbin-3 with the precursor of PACE4 plays an important role in the biosynthesis of PACE4
-
additional information
-
the E2F1 transcription factor upregulates the expression of PACE4
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
2-(11-hydroxy-3-oxo-3H-dibenzo[c,h]xanthen-7-yl)benzoic acid
-
0.0083
3,3',3'',3'''-(benzene-1,4-diyldimethanetriyl)tetrakis(4-hydroxy-2H-chromen-2-one)
-
0.014
3,3'-(1,3-benzodioxol-5-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
0.013
3,3'-(2,3-dihydro-1H-inden-5-ylmethanediyl)bis(4-hydroxy-2H-chromen-2-one)
-
0.00011
Ac-LLLLR-((2S)-amino-3S-guanidinobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00051
Ac-LLLLR-((2S,3R)-diaminobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00027
Ac-LLLLR-((2S,3S)-diaminobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00066
Ac-LLLLR-(2,3-diaminobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.00216
Ac-LLLLR-(2,3-diaminopropionyl)-KR-NH2
pH and temperature not specified in the publication
0.00055
Ac-LLLLR-(2-amino-3-guanidinopropionyl)-KR-NH2
pH and temperature not specified in the publication
0.000087
Ac-LLLLR-(2-amino-4-guanidinobutyryl)-KR-NH2
pH and temperature not specified in the publication
0.000105
Ac-LLLLR-Orn-KR-NH2
pH and temperature not specified in the publication
0.000195
Ac-LLLLRAKR-NH2
pH and temperature not specified in the publication
0.000083
Ac-LLLLRKKR-NH2
pH and temperature not specified in the publication
0.000088
Ac-LLLLRRKR-NH2
pH and temperature not specified in the publication
0.000022
Ac-LLLLRVKR-NH2
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
Ac-[C8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.08
Ac-[C8]LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.07
Ac-[PEG8](D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.09
H2N-[C8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.015
H2N-[C8]LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.04
Ac-(D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.21
Ac-(D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.025
Ac-(D)LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.04
Ac-(D)LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.07
Ac-LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.09
Ac-LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.025
Ac-LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.04
Ac-LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.04
Ac-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.04
Ac-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.11
Ac-[PEG8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.15
Ac-[PEG8](D)LLLLRVKR-NH2
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.06
H2N-[C8](D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.09
H2N-[C8](D)LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.04
H2N-[C8]LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.13
H2N-[C8]LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.046
H2N-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in LNCap cells, pH 7.5, 37°C
0.047
H2N-[C8]LLLLRVK-4-amidinobenzylamide
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
0.013
[C8]LLLLRVK-2,3-dehydroagmatine
Homo sapiens
cell survival assay in DU145 cells, pH 7.5, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
preference of the enzyme for cleaving substrates at neutral pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
maximum expression of XPACE4 at the early blastula stage
brenda
-
expression pattern of bone-related genes by RT-PCR/quantitative real-time PCR
brenda
presence of PACE4 protein is restricted to chondrocytes of healthy cartilage, whereas the expression is increased in osteoarthritis cartilage
brenda
enzyme expression in non-small cell lung cancer cells is significantly higher than in normal lung cell and tissues
brenda
enriched in vegetal halves, with no significant asymmetrical distribution between dorsal and ventral halves
brenda
-
PACE4 is limited to the glia and the retina of the optic nerve head
brenda
the enzyme regulates apoptosis in human pancreatic cancer PANC-1 cells via the mitochondrial signaling pathway
brenda
-
PACE4 is limited to the glia and the retina of the optic nerve head
brenda
additional information
enriched in vegetal masses, with no significant asymmetrical distribution between dorsal and ventral halves
brenda
enzyme expression in non-small cell lung cancer cells is significantly higher than in normal lung cell and tissues
brenda
-
PACE4 is intensely expressed in the submandibular epithelium-derived cells including proacinar, terminal tubular, and presumptive ductal cells in the prenatal submandibular gland
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme is constitutively secreted into the extracellular media and localizes at the cell surface and in the extracellular matrix
-
brenda
in stage 1 oocytes, XPACE4 localizes to the mitochondrial cloud, at stage 2, the mitochondrial cloud disperses, then XPACE4 mRNA co-localizes with the vegetal cortex where it remains for the rest of oogenesis
brenda
-
activated at the cell surface where it is tethered to heparan sulfate proteoglycans
brenda
the enzyme is constitutively secreted into the extracellular media and localizes at the cell surface and in the extracellular matrix
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the subtilisin-like proprotein convertase (SPC) family
malfunction
metabolism
insulin receptor requires the proteolytic cleavage of its proform by intra-Golgi furin-like activity. In mammalian cells, insulin receptor is expressed as two isoforms B and A that are responsible for insulin action, but only isozyme A transmits the growth-promoting and mitogenic effects of insulin-like growth factor 2. The two insulin receptor isoforms are similarly cleaved by furin, but when this furin-dependent maturation is inefficient, insulin receptor proforms move to the cell surface where the proprotein convertase PACE4 selectively supports insulin receptor B maturation
physiological function
malfunction
-
the expression of myosin light chain mRNA transcript is markedly reduced in PACE4 knockdown cells
malfunction
-
silencing of PACE4 causes the suppression of branching morphogenesis and aquaporin 5 expression in rat embryonic submandibular gland rudiments culture system
malfunction
-
the PACE4 gene-knockdown cells show a drastic decrease in mineralization even in the presence of any estrogen stimulus
malfunction
-
enzyme PACE4 knockdown causes blockage of chondrogenic differentiation through downregulation of proBMP6 activation
malfunction
when the PACE4 gene is silenced by small interfering RNA the knockdown of human breast cancer MDA-MB-231 cells shows significantly reduced proliferation, migration and invasion rates
physiological function
-
PACE4 regulates submandibular gland development via the activation of proproteins involved in salivary branching and/or salivary acinar differentiation
physiological function
-
PACE4 plays a critical role in myogenic differentiation of C2C12 cells through its association with the insulin-like growth factor-II pathway
physiological function
-
Pace4 activates Nodal in the epiblast to maintain pluripotency. Secreted Pace4 stimulates mesoderm and endoderm formation. Expression of Pace4 in the extraembryonic ectoderm suppresses neural differentiation
physiological function
-
PACE4 plays an important role in submandibular gland development
physiological function
-
the enzyme participates in bone formation at least in osteoblast differentiation, estrogen stimuli promote osteoblastic differentiation via the subtilisin-like proprotein convertase PACE4 in MC3T3-E1 cells. Downregulators of the enzyme, e.g. equol or daidzein, restore the differentiation of MC3T3-E1 cells
physiological function
-
the enzyme is required for chondrogenic differentiation, e.g. for differentiation of ATDC-5 cells into type II collagen-expressing chondrocytes, type X collagen-expressing hypertrophic chondrocytes, and mineralizing chondrocytes
physiological function
the enzyme is involved in the maturation of insulin receptor isoform B, thereby reducing the specific insulin receptor-dependent effects of insulin-like growth factor 2, IGF2
physiological function
the enzyme regulates apoptosis in human prostate cancer cells via endoplasmic reticulum stress and mitochondrial signaling pathways
physiological function
the enzyme play an important role in prostate cancer cell proliferation
physiological function
the enzyme regulates apoptosis in human pancreatic cancer PANC-1 cells via the mitochondrial signaling pathway
physiological function
the enzyme participate in the post-translational activation of inactive proteins, leading to mature, biologically active proteins. It regulates proliferation, migration and invasion in human breast cancer MDA-MB-231 cells
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
physiological function
knockdown of PACE4 in LNCaP cells results in less processing of prorenin receptor PRR and lower levels of soluble prorenin receptor sPRR in the conditioned media. PACE4 overexpression leads to increased PRR processing
physiological function
PACE4-knockout mice exhibit less processing of prorenin receptor PRR, and phosphatase and tensin homolog PTEN controls PACE4-mediated PRR processing in a mouse model of prostate cancer
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PCSK4_MOUSE
655
0
73214
Swiss-Prot
Secretory Pathway (Reliability: 2)
PCSK6_HUMAN
969
0
106420
Swiss-Prot
Secretory Pathway (Reliability: 1)
PCSK4_RAT
678
0
75740
Swiss-Prot
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
103000
110000
25000 - 70000
Northern blot analysis, three different XPACE4 RNA species
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
precursor protein can exist as a dimer as well as a monomer, sedimentation velocity experiments and chemical cross-linking analysis
monomer
-
mature protein and precursor protein, sedimentation velocity experiments and chemical cross-linking analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
autocatalytic processing, cleavage of proprotein after Arg-Val-Lys-Arg149 results in mature protein
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
deletion of 25 amino acids at the C-terminus results in accelerated maturation of the protein
additional information
-
mutant pIRES2-PACE4-deltaC-V5 lacking the cysteine-rich domain
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression pattern analysis of the bone-related enzyme gene by RT-PCR/quantitative real-time PCR
-
full length PACE4-A, C-terminally truncated PACE4-C which lacks 11 amino acids a t the end of its chaperone-like P-domain, C-terminally shortened version of PACE4-C and PACE4-CS
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decanoyl-L-Arg-L-Val-L-Lys-L-Arg-chloromethylketone suppresses the expression of PACE4
-
enzyme PACE4 mRNA levels increase markedly during chondrogenic differentiation of ATDC-5 cells, overview
-
PACE4 expression is markedly decreased in the presence of 0.05 mM decanoyl-L-Arg-L-Val-L-Lys-L-Arg-chloromethylketone
-
PACE4 mRNA levels increase markedly during myogenesis, the PI3K inhibitor LY294002 blocks the induction of PACE4 mRNA, up-regulation of PACE4 transcripts is mediated through the PI3 kinase pathway
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
expression of the enzyme correlates with prognosis in non-small cell lung cancer patients. Overall survival is significantly prolonged in PACE4 negative group when compared with PACE4 positive group (5-year survival rates, 23.1% vs. 54.5%, log-rank test), as is disease-free survival (5-year survival rates, 23.4% vs. 55.4%). Positive expression of PACE4 is an independent factor for non-small cell lung cancer patients and it might serve as a potential prognostic biomarker for patients with non-small cell lung cancer
medicine
additional information
medicine
-
PACE4 overexpression results in enhanced susceptibility to carcinogenesis and tumor progression pointing to a new target for blocking tumor cell invasiveness, PACE4 enhances induced epidermal proliferation, activates matrix metalloproteinases in vivo, disrupts basement membrane structure, increases susceptibility to skin cancer and induces higher levels of matrix metalloproteinases and tumors of advanced malignant phenotype
medicine
PACE4 represents a target for the development of osteoarthritis therapeutics
medicine
the enzyme has an important role in prostate cancer cell proliferation and is a potential therapeutic target
medicine
the inhibition of the enzyme slows prostate cancer progression and is emerging as a promising therapeutic strategy
medicine
PACE4 siRNA may exert antitumor activity through the mitochondrial pathway and is expected to be a promising therapeutic strategy for the treatment of pancreatic cancer
medicine
isoform PACE4-altCT arises in neoplastic lesions. PACE4-altCT is only strongly overexpressed in prostate cancer patients and correlates with ERG expression levels. PACE4-altCT can be detected in the plasma of most patients with prostate cancer, but is only found at low levels in normal patients. Total plasmatic PACE4 levels do not vary significantly between groups
medicine
PACE4 cleavage of PRR is needed for efficient V-ATPase activity and prostate cancer cell growth
additional information
maternal XPACE4 plays an important role in embryonic patterning by regulating the production of a subset of active mature TGFbeta proteins in specific sites, it is required for the endogenous mesoderm inducing activity of vegetal cells before gastrulation
additional information
maternal XPACE4 plays an important role in embryonic patterning by regulating the production of a subset of active mature TGFbeta proteins in specific sites, it is required for the endogenous mesoderm inducing activity of vegetal cells before gastrulation
additional information
-
selective and transient association of reticulocalbin-3 with the precursor of PACE4 plays an important role in the biosynthesis of PACE4
additional information
the pattern of PACE4 expression in development suggests a role in the extracellular actions or activation of inductive signals
additional information
-
PACE4 contributes to prohormone processing under some circumstances
additional information
-
the cysteine-rich domain of PACE4 binds the C-terminal segment of tissue inhibitor of metalloproteinase-2, which is responsible for the attachment of this complex to the cell surface
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taniguchi, T.; Kuroda, R.; Sakurai, K.; Nagahama, M.; Wada, I.; Tsuji, A.; Matsuda, Y.
A critical role for the carboxy terminal region of the proprotein convertase, PACE4A, in the regulation of its autocatalytic activation coupled with secretion
Biochem. Biophys. Res. Commun.
290
878-884
2002
Homo sapiens
brenda
Mains, R.E.; Berard, C.A.; Denault, J.B.; Zhou, A.; Johnson, R.C.; Leduc, R.
PACE4: a subtilisin-like endoprotease with unique properties
Biochem. J.
321
587-593
1997
Rattus norvegicus
-
brenda
Sucic, J.F.; Moehring, J.M.; Inocencio, N.M.; Luchini, J.W.; Moehring, T.J.
Endoprotease PACE4 is Ca2+-dependent and temperature-sensitive and can partly rescue the phenotype of a furin-deficient cell strain
Biochem. J.
339
639-647
1999
Homo sapiens
brenda
Rehemtulla, A.; Barr, P.J.; Rhodes, C.J.; Kaufman, R.J.
PACE4 is a member of the mammalian propeptidase family that has overlapping but not identical substrate specificity to PACE
Biochemistry
32
11586-11590
1993
Homo sapiens
brenda
Tsuji, A.; Sakurai, K.; Kiyokage, E.; Yamazaki, T.; Koide, S.; Toida, K.; Ishimura, K.; Matsuda, Y.
Secretory proprotein convertases PACE4 and PC6A are heparin-binding proteins which are localized in the extracellular matrix. Potential role of PACE4 in the activation of proproteins in the extracellular matrix
Biochim. Biophys. Acta
1645
95-104
2003
Homo sapiens
brenda
Johnson, R.C.; Darlington, D.N.; Hand, T.A.; Bloomquist, B.T.; Mains, R.E.
PACE4: a subtilisin-like endoprotease prevalent in the anterior pituitary and regulated by thyroid status
Endocrinology
135
1178-1185
1994
Rattus norvegicus (Q63415), Rattus norvegicus
brenda
Pinnix, I.; Council, J.E.; Roseberry, B.; Onstead, L.; Mallender, W.; Sucic, J.; Sambamurti, K.
Convertases other than furin cleave beta-secretase to its mature form
FASEB J.
15
1810-1812
2001
Homo sapiens
brenda
Creemers, J.W.; Groot Kormelink, P.J.; Roebroek, A.J.; Nakayama, K.; Van de Ven, W.J.
Proprotein processing activity and cleavage site selectivity of the Kex2-like endoprotease PACE4
FEBS Lett.
336
65-69
1993
Homo sapiens
brenda
Brakch, N.; Galanopoulou, A.S.; Patel, Y.C.; Boileau, G.; Seidah, N.G.
Comparative proteolytic processing of rat prosomatostatin by the convertases PC1, PC2, furin, PACE4 and PC5 in constitutive and regulated secretory pathways
FEBS Lett.
362
143-146
1995
Mammalia
brenda
Zhong, M.; Benjannet, S.; Lazure, C.; Munzer, S.; Seidah, N.G.
Functional analysis of human PACE4-A and PACE4-C isoforms: identification of a new PACE4-CS isoform
FEBS Lett.
396
31-36
1996
Homo sapiens
brenda
Nagahama, M.; Taniguchi, T.; Hashimoto, E.; Imamaki, A.; Mori, K.; Tsuji, A.; Matsuda, Y.
Biosynthetic processing and quaternary interactions of proprotein convertase SPC4 (PACE4)
FEBS Lett.
434
155-159
1998
Homo sapiens
brenda
Gordon, V.M.; Rehemtulla, A.; Leppla, S.H.
A role for PACE4 in the proteolytic activation of anthrax toxin protective antigen
Infect. Immun.
65
3370-3375
1997
Mammalia
brenda
Mori, K.; Kii, S.; Tsuji, A.; Nagahama, M.; Imamaki, A.; Hayashi, K.; Akamatsu, T.; Nagamune, H.; Matsuda, Y.
A novel human PACE4 isoform, PACE4E is an active processing protease containing a hydrophobic cluster at the carboxy terminus
J. Biochem.
121
941-948
1997
Homo sapiens (P29122), Homo sapiens
brenda
Mori, K.; Imamaki, A.; Nagata, K.; Yonetomi, Y.; Kiyokage-Yoshimoto, R.; Martin, T.J.; Gillespie, M.T.; Nagahama, M.; Tsuji, A.; Matsuda, Y.
Subtilisin-like proprotein convertases, PACE4 and PC8, as well as furin, are endogenous proalbumin convertases in HepG2 cells
J. Biochem.
125
627-633
1999
Homo sapiens
brenda
Tsuji, A.; Ikoma, T.; Hashimoto, E.; Matsuda, Y.
Development of selectivity of alpha1-antitrypsin variant by mutagenesis in its reactive site loop against proprotein convertase. A crucial role of the P4 arginine in PACE4 inhibition
Protein Eng.
15
123-130
2002
Homo sapiens
brenda
Tsuji, A.; Kikuchi, Y.; Sato, Y.; Koide, S.; Yuasa, K.; Nagahama, M.; Matsuda, Y.
A proteomic approach reveals transient association of reticulocalbin-3, a novel member of the CREC family, with the precursor of subtilisin-like proprotein convertase, PACE4
Biochem. J.
396
51-59
2006
Homo sapiens
brenda
Bassi, D.E.; Lopez De Cicco, R.; Cenna, J.; Litwin, S.; Cukierman, E.; Klein-Szanto, A.J.
PACE4 expression in mouse basal keratinocytes results in basement membrane disruption and acceleration of tumor progression
Cancer Res.
65
7310-7319
2005
Rattus norvegicus
brenda
Birsoy, B.; Berg, L.; Williams, P.H.; Smith, J.C.; Wylie, C.C.; Christian, J.L.; Heasman, J.
XPACE4 is a localized pro-protein convertase required for mesoderm induction and the cleavage of specific TGFb proteins in Xenopus development
Development
132
591-602
2005
Xenopus laevis (Q5G5T9), Xenopus laevis (Q5G5T8)
brenda
Mains, R.E.
Proprotein convertase PACE4
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , Eds. ) Academic Press
2
1871-1874
2004
Homo sapiens (P29122), Mus musculus, Rattus norvegicus (Q63415), Aplysia sp.
-
brenda
Nour, N.; Mayer, G.; Mort, J.S.; Salvas, A.; Mbikay, M.; Morrison, C.J.; Overall, C.M.; Seidah, N.G.
The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases
Mol. Biol. Cell
16
5215-5226
2005
Mus musculus
brenda
Lapierre, M.; Siegfried, G.; Scamuffa, N.; Bontemps, Y.; Calvo, F.; Seidah, N.G.; Khatib, A.M.
Opposing function of the proprotein convertases furin and PACE4 on breast cancer cells malignant phenotypes: role of tissue inhibitors of metalloproteinase-1
Cancer Res.
67
9030-9034
2007
Homo sapiens
brenda
Page, R.E.; Klein-Szanto, A.J.; Litwin, S.; Nicolas, E.; Al-Jumaily, R.; Alexander, P.; Godwin, A.K.; Ross, E.A.; Schilder, R.J.; Bassi, D.E.
Increased expression of the pro-protein convertase furin predicts decreased survival in ovarian cancer
Cell. Oncol.
29
289-299
2007
Homo sapiens
brenda
Akamatsu, T.; Purwanti, N.; Karabasil, M.R.; Li, X.; Yao, C.; Kanamori, N.; Hosoi, K.
Temporospatially regulated expression of subtilisin-like proprotein convertase PACE4 (SPC4) during development of the rat submandibular gland
Dev. Dyn.
236
314-320
2007
Rattus norvegicus (Q63415)
brenda
Yuasa, K.; Suzue, K.; Nagahama, M.; Matsuda, Y.; Tsuji, A.
Transcriptional regulation of subtilisin-like proprotein convertase PACE4 by E2F: possible role of E2F-mediated upregulation of PACE4 in tumor progression
Gene
402
103-110
2007
Homo sapiens
brenda
Seidah, N.G.; Mayer, G.; Zaid, A.; Rousselet, E.; Nassoury, N.; Poirier, S.; Essalmani, R.; Prat, A.
The activation and physiological functions of the proprotein convertases
Int. J. Biochem. Cell Biol.
40
1111-1125
2008
Homo sapiens
brenda
Tsuji, A.; Kanie, H.; Makise, H.; Yuasa, K.; Nagahama, M.; Matsuda, Y.
Engineering of alpha 1-antitrypsin variants selective for subtilisin-like proprotein convertases PACE4 and PC6: importance of the P2 residue in stable complex formation of the serpin with proprotein convertase
Protein Eng. Des. Sel.
20
163-170
2007
Homo sapiens
brenda
Freyer, C.; Kilpatrick, L.M.; Salamonsen, L.A.; Nie, G.
Pro-protein convertases (PCs) other than PC6 are not tightly regulated for implantation in the human endometrium
Reproduction
133
1189-1197
2007
Homo sapiens (P29122), Homo sapiens
brenda
Malfait, A.M.; Arner, E.C.; Song, R.H.; Alston, J.T.; Markosyan, S.; Staten, N.; Yang, Z.; Griggs, D.W.; Tortorella, M.D.
Proprotein convertase activation of aggrecanases in cartilage in situ
Arch. Biochem. Biophys.
478
43-51
2008
Rattus norvegicus (Q78EH2)
brenda
Padua, M.B.; Hansen, P.J.
Regulation of DNA synthesis and the cell cycle in human prostate cancer cells and lymphocytes by ovine uterine serpin
BMC Cell Biol.
9
5
2008
Mus musculus (P29121)
brenda
Akamatsu, T.; Azlina, A.; Purwanti, N.; Karabasil, M.R.; Hasegawa, T.; Yao, C.; Hosoi, K.
Inhibition and transcriptional silencing of a subtilisin-like proprotein convertase, PACE4/SPC4, reduces the branching morphogenesis of and AQP5 expression in rat embryonic submandibular gland
Dev. Biol.
325
434-443
2009
Rattus norvegicus (Q78EH2)
brenda
Remacle, A.G.; Shiryaev, S.A.; Oh, E.S.; Cieplak, P.; Srinivasan, A.; Wei, G.; Liddington, R.C.; Ratnikov, B.I.; Parent, A.; Desjardins, R.; Day, R.; Smith, J.W.; Lebl, M.; Strongin, A.Y.
Substrate cleavage analysis of furin and related proprotein convertases. A comparative study
J. Biol. Chem.
283
20897-20906
2008
Homo sapiens (P29122), Homo sapiens
brenda
Komiyama, T.; Coppola, J.M.; Larsen, M.J.; van Dort, M.E.; Ross, B.D.; Day, R.; Rehemtulla, A.; Fuller, R.S.
Inhibition of furin/PC-catalyzed surface and intracellular processing by small molecules
J. Biol. Chem.
284
15729-15738
2009
Rattus norvegicus (Q78EH2)
brenda
Xiao, Y.; Chen, G.; Richard, J.; Rougeau, N.; Li, H.; Seidah, N.G.; Cohen, E.A.
Cell-surface processing of extracellular human immunodeficiency virus type 1 Vpr by proprotein convertases
Virology
372
384-397
2008
Homo sapiens (Q6UW60), Homo sapiens
brenda
Fuller, J.A.; Brun-Zinkernagel, A.M.; Clark, A.F.; Wordinger, R.J.
Subtilisin-like proprotein convertase expression, localization, and activation in the human retina and optic nerve head
Invest. Ophthalmol. Vis. Sci.
50
5759-5768
2009
Homo sapiens
brenda
Byun, S.; Tortorella, M.D.; Malfait, A.M.; Fok, K.; Frank, E.H.; Grodzinsky, A.J.
Transport and equilibrium uptake of a peptide inhibitor of PACE4 into articular cartilage is dominated by electrostatic interactions
Arch. Biochem. Biophys.
499
32-39
2010
Rattus norvegicus
brenda
Yuasa, K.; Masuda, T.; Yoshikawa, C.; Nagahama, M.; Matsuda, Y.; Tsuji, A.
Subtilisin-like proprotein convertase PACE4 is required for skeletal muscle differentiation
J. Biochem.
146
407-415
2009
Mus musculus
brenda
Akamatsu, T.; Azlina, A.; Javkhlan, P.; Hasegawa, T.; Yao, C.; Hosoi, K.
Salivary gland development: its mediation by a subtilisin-like proprotein convertase, PACE4
J. Med. Invest.
56
241-246
2009
Rattus norvegicus
brenda
Mesnard, D.; Donnison, M.; Fuerer, C.; Pfeffer, P.L.; Constam, D.B.
The microenvironment patterns the pluripotent mouse epiblast through paracrine Furin and Pace4 proteolytic activities
Genes Dev.
25
1871-1880
2011
Mus musculus
brenda
Akamatsu, T.
Physiological role of a subtilisin - Like proprotein convertase, PACE4, in submandibular gland development
J. Oral Biosci.
52
81-93
2010
Rattus norvegicus
-
brenda
Yuasa, K.; Futamatsu, G.; Kawano, T.; Muroshita, M.; Kageyama, Y.; Taichi, H.; Ishikawa, H.; Nagahama, M.; Matsuda, Y.; Tsuji, A.
Subtilisin-like proprotein convertase paired basic amino acid-cleaving enzyme 4 is required for chondrogenic differentiation in ATDC5 cells
FEBS J.
279
3997-4009
2012
Mus musculus
brenda
Kara, I.; Poggi, M.; Bonardo, B.; Govers, R.; Landrier, J.F.; Tian, S.; Leibiger, I.; Day, R.; Creemers, J.W.; Peiretti, F.
The paired basic amino acid-cleaving enzyme 4 (PACE4) is involved in the maturation of insulin receptor isoform B: an opportunity to reduce the specific insulin receptor-dependent effects of insulin-like growth factor 2 (IGF2)
J. Biol. Chem.
290
2812-2821
2015
Homo sapiens (P29122)
brenda
Kim, H.; Tabata, A.; Tomoyasu, T.; Ueno, T.; Uchiyama, S.; Yuasa, K.; Tsuji, A.; Nagamune, H.
Estrogen stimuli promote osteoblastic differentiation via the subtilisin-like proprotein convertase PACE4 in MC3T3-E1 cells
J. Bone Miner. Metab.
33
30-39
2015
Mus musculus
brenda
Kwiatkowska, A.; Couture, F.; Levesque, C.; Ly, K.; Beauchemin, S.; Desjardins, R.; Neugebauer, W.; Dory, Y.L.; Day, R.
Novel insights into structure-activity relationships of N-terminally modified PACE4 inhibitors
ChemMedChem
11
289-301
2016
Homo sapiens (P29122)
brenda
Dianati, V.; Shamloo, A.; Kwiatkowska, A.; Desjardins, R.; Soldera, A.; Day, R.; Dory, Y.L.
Rational design of a highly potent and selective peptide inhibitor of PACE4 by salt bridge interaction with D160 at position P3
ChemMedChem
12
1169-1172
2017
Homo sapiens (P29122)
brenda
Yao, Z.; Sun, B.; Hong, Q.; Yan, J.; Mu, D.; Li, J.; Sheng, H.; Guo, H.
PACE4 regulates apoptosis in human prostate cancer cells via endoplasmic reticulum stress and mitochondrial signaling pathways
Drug Des. Devel. Ther.
9
5911-5923
2015
Homo sapiens (P29122), Homo sapiens
brenda
Bessonnard, S.; Mesnard, D.; Constam, D.
PC7 and the related proteases Furin and Pace4 regulate E-cadherin function during blastocyst formation
J. Cell Biol.
210
1185-1197
2015
Mus musculus
brenda
Lin, Y.E.; Wu, Q.N.; Lin, X.D.; Li, G.Q.; Zhang, Y.J.
Expression of paired basic amino acid-cleaving enzyme 4 (PACE4) correlated with prognosis in non-small cell lung cancer (NSCLC) patients
J. Thorac. Dis.
7
850-860
2015
Homo sapiens (P29122), Homo sapiens
brenda
Wang, F.; Wang, L.; Pan, J.
PACE4 regulates proliferation, migration and invasion in human breast cancer MDA-MB-231 cells
Mol. Med. Rep.
11
698-704
2015
Homo sapiens (P29122), Homo sapiens
brenda
Tian, X.F.; Huang, G.M.; Zang, H.L.; Cao, H.
PACE4 regulates apoptosis in human pancreatic cancer Panc-1 cells via the mitochondrial signaling pathway
Mol. Med. Rep.
14
5205-5210
2016
Homo sapiens (P29122), Homo sapiens
brenda
Mohammad, A.H.; Couture, F.; Gamache, I.; Chen, O.; El-Assaad, W.; Abdel-Malak, N.; Kwiatkowska, A.; Muller, W.; Day, R.; Teodoro, J.G.
Cleavage of the V-ATPase associated prorenin receptor is mediated by PACE4 and is essential for growth of prostate cancer cells
PLoS ONE
18
e0288622
2023
Homo sapiens (P29122), Mus musculus (Q62030)
brenda
Couture, F.; Wang, L.; Dufour, F.; Chabot-Maheux, K.; Ekindi Ndongo, N.; Sabbagh, R.; Day, R.
PACE4-altCT isoform of proprotein convertase PACE4 as tissue and plasmatic biomarker for prostate cancer
Sci. Rep.
12
6066
2022
Homo sapiens (P29122)
brenda
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