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Information on EC 3.4.21.93 - Proprotein convertase 1
for references in articles please use BRENDA:EC3.4.21.93
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.93 Proprotein convertase 1
IUBMB Comments
A Ca2+-dependent enzyme, maximally active at about pH 5.5. Substrates include pro-opiomelanocortin, prorenin, proenkephalin, prodynorphin, prosomatostatin and proinsulin. Unlike prohormone convertase 2, does not hydrolyse proluteinizing-hormone-releasing-hormone. Unusually, processing of prodynorphin occurs at a bond in which P2 is Thr. Present in the regulated secretory pathway of neuroendocrine cells, commonly acting co-operatively with prohormone convertase 2. In peptidase family S8 (subtilisin family)
The enzyme appears in viruses and cellular organisms
- 3.4.21.93
- obesity
- proinsulin
- proglucagon
-
subtilisin-like
- endoproteases
- medicine
-
tmem18
-
proneuropeptides
- drug development
- analysis
Reaction Schemes
showrelease of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-/- bonds
Synonyms
pcsk1, pc1/pc3, prohormone convertase 3, proprotein convertase 1, proprotein convertase pc1/3, mpc1/3, propeptide convertase, furin homolog, neuroendocrine convertase 1, protein convertase 1/3, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Furin homolog
-
-
-
-
Neuroendocrine convertase 1
PC 1/3
PC1
PC1/3
PC1/PC3
PC3
PCSK1
prohormone convertase
prohormone convertase 1
prohormone convertase 1/3
Prohormone convertase 3
-
-
-
-
prohormone convertase PC3
Propeptide processing protease
-
-
-
-
proprotein convertase 1/3
proprotein convertase PC1
additional information
-
also cf. EC 3.4.21.75. Prohormone convertases are calcium-dependent serine endoproteases of the subtilisin family
Neuroendocrine convertase 1
-
-
-
-
PC1
-
-
-
-
PC1/3
-
-
PC3
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-/- bonds
release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-/- bonds
-
-
-
-
release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-/- bonds
active site and substrate binding structure, enzyme-substrate interactions at prime and non-prime subsites
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
99676-46-7
-
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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
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala + H2O
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg + Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
Substrates: -
Products: -
Products: -
?
Boc-Arg-Val-Arg-Arg-4-methyl-coumaryl-7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
brain-derived neurotrophic factor precursor protein + H2O
brain-derived neurotrophic factor + ?
-
Substrates: -
Products: -
Products: -
?
cholecystokinin 8-containing peptide + H2O
?
-
Substrates: a synthetic peptide substrate containing the CCK 8 Gly Arg Arg peptide sequence, i.e. DYMGWMDF, and the cleavage site of pro-cholecystokinin for its liberation, overview
Products: -
Products: -
?
glucose-dependent insulinotropic polypeptide precursor + H2O
glucose-dependent insulinotropic polypeptide + propeptide of glucose-dependent insulinotropic polypeptide
L-pGlu-L-Arg-L-Thr-L-Lys-Arg-7-amido-4-methylcoumarin + H2O
L-pGlu-L-Arg-L-Thr-L-Lys-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
pGlu-Arg-Thr-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
Substrates: -
Products: -
Products: -
?
pGlu-Arg-Thr-Lys-Arg-4-methyl-coumaryl-7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin-7-amide + H2O
?
-
Substrates: -
Products: -
Products: -
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pro-cholecystokinin + H2O
N-terminal propeptide + C-terminal cholecystokinin 8 Gly Arg Arg peptide + remaining CCK peptide
-
Substrates: the substrate is only cleaved in vivo since defolding proteins ar required, in vitro the cleavage site is inaccessible for the enzyme
Products: peptide product analysis
Products: peptide product analysis
?
pro-cholecystokinin + H2O
N-terminal propeptide + cholecystokinin 58
-
Substrates: the substrate is only cleaved at the CKK 8 peptide in vivo since defolding proteins ar required, in vitro the cleavage site is inaccessible for the enzyme
Products: peptide product analysis
Products: peptide product analysis
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + GHRH-RP + pro-peptide of growth hormone-releasing hormone
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + pro-peptide of growth hormone-releasing hormone
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-peptides of islet amyloid polypeptide
-
Substrates: precursor of IAPP or amylin, the major component of islet amyloid, cleavage at the C- and N-terminus
Products: -
Products: -
?
pro-opiomelanocortin + H2O
bioactive ACTH + ?
-
Substrates: -
Products: -
Products: -
?
progastrin + H2O
gastrin-34 + gastrin-17
-
Substrates: PC1/3 initiates cleavage at the N-terminal di-arginine site (Arg36-Arg37) at an early stage in the processing. The endoproteolytic maturation of progastrin in normal G-cells appears to require an interplay, primarily between PC1/3 and PC2. Processing may begin with PC1/3, which is solely responsible for the cleavage of Arg36-Arg37. Subsequently, PC1/3 cleaves the crucial Arg73-Arg74. Later, in secretory granules, PC2 performs the partial cleavage of Lys53-Lys54 to ensure the production of gastrin-17
Products: -
Products: -
?
proglucagon + H2O
glicentin + major proglucagon fragment
-
Substrates: can be differentially processed to produce alternative final products, depending on the cell type in which they are expressed
Products: -
Products: -
?
proglucagon1-158 + H2O
oxyntomodulin + glicentin-related polypeptide + IP2/GLP-2
-
Substrates: glicentin lacks the signal sequence of proglucagon, residues -20-1, recombinant hamster substrate and murine enzyme co-expressed in rat GH4C1 cells, low activity, cleavage at the proglucagon interdomain site Lys70-Arg71-/-, and at Lys31-Arg32-/-
Products: mature glucagon consists of residues 33-61, glicentin-related polypeptide comprises the C-terminal residues 1-32, GLP-1 is the N-terminal glucagon-like peptide comprising residues 62-69, IP2/GLP-2 comprises residues 72-158
Products: mature glucagon consists of residues 33-61, glicentin-related polypeptide comprises the C-terminal residues 1-32, GLP-1 is the N-terminal glucagon-like peptide comprising residues 62-69, IP2/GLP-2 comprises residues 72-158
?
proopiomelanocortin + H2O
?
-
Substrates: is cleaved by prohormone convertase 1/3 to produce peptides that regulate the body's response to energy availability
Products: -
Products: -
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
somatostatin + H2O
?
-
Substrates: PC1 may function as sorting element for somatostatin for its maturation and processing to appropiate targets
Products: -
Products: -
?
glucose-dependent insulinotropic polypeptide precursor + H2O
glucose-dependent insulinotropic polypeptide + propeptide of glucose-dependent insulinotropic polypeptide
-
Substrates: PC1/3 is essential for pro-GIP processing
Products: GIP
Products: GIP
?
glucose-dependent insulinotropic polypeptide precursor + H2O
glucose-dependent insulinotropic polypeptide + propeptide of glucose-dependent insulinotropic polypeptide
-
Substrates: i.e. pro-GIP, incretin hormone
Products: GIP
Products: GIP
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
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: -
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
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-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + GHRH-RP + pro-peptide of growth hormone-releasing hormone
-
Substrates: posttranslational processing mechanism, PC1 is the primary enzyme involved in the processing, overview
Products: -
Products: -
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + GHRH-RP + pro-peptide of growth hormone-releasing hormone
-
Substrates: proGHRH, processing
Products: products are the pro-peptide of 1.7 kDa, the mature GHRH of 5.2 kDa, and GHRH-RP of 3.6 kDa
Products: products are the pro-peptide of 1.7 kDa, the mature GHRH of 5.2 kDa, and GHRH-RP of 3.6 kDa
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + pro-peptide of growth hormone-releasing hormone
-
Substrates: PC1/3 and furin, EC 3.4.21.75, are major processing enzymes, processing overview
Products: -
Products: -
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + pro-peptide of growth hormone-releasing hormone
-
Substrates: pro-GHRH, processing, cleavage of C-terminal -RXRXXR-/-, cleavage site specificity determination by substrate mutational analysis, activity with pro-GHRH mutants R8A, R11A, and Q10R, overview
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
Substrates: -
Products: small amounts of beta-endorphin
Products: small amounts of beta-endorphin
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
Substrates: -
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
Substrates: -
Products: small amounts of beta-endorphin
Products: small amounts of beta-endorphin
?
Pro-opiomelanocortin + H2O
Adrenocorticotropic hormone + beta-lipotropin + beta endorphin
-
Substrates: -
Products: -
Products: -
?
pro-thyrotropin-releasing hormone + H2O
fragments of pro-thyrotropin-releasing hormone
-
Substrates: prohormone processing within the regulated secretory pathway of neuroendocrine cells
Products: 5 TRH peptide and 7 to 9 other peptides
Products: 5 TRH peptide and 7 to 9 other peptides
?
pro-thyrotropin-releasing hormone + H2O
fragments of pro-thyrotropin-releasing hormone
-
Substrates: activity with wild-type and mutant pro-TRH, expressed in murine AtT20 cells, recognized epitopes and moieties in pro-TRH by PC1, overview
Products: 5 TRH peptide and 7 to 9 other peptides
Products: 5 TRH peptide and 7 to 9 other peptides
?
prodynorphin + H2O
dynorphin + ?
-
Substrates: hydrolyzes peptide bonds with Tyr at position P2
Products: -
Products: -
?
prodynorphin + H2O
dynorphin + ?
-
Substrates: hydrolyzes peptide bonds with Tyr at position P2
Products: -
Products: -
?
Proinsulin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
Proinsulin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
Proinsulin + H2O
Insulin + ?
-
Substrates: cleaves at both C peptide junctions to release rat insulin I but generates a larger proportion of intermediate cleaved at the B chain-C peptide junction, indicating a preference for this site
Products: -
Products: -
?
Proinsulin + H2O
Insulin + ?
-
Substrates: cleaves at both C peptide junctions to release rat insulin I but generates a larger proportion of intermediate cleaved at the B chain-C peptide junction, indicating a preference for this site
Products: -
Products: -
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
-
Substrates: processing and activation of the inactive prohormone is required for regulation of energy balance via leptin, enzyme regulation, overview
Products: -
Products: -
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
-
Substrates: processing of the prohormone
Products: -
Products: -
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
Products: -
Products: -
?
additional information
?
-
-
Substrates: unlike prohormone convertase 2, does not hydrolyze proluteinizing-hormone-releasing-hormone
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleaves precursors both at specific single and pairs of basic residues
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of peptide hormones by processing of larger precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme capable of processing a variety of prohormones to their bioactive forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows specific binding protein 7B2
Products: -
Products: -
?
additional information
?
-
-
Substrates: enhanced proprotein convertase 1/3 levels, leading to improved processing of proinsulin and proglucagon, may contribute to the benefits of pioglitazone therapy
Products: -
Products: -
?
additional information
?
-
-
Substrates: a congenital deficiency of prohormone convertase 1/3 which cleaves POMC, AgRP, cholecystokinin, proglucagon, glucagon-like peptide-1 and pro-insulin leads to a syndrome characterized by obesity, small intestinal dysfunction, hyperphagia and dysregulation of glucose homeostasis
Products: -
Products: -
?
additional information
?
-
-
Substrates: unlike prohormone convertase 2, does not hydrolyze proluteinizing-hormone-releasing-hormone
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleaves precursors both at specific single and pairs of basic residues
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleaves polypeptide hormones and many proteins at specific sites
Products: -
Products: -
?
additional information
?
-
-
Substrates: constitutive secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: implicated in processing of proproteins in the secretory pathway, synthesized as a zymogen, cleaves his own profragment in the endoplasmic reticulum
Products: -
Products: -
?
additional information
?
-
-
Substrates: regulated secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the regulated secretory pathway in neuroendocrine cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the regulated secretory pathway in neuroendocrine cells, the enzyme activity is regulated by the PC1-propeptide and by proSAAS CT peptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleavage site specificity, activity with mutant proglucagon and truncation variants, analysis of importance of substrate domain structure, molecular modeling, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PC1/3 CT peptide is not cleaved by enzymatically active PC1/3
Products: -
Products: -
?
additional information
?
-
-
Substrates: prohormone convertase 1/3 mRNA levels in the arcuate nucleus respond normally to signals of energy availability in wild-type mice but not in N2KO mice
Products: -
Products: -
?
additional information
?
-
-
Substrates: constitutive secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme capable of processing a variety of prohormones to their bioactive forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: regulated secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: constitutive secretory pathway
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
brain-derived neurotrophic factor precursor protein + H2O
brain-derived neurotrophic factor + ?
-
Substrates: -
Products: -
Products: -
?
glucose-dependent insulinotropic polypeptide precursor + H2O
glucose-dependent insulinotropic polypeptide + propeptide of glucose-dependent insulinotropic polypeptide
-
Substrates: PC1/3 is essential for pro-GIP processing
Products: GIP
Products: GIP
?
pro-cholecystokinin + H2O
N-terminal propeptide + C-terminal cholecystokinin 8 Gly Arg Arg peptide + remaining CCK peptide
-
Substrates: the substrate is only cleaved in vivo since defolding proteins ar required, in vitro the cleavage site is inaccessible for the enzyme
Products: peptide product analysis
Products: peptide product analysis
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + GHRH-RP + pro-peptide of growth hormone-releasing hormone
-
Substrates: posttranslational processing mechanism, PC1 is the primary enzyme involved in the processing, overview
Products: -
Products: -
?
pro-growth hormone-releasing hormone + H2O
growth hormone-releasing hormone + pro-peptide of growth hormone-releasing hormone
-
Substrates: PC1/3 and furin, EC 3.4.21.75, are major processing enzymes, processing overview
Products: -
Products: -
?
pro-islet amyloid polypeptide + H2O
islet amyloid polypeptide + pro-peptides of islet amyloid polypeptide
-
Substrates: precursor of IAPP or amylin, the major component of islet amyloid, cleavage at the C- and N-terminus
Products: -
Products: -
?
pro-thyrotropin-releasing hormone + H2O
fragments of pro-thyrotropin-releasing hormone
-
Substrates: prohormone processing within the regulated secretory pathway of neuroendocrine cells
Products: 5 TRH peptide and 7 to 9 other peptides
Products: 5 TRH peptide and 7 to 9 other peptides
?
prothyrotropin-releasing hormone + H2O
thyrotropin-releasing hormone + pro-peptide of thyrotropin-releasing hormone
-
Substrates: processing and activation of the inactive prohormone is required for regulation of energy balance via leptin, enzyme regulation, overview
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
Proinsulin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
Proinsulin + H2O
?
-
Substrates: the enzyme together with prohormone convertase 2 represents the major secretory granule processing activity responsible for processing neuroendocrine precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
Products: -
Products: -
?
additional information
?
-
-
Substrates: biosynthesis of peptide hormones by processing of larger precursors
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme capable of processing a variety of prohormones to their bioactive forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleaves polypeptide hormones and many proteins at specific sites
Products: -
Products: -
?
additional information
?
-
-
Substrates: constitutive secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: implicated in processing of proproteins in the secretory pathway, synthesized as a zymogen, cleaves his own profragment in the endoplasmic reticulum
Products: -
Products: -
?
additional information
?
-
-
Substrates: regulated secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the regulated secretory pathway in neuroendocrine cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in the regulated secretory pathway in neuroendocrine cells, the enzyme activity is regulated by the PC1-propeptide and by proSAAS CT peptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: constitutive secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme capable of processing a variety of prohormones to their bioactive forms
Products: -
Products: -
?
additional information
?
-
-
Substrates: regulated secretory pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: constitutive secretory pathway
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PC1/3 CT peptide
-
decreases PC1/3 activity at high concentrations (micromol range)
-
proSAAS CT peptide
-
endogenous inhibitor, inhibits the C-terminal PC1 processing
-
Synthetic inhibitor
-
can be used for developing an affinity purification procedure
-
morphine
-
human prohormone convertase 1/3 promoter activity is 73.1% in GH3-mu-opioid receptor cells receiving morphine compared with cells receiving media, and this reduction is reversed by naltrexone. In cells transfected with the prohormone convertase 1/3-minusCRE1/2 promoter construct, morphine does not reduce prohormone convertase 1/3-promoter activity. In wild-type GH3 cells (without the mu-opioid receptor), human prohormone convertase 1/3 promoter does not respond to morphine treatment. Regulation of prohormone convertase 1/3 promoter activity by morphine is mediated through the mu-opioid receptor
morphine
-
short-term morphine (24 h) exposure downregulates prohormone convertase 1/3 protein levels in the rat hypothalamus. The cyclic-AMP response element in the promoter of prohormone convertase 1/3 is required for morphine-induced regulation of prohormone convertase 1/3
PC1/3 propeptide
inhibits the mature enzyme competitively, inhibition mechanism, interaction with the enzyme at the 50RRSRR54, 61KR62 and 65DDD67 sequences, molecular modeling, overview
-
additional information
-
proprotein convertase 1/3 expression is reduced in Bon-1 cells overexpressing Pdcd4
-
additional information
-
in wild-type mice prohormone convertase 1/3 mRNA levels show a 75% reduction with food deprivation and exceed ad libitum-fed levels after leptin treatment. Hypothalamic prohormone convertase 1/3 mRNA levels in N2KO mice show no significant variation between the deprived condition and ad libitum feeding. Leptin-treated N2KO mice have significantly lower prohormone convertase 1/3 mRNA levels than leptin-treated wild-type mice
-
additional information
-
starvation reduces the serum levels of leptin which decreases PC1 expression, the effect can be reversed by administration of exogenous leptin
-
additional information
-
hyperthyroidism suppresses enzyme expression in hypothalamus and cerebral cortex
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-n-propyl-2-thiouracil
-
produces hypothyroidism and induces a significant increase in the expression of PC1/3 in the paraventricular nucleus and lateral hypothalamus, but not ventromedial nucleus. Regulates colocalization of PC1/3 or PC2 in pro-thyrotropin-releasing hormone in the paraventricular nucleus, but not in lateral hypothalamus and ventromedial nucleus
leptin
-
leptin stimulation of the prohormone convertase 1/3 promoter is regulated by Nhlh2 and STAT3 in vitro. Nhlh2 binds to both E-box motifs on the prohormone convertase 1/3 promoter. The Nhlh2 and STAT3 transcription factors heterodimerize and interact on the prohormone convertase 1/3 promoter. Leptin-treated N2KO mice have significantly higher prohormone convertase 1/3 mRNA levels than ad libitum-fed N2KO mice
-
morphine
-
long-term morphine exposure (7 days) upregulates prohormone convertase 1/3 protein levels in the rat hypothalamus. The cyclic-AMP response element in the promoter of prohormone convertase 1/3 is required for morphine-induced regulation of prohormone convertase 1/3
PC1/3 CT peptide
-
increases PC1/3 activity at low concentrations (nanomol range). Interaction with the active site of PC1/3 does not result in the formation of a stable complex. Activation of PC1/3 by 5 nanomol CT-peptide is the same in the presence or absence of propeptide
-
pioglitazone
-
oral medication used in the treatment of type 2 diabetes, which decreases Pdcd4 levels, activates Akt, increases CgA and Sg II secretion and augments proprotein convertase 1/3 protein in Bon-1 cells. 7fold increase in proprotein convertase 1/3 mRNA in shPdcd4-transfected cells
additional information
-
leptin stimulates the PC1 expression via STAT3 acting on the PC1 promoter
-
additional information
-
hypothyroidism increases enzyme expression in hypothalamus and cerebral cortex
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0024
proPC1/3 55-83 SALHITKRLSDDDRVTWAEQQYEKERSKR
-
pH 7.0, 25°C, mixed inhibition
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
different purified recombinant PC1 constructs, overview
additional information
-
pro-TRH-derived peptide production levels in wild-type and recombinant GH4C1 and AtT20 cells, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.5 - 6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
at pH 7.8 increase of enzymatic activity up to 50-60%, irrespective of the amount of PC1/3 CT peptide used up to 0.005 mM
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DNA samples from three genetic types reared in the Chinese province of Jiangsu: Boer goat, Chinese Xuhuai white goat, and Chinese Haimen goat
UniProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
neuroendocrine cell line, which shows dramatic increase in proprotein convertase 1/3 protein expression after suppression of Pdcd4
brenda
-
PC1/PC3 is absent in undifferentiated bone marrow stromal stem cells, its expression is initiated upon the induction of differentiation. PC1 is expressed at a relatively lower level as compared to enzymes functioning in the constitutive pathway
brenda
-
ischemic cortex after transient focal cerebral ischemia. Both the mRNA and protein levels of PC1 in ischemic cortices decrease gradually at 4, 8, and 16 hours of reperfusion after 100 min of middle cerebral artery occlusion. After 24 hours of reperfusion, enhanced intensities of signals for PC1 protein are observed, while signals for PC1 mRNA remain low
brenda
-
lower expression in comparison to the cortex and striatum. In the hippocampal regions CA1 and CA2 all somatostatin positive interneurons moderately colocalize with PC1, no colocalization of PC1 with carboxypeptidase-E. Weak colocalization between PC1 and carboxypeptidase-E confined to neurons of the pyramidal layer
brenda
-
metastasis originating from colorectal cancer, 2fold increased expression level of PC1 compared to healthy liver, the expression pattern is influenced by colon cancer cells, overview
brenda
additional information
-
paraventricular nucleus, lateral hypothalamus and ventromedial nucleus
brenda
-
colocalization with somatostatin, carboxypeptidase-E and PC2 in pyramidal and non-pyramidal neurons. Colocalization with carboxypeptidase-E confined to pyramidal neurons of deeper layer. PC1 exhibits 26% colocalization with somatostatin and 34% with carboxypeptidase-E
brenda
-
in the digestive gland the PC1 activity of pre-breeding stage is 1.17fold and 1.55fold as that of the during-breeding and the post-breeding stages, respectively
brenda
-
relative activity of PC1 in gonad is 10% of that in the digestive gland. In male, the PC1 activity in digestive gland is slightly lower than in female
brenda
-
increase in prohormone convertase 1/3 is most abundant in the ventral region of the posterior region of the hypothalamic nucleus and in the paraventricular hypothalamic medial area
brenda
-
expressed in larger neurons (interneurons) of the striatum. Either weak or no expression in smaller neurons. Colocalization with somatostatin or carboxypeptidase-E confined to interneurons. PC1 exhibits 11% colocalization with somatostatin and 29% with carboxypeptidase-E in the striatum
brenda
-
discrete expression of PC1/3 in the paraventricular nucleus, lateral hypothalamus and ventromedial nucleus of euthyroid animals
brenda
-
in the dorso-medial nucleus, significant increase in the number of prohormone convertase 1/3-positive neurons after long-term morphine exposure
brenda
-
alpha-cells in the islet of Langerhans express both prohormone convertase 2 and 1/3, which results in the processing of the proglucagon precursor into glucagon-like peptide 1, thereby leading to local production of this beta-cell growth factor. alpha-Cells in the adult basically only express PC2, but significant activation of PC1/3 is also observed in mouse models of insulin resistance such as pregnant, obese, diabetic and prediabetic NOD mice
brenda
additional information
-
overexpression of PC2 in colorectal liver mestatasis correlates with enhanced expression of its specific binding protein 7B2
brenda
additional information
-
alphaTCdeltaPC2 cells express abundant PC1/3, whereas alphaTC-1 cells express little or no PC1/3
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in NR-8383 cells, convertase PC1/3 is localized at the trans-Golgi network and traffics to lysosome-related vesicles upon lipopolysaccharide stimulation. Co-localization of PC1/3 and Toll-like receptor 4 is found upon lipopolysaccharide stimulation
brenda
enzyme is activated in secretory vesicles at pH 5.5
brenda
additional information
-
the enzyme is part of the regulated secretory pathway of neuroendocrine cells
brenda
-
in NR-8383 cells, convertase PC1/3 is localized at the trans-Golgi network and traffics to lysosome-related vesicles upon lipopolysaccharide stimulation
brenda
-
peripherally attached to the secretory granule membrane, the enzyme is no transmembrane protein, subcellular localization analysis, overview
brenda
-
full length PC3 is associated with lipid rafts in Neuro2A cells, undergoes stimulated secretion and is colocalized with the secretory granule marker, chromogranin A, by immunocytochemistry
brenda
-
the enzyme is part of the regulated secretory pathway of neuroendocrine cells
brenda
additional information
-
the enzyme is transferred through the endoplasmic reticulum membrane
-
brenda
additional information
-
lacks a hydrophobic transmembrane anchor, but has a potential C-terminal amphipathic helical segment similar to the putative membrane anchor of carboxypeptidase H
-
brenda
additional information
-
the enzyme is localized in the regulated secretory pathway of neuroendocrine cells
-
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
-
PC members are paralogous genes derived from a common ancestor, which represents independent lineages by gene replication in evolution. Abalone PC1 is located in PC1 clade which is orthologous genes in different species. The potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
malfunction
-
preprotein convertase 1/3 deficiency is a rare autosomal recessive disorder in which patients present with malabsorptive diarrhea and a series of symptoms of endocrine disorders such as polydipsia, reactive hypoglycemia, growth hormone deficiency, hypothyroidism, adrenal insufficiency, and early onset obesity. In its essence, pituitary hormone deficiency is caused by insufficient cleavage of pituitary prohormones
physiological function
physiological function
-
the enzyme plays a key role in the posttranslational processing of precursors for bioactive peptides
physiological function
-
PC1 is a potential prohormone processing enzyme and plays a critical role in abalone physiological processes related to reproduction
physiological function
-
downregulation of convertase PC1/3 by shRNA produces a phenotype in NR-8383 cells similar to isolated peritoneal macrophages. PC1/3 shRNA induces changes in the cellular organization and expression of the specific trafficking regulator RAB GTPase. NR-8383 cells down-regulated for PC1/3 present an abnormal cytokine secretion profile
physiological function
-
conditional Pick1-knockout mice lacking protein interacting with C-kinase 1, show elevated proinsulin levels in the circulation and in the pancreatic islets, accompanied by a reduction in the proinsulin processing enzyme prohormone convertase 1/3. The deletion of Pick1 triggers the specific elimination of chromogranin B in pancreatic beta cells
physiological function
-
proprotein convertase PC1/3 regulates the endosomal toll-like receptor TLR9. Under CpG oligodesoxynucleotide challenge, PC1/3 traffics rapidly to colocalize with TLR9 in CpG oligodesoxynucleotide-containing endosomes with acidic pH. In PC1/3 knockdown macrophages, compartmentalization of TLR9 is altered and TLR9 clustered in multivesicular bodies. This clustering of TLR9 in multivesicular bodies dampens the anti-inflammatory STAT3 signalling pathway while it promotes the pro-inflammatory NF-kappaB pathway
physiological function
-
cleavage of brain-derived neurotrophic factor (BNDF) by the enzyme is critical for the conversion of precursor protein of BDNF in rat cortical neurons during ischemia
Show AA Sequence and Transmembrane Helices (989 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
71000
85000
87000
66000
-
Western blotting, intramolecular autocatalytically cleaved 85 kDa isoform
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
amino acid sequence alignment of soluble ectodomain and active site cleft, domain structures, enzyme structure modeling based on the crystal structures of furin and kexin, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
-
the PC3 C-terminus is not accessible to cytosolic protein kinase, recombinant PC3 is not phosphorylated in transfected COS-1 cells at a C-terminal phosphorylation site
glycoprotein
-
the catalytic domain of PC1 contains two potential N-glycosylation sites
glycoprotein
-
the catalytic domain of PC1 contains two N-glycosylation sites, the C-terminal domain contains one N-glycosylation site
proteolytic modification
proteolytic activation occurs in secretory vesicles at pH 5.5. The pKa of the conserved histidine in proprotein convertase 1/3 is acid-shifted compared with furin and is consistent with its lower pH of activation
proteolytic modification
-
PC1 zymogen is activated by proteolytic cleavage of the signal and the propeptide and is processed at the C-terminal domain, which is regulated by the separate PC1 propeptide and the SAAS CT propeptide, overview
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N309K
naturally occuring mutation identified in four siblings presenting with congenital diarrhea and various endocrinopathies. The mutation affects the oxyanion hole transition state-stabilizing amino acid within the active site, which is critical for appropriate proprotein maturation and enzyme activity. The N309K mutant protein exhibits normal, though slowed, prodomain removal and is secreted from both HEK-293 and Neuro-2A cells. The secreted enzyme shows no catalytic activity, and is not processed into the 66 kDa form
S253L/G255R
-
the mutations are found in a patient shortly after birth with uncorrectable diarrhea and symptoms of metabolic acidosis with hypothyroidism. The proteins expressed by the mutations show a significant decrease in the enzyme activity compared to the wild type
S307L
-
naturally occurring mutation (patient homozygous for the mutation). Markedly impairs catalytic activity, intracellular trafficking appears normal. Retains some autocatalytic activity, even though it is completely inactive on other substrates. Patient has obesity and persistent diarrhea, but no history of reactive hypoglycemia. Hyperphagia makes a major contribution to the obesity in this syndrome
S357G
mutant represents a prohormone convertase PC1/3 hypermorph. Mutant protein exhibits a lower calcium dependence, a higher pH optimum, and a higher resistance to peptide inhibitors than the wild-type enzyme. The mutant exhibits increased cleavage to the C-terminally truncated form, and kinetic parameters of the full-length and truncated mutant enzymes are also altered. The S357G mutation broadens the specificity of the enzyme, it displays proprotein convertase 2-like specificity on the substrate proCART, the precursor of the cocaine- and amphetamine regulated transcript neuropeptide. The mutant enzyme possesses unusual processing activity that may significantly change the profile of circulating peptide hormones
D65A
site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
D66A
site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
D67A
site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
K61A
site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
N222D
-
leads to obesity, abnormal proinsulin processing, reduced fecundity, impaired autocatalysis and multiple endocrinological defects in mice homozygous for the mutation. Increased energy intake, a more efficient metabolism and reduced alpha-MSH signaling contribute to the obesity. Heterozygous littermates exhibit an intermediate phenotype for both sexes, thus this mutation results in a semi-dominant phenotype
R50A
site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
R51A
site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
R53A
site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
R54A
site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
R62A
site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
S52A
site-directed mutagenesis of the propeptide residue, unaltered inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
S52A/R53A
site-directed mutagenesis of the propeptide residues, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide
N222D
-
leads to obesity, abnormal proinsulin processing, reduced fecundity, impaired autocatalysis and multiple endocrinological defects in mice homozygous for the mutation. Increased energy intake, a more efficient metabolism and reduced alpha-MSH signaling contribute to the obesity. Heterozygous littermates exhibit an intermediate phenotype for both sexes, thus this mutation results in a semi-dominant phenotype
-
additional information
additional information
identification of polymorphisms of the PC1 gene in 447 individuals from three breeds. Only the P1, P2, P3, P9, and P10 loci show polymorphisms, and 12 SNPs in the PC1 gene have been identified. The polymorphisms are significantly associated with caprine body height and chest circumference
additional information
-
construction of an PC3 containing a 19 amino-acid transmembrane sequence, and/or a C-terminal glycosylation tag, the C-terminal extension is exposed to the endoplasmic reticulum lumen, overview
additional information
-
generation of chimeric PC1-propeptide/SAAS CT peptide constructs, effects on C-terminal PC1 processing are limited to the construct containing the PC1 propeptide alone when expressed in AtT20 cells, while both the PC1 propeptide and the SAAS CT propeptide are inhibitory on C-terminal PC1 zymogen processing when expressed in HEK293 cells, overview
additional information
-
construction of PC1 prosegment, amino acids 1-110, fused to the C-terminal PC1 tail, amino acids 619-753, termed proCT construct
additional information
single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme
additional information
-
PC1/3 null mutant mice show C-terminally impaired but not completely blocked proIAPP processing, overview
additional information
-
concentration of progastrin in the antrum of PC1/3-null mice is elevated 3fold. Progastrin molecule is only partly cleaved at the dibasic Arg36-Arg37 site and even less at the Lys53-Lys54 site in the PC1/3-null mice
additional information
-
PC1/3DELTA significantly decreases prohormone convertase 1/3 promoter activity by more than 60%. A 50% reduction when both E-boxes are mutated, even though the STAT3 sites remain intact (PC1/3DELTAE12). Mutation of both STAT3 sites (PC1/3DELTAS12) does not affect basal prohormone convertase 1/3 promoter activity, but leptin stimulation is lost. Mutating the E-box furthest from the start site (E-box 1, PC1/3DELTAE1) only has a significant effect on prohormone convertase 1/3 promoter activity under leptin stimulation, whereas mutating the E-box closest to the start site (E-box 2, PC1/3DELTAE2) has a more pronounced effect on luciferase expression with a loss of approximately 50% prohormone convertase 1/3 promoter activity levels in both leptin-stimulated and unstimulated cells
additional information
-
design of prohormone convertase-2-specific mutations into the catalytic domain of PC1/3 in order to investigate the molecular contributions of these sequences to PC1/3-specific properties. The exchange of residues RQG314 with the SY sequence present in the same location within PC2 shifts the pH optimum of PC1/3 upward into the neutral range, other mutations in the catalytic domain had no effect. None of the full-length PC1/3 mutants examined exhibits increased specific activity, but the 66-kDa form of the RQG314SY mutant is 2 to 4 times more active than the 66-kDa form of wild-type PC1/3. Mutation of GIVTDA243248 to QPFMTDI, a molecular determinant of 7B2 binding, results in increased zymogen expression but no propeptide cleavage or secretion, suggesting that this mutant is trapped in the endoplasmic reticulum. None of the mutations examined confers PC2-specific properties. No mutant exhibits altered calcium requirements
additional information
-
carboxyl terminus-truncated PC3 (1-638) containing the transmembrane domain is associated with lipid rafts in Neuro2A cells, while PC3 (1-616) and PC3-deltaTM lacking the transmembrane domain are not. PC3 (1-638) undergoes stimulated secretion and is colocalized with the secretory granule marker, chromogranin A, by immunocytochemistry. In contrast, PC3 (1-616) and PC3-deltaTM are constitutively secreted and primarily localized in the Golgi
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a synthetic inhibitor can be used for developing an affinity purification procedure
-
recombinant enzyme from insect cells and larvae, about 48fold from larvae by PEG precipitation, concanavalin A affinity and hydroxyapatite chromatography, and gel filtration
-
recombinant PC1/3 purified. PC1/3 CT peptide purified by His-affinity chromatography and RP-HPLC
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-expression of PC1/3 and rat pro-islet amyloid polypeptide, proIAPP, in GH3 cells lacking the enzyme, leads to cleavage of recombinant proIAPP
-
expressed in GH4 cells, entire C-terminal tail of PC1 overexpressed in AtT-20 cells
-
expression in Spodoptera frugiperda Sf9 cells and Trichoplusioa ni larvae using the baculovirus Autographa californica transfection system, method optimization, modification of the enzyme by C-terminal truncation and exchange of the PC1/3 signal peptide for the glycoprotein gp67 signal peptide, overview
-
expression of chimeric PC1-propeptide/SAAS CT peptide constructs in AtT20 cells and in HEK293 cells
-
expression of PC1 in GH3 cells, co-expression with proGHRH or preproGHRH, GH3 cells lack endogenous PC1 but contain PC2, EC 3.4.21.94, another prohormone processing enzyme
-
expression of PC1 in human 293T cells, leptin has a stimulatory effect on the PC1 pomoter, which is enhanced by co-expression of STAT3, overview
-
expression of PC1 using a human PC1 promoter in PC1-deficient GH3 cells, the large region of the PC1 promoter contains negative thyroid hormone response elements which interact with triiodothyronine for regulation of anterior pituitary PC1 mRNA levels, interaction analysis, overview
-
full-length PC3, mutant PC3-deltaTM and truncated forms PC3 (1-638) and PC3 (1-616) expressed in Neuro2A cells
-
hPC1 is expressed in High Five insect cells using a baculovirus protein expression system
-
human PC1 cDNA (amino acids 28-753) amplified, His-tagged and cloned into the MluI and NotI sites of a modified pFASTBAC1 expression vector. Wild-type and mutant N222D human PC1 expressed using baculovirus to infect Sf9 cells
-
into pGL3 basic vector to yield wild-type prohormone convertase 1/3 promoter construct, expressed in N29/2 cell line
-
PC1, DNA and amino acid sequence determination and analysis, phylogenetic tree
-
PC1/3 produced using the baculovirus expression system in Sf9 insect cells or through intracoelemic injection in insect larvae. PC1/3 CT-peptide from positions 592-726 cloned into a pet24b+ bacterial expression vector. The resulting C-terminally His-tagged protein expressed in Escherichia coli strain BL21 (DE3)
-
recombinant enzyme expressed in Sf9 cells, mPC1 cDNA inserted intoAutographa californica nuclear polyhedrosis virus, infection of Sf9 cells, mPC1 insert excised from recombinant vaccinia virus vector containg full-length cDNA
-
transfection of pituitary GH3 cells with promoter for human prohormone convertase 1/3 or with the prohormone convertase 1/3-minusCRE1/2 promoter construct
-
transient enzyme expression in enzyme-deficient rat GH4C1 cells, co-expression with wild-type and mutant proglucagon, glicentin, and/or glicentin-related polypeptide-glucagon, and oxyntomodulin from hamster, overview
-
transient expression of proCT construct in HEK293, FD11, CHO-K1, and AtT20 cells, the proCT construct is processed in the secretory pathway
-
transplantation of encapsulated PC2-expressing alpha TC-1 cells with PC1/3-expressing alpha TCdeltaPC2 cells in normal mice and low-dose streptozotocin-treated mice
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in female digestive gland the PC1 activity of pre-breeding stage is 1.17 and 1.55fold as that of the during-breeding and the post-breeding stages, respectively. The level of PC1 in male individual does not exhibit a significant difference in various reproduction stages
-
in ischemic cortices after 24 hours of reperfusion, enhanced intensities of signals for PC1 protein are observed, while signals for PC1 mRNA remain low
-
patients with type 2 diabetes have increased alpha-cell prohormone convertase 1 levels
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
highly specific and potent PC1 inhibitors proSAAS-(235-246) and proSAAS-(235-244) may be useful in development of an effective affinity procedure for the purification of PC1
drug development
-
repression of proprotein convertase 1/3 by Pdcd4 may represent a novel mechanism for the function of Pdcd4 as a tumour suppressor
medicine
additional information
medicine
-
extension of the clinical and molecular spectrum of human congenital PC1/3 deficiency
medicine
-
transplantation of PC1/3-expressing alpha-cells prevents streptozotocin-induced hyperglycemia by preserving beta-cell area and islet morphology, possibly via stimulating beta-cell replication. Expression of PC1/3 rather than PC2 in alpha-cells induces glucagon-like peptide 1 and glucagon-like peptide 2 production and converts the alpha-cell from a hyperglycemia-promoting cell to one that lowers blood glucose levels. Alteration of proglucagon processing in the alpha-cell may be therapeutically useful in the context of type 1 diabetes
medicine
-
Pc1 N222D homozygous mice are obese and mimic humans with mutations in PC1. This mutation will be a valuable resource in understanding the role of prohormone processing in energy homeostasis
medicine
-
downregulation of prohormone convertase 1/3 by short-term morphine and upregulation by long-term morphine treatment may be a signal mediating the switch from drug use to drug abuse
medicine
-
downregulation of prohormone convertase 1/3 by short-term morphine and upregulation by long-term morphine treatment may be a signal mediating the switch from drug use to drug abuse
medicine
-
significant activation of PC1/3 in the alpha-cells of pancreatic islet is observed in mouse models of insulin resistance such as pregnant, obese, diabetic and prediabetic NOD mice. Data suggest a role of alpha-cells for beta-cell proliferation and further for the endocrine cell network within an islet
medicine
prohormone convertase 1/3 activity is significantly lower in type 2 diabetic patients than in the control group. Decreased activity of prohormone convertase 1/3 rather than prohormone convertase 2 in pancreatic beta-cells is involved in the impaired proinsulin processing, resulting in elevated intact proinsulin levels in type 2 diabetic patients
medicine
UVB irradiation to the eye and stress loading increase the expression of prohormone convertase 1/3 and prohormone convertase 2 in the pituitary gland. The increase in expression of pituitary prohormone convertase 2 is greater in animals subjected to UVB eye irradiation than to stress, whereas no difference is seen between the two groups for the increase in PC1/3
medicine
role of prohormone convertase 1/3 in the transformation of corticotroph cell adenomas into Cushing's disease. Prohormone convertase 1/3 expression is negative or weak in the three patients in the initial phase of corticotroph cell adenoma, while a strong expression is observed in the majority of neoplastic cells in tissue specimens obtained from the same three patients at the time of recurrence as Cushing's disease
medicine
-
Pc1 N222D homozygous mice are obese and mimic humans with mutations in PC1. This mutation will be a valuable resource in understanding the role of prohormone processing in energy homeostasis
-
additional information
-
PC1 may be a potential target for the maturation of somatostatin
additional information
-
transmembrane domain of PC3 plays a key role in sorting the enzyme to the regulated secretory pathway
additional information
-
PC1/3, through its various domains, is capable of controlling its enzymatic activity in all regions of the cell that it encounters
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Steiner, D.F.; Smeekens, S.P.; Ohagi, S.; Chan, S.J.
The new enzymology of precursor processing endoproteases
J. Biol. Chem.
267
23435-23438
1992
Mus musculus, Homo sapiens
brenda
Jean, F.; Basak, A.; DiMaio, J.; Seidah, N.G.; Lazure, C.
An internally quenched fluorogenic substrate of prohormone convertase 1 and furin leads to a potent prohormone convertase inhibitor
Biochem. J.
307
689-695
1995
Homo sapiens
brenda
Smeekens, S.P.; Avruch, A.S.; LaMendola, J.; Chan, S.J.; Steiner, D.F.
Identification of a cDNA encoding a second putative prohormone convertase related to PC2 in AtT20 cells and islets of Langerhans
Proc. Natl. Acad. Sci. USA
88
340-344
1991
Mus musculus
brenda
Seidah, N.G.; Chretien, M.
Pro-protein convertases of subtilisin/kexin family
Methods Enzymol.
244
175-188
1994
Mus musculus, Homo sapiens
brenda
Li, Q.L.; Jansen, E.; Brent, G.A.; Friedman, T.C.
Regulation of prohormone convertase 1 (PC1) by thyroid hormone
Am. J. Physiol. Endocrinol. Metab.
280
E160-170
2001
Homo sapiens, Rattus norvegicus
brenda
Basak, A.; Lazure, C.
Synthetic peptides derived from the prosegments of proprotein convertase 1/3 and furin are potent inhibitors of both enzymes
Biochem. J.
373
231-239
2003
Mus musculus
brenda
Jutras, I.; Seidah, N.G.; Reudelhuber, T.L.; Brechler, V.
Two activation states of the prohormone convertase PC1 in the secretory pathway
J. Biol. Chem.
272
15184-15188
1997
Mus musculus
brenda
Boudreault, A.; Gauthier, D.; Lazure, C.
Proprotein convertase PC1/3-related peptides are potent slow tight-binding inhibitors of murine PC1/3 and Hfurin
J. Biol. Chem.
273
31574-31580
1998
Mus musculus
brenda
Viale, A.; Ortola, C.; Hervieu, G.; Furuta, M.; Barbero, P.; Steiner, D.F.; Seidah, N.G.; Nahon, J.L.
Cellular localization and role of prohormone convertases in the processing of pro-melanin concentrating hormone in mammals
J. Biol. Chem.
274
6536-6545
1999
Mus musculus, Rattus norvegicus, Rattus norvegicus Wistar
brenda
Jutras, I.; Seidah, N.G.; Reudelhuber, T.L.
A predicted alpha-helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway
J. Biol. Chem.
275
40337-40343
2000
Rattus norvegicus, Mus musculus
brenda
Basak, A.; Koch, P.; Dupelle, M.; Fricker, L.D.; Devi, L.A.; Chretien, M.; Seidah, N.G.
Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1
J. Biol. Chem.
276
32720-32728
2001
Mus musculus
brenda
Li, Q.L.; Jansen, E.; Friedman, T.C.
Regulation of prohormone convertase 1 (PC1) by gp130-related cytokines
Mol. Cell. Endocrinol.
158
143-152
1999
Mus musculus, Rattus norvegicus
brenda
Muller, L.; Lindberg, I.
The cell biology of the prohormone convertases PC1 and PC2
Prog. Nucleic Acid Res. Mol. Biol.
63
69-108
1999
Drosophila sp. (in: flies), Rattus norvegicus, no activity in Lymnaea stagnalis, no activity in Caenorhabditis elegans, Mus musculus
brenda
Boudreault, A.; Gauthier, D.; Rondeau, N.; Savaria, D.; Seidah, N.G.; Chretien, M.; Lazure, C.
Molecular characterization, enzymatic analysis, and purification of murine proprotein convertase-1/3 (PC1/PC3) secreted from recombinant baculovirus-infected insect cells
Protein Expr. Purif.
14
353-366
1998
Mus musculus
brenda
Bonic, A.; Mackin, R.B.
Expression, purification, and PC1-mediated processing of human proglucagon, glicentin, and major proglucagon fragment
Protein Expr. Purif.
28
15-24
2003
Homo sapiens
brenda
Stettler, H.; Suri, G.; Spiess, M.
Proprotein convertase PC3 is not a transmembrane protein
Biochemistry
44
5339-5345
2005
Homo sapiens
brenda
Tzimas, G.N.; Chevet, E.; Jenna, S.; Nguyen, D.T.; Khatib, A.M.; Marcus, V.; Zhang, Y.; Chretien, M.; Seidah, N.; Metrakos, P.
Abnormal expression and processing of the proprotein convertases PC1 and PC2 in human colorectal liver metastases
BMC Cancer
5
149
2005
Homo sapiens
brenda
Marzban, L.; Trigo-Gonzalez, G.; Zhu, X.; Rhodes, C.J.; Halban, P.A.; Steiner, D.F.; Verchere, C.B.
Role of beta-cell prohormone convertase (PC)1/3 in processing of pro-islet amyloid polypeptide
Diabetes
53
141-148
2004
Mus musculus
brenda
Posner, S.F.; Vaslet, C.A.; Jurofcik, M.; Lee, A.; Seidah, N.G.; Nillni, E.A.
Stepwise posttranslational processing of pro-growth hormone-releasing hormone (proGHRH) polypeptide by furin and PC1
Endocrine
23
199-213
2004
Mus musculus
brenda
Dey, A.; Norrbom, C.; Zhu, X.; Stein, J.; Zhang, C.; Ueda, K.; Steiner, D.F.
Furin and prohormone convertase 1/3 are major convertases in the processing of mouse pro-growth hormone-releasing hormone
Endocrinology
145
1961-1971
2004
Mus musculus
brenda
Dey, A.; Lipkind, G.M.; Rouille, Y.; Norrbom, C.; Stein, J.; Zhang, C.; Carroll, R.; Steiner, D.F.
Significance of prohormone convertase 2, PC2, mediated initial cleavage at the proglucagon interdomain site, Lys70-Arg71, to generate glucagon
Endocrinology
146
713-727
2005
Mus musculus
brenda
Salvas, A.; Benjannet, S.; Reudelhuber, T.L.; Chretien, M.; Seidah, N.G.
Evidence for proprotein convertase activity in the endoplasmic reticulum/early Golgi
FEBS Lett.
579
5621-5625
2005
Mus musculus
brenda
Mulcahy, L.R.; Vaslet, C.A.; Nillni, E.A.
Prohormone-convertase 1 processing enhances post-Golgi sorting of prothyrotropin-releasing hormone-derived peptides
J. Biol. Chem.
280
39818-39826
2005
Rattus norvegicus
brenda
Ugleholdt, R.; Poulsen, M.L.; Holst, P.J.; Irminger, J.C.; Orskov, C.; Pedersen, J.; Rosenkilde, M.M.; Zhu, X.; Steiner, D.F.; Holst, J.J.
Prohormone convertase 1/3 is essential for processing of the glucose-dependent insulinotropic polypeptide precursor
J. Biol. Chem.
281
11050-11057
2006
Mus musculus
brenda
Rabah, N.; Gauthier, D.; Wilkes, B.C.; Gauthier, D.J.; Lazure, C.
Single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme
J. Biol. Chem.
281
7556-7567
2006
Mus musculus (P63239)
brenda
Sanchez, V.C.; Goldstein, J.; Stuart, R.C.; Hovanesian, V.; Huo, L.; Munzberg, H.; Friedman, T.C.; Bjorbaek, C.; Nillni, E.A.
Regulation of hypothalamic prohormone convertases 1 and 2 and effects on processing of prothyrotropin-releasing hormone
J. Clin. Invest.
114
357-369
2004
Rattus norvegicus
brenda
Lee, S.N.; Prodhomme, E.; Lindberg, I.
Prohormone convertase 1 (PC1) processing and sorting: effect of PC1 propeptide and proSAAS
J. Endocrinol.
182
353-364
2004
Mus musculus
brenda
Henrich, S.; Lindberg, I.; Bode, W.; Than, M.E.
Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity
J. Mol. Biol.
345
211-227
2004
Homo sapiens
brenda
Shen, X.; Li, Q.L.; Brent, G.A.; Friedman, T.C.
Thyroid hormone regulation of prohormone convertase 1 (PC1): regional expression in rat brain and in vitro characterization of negative thyroid hormone response elements
J. Mol. Endocrinol.
33
21-33
2004
Rattus norvegicus
brenda
Tagen, M.B.; Beinfeld, M.C.
Recombinant prohormone convertase 1 and 2 cleave purified pro cholecystokinin (CCK) and a synthetic peptide containing CCK 8 Gly Arg Arg and the carboxyl-terminal flanking peptide
Peptides
26
2530-2535
2005
Mus musculus
brenda
Rabah, N.; Gauthier, D.J.; Gauthier, D.; Lazure, C.
Improved PC1/3 production through recombinant expression in insect cells and larvae
Protein Expr. Purif.
37
377-384
2004
Mus musculus
brenda
Rabah, N.; Gauthier, D.; Dikeakos, J.D.; Reudelhuber, T.L.; Lazure, C.
The C-terminal region of the proprotein convertase 1/3 (PC1/3) exerts a bimodal regulation of the enzyme activity in vitro
FEBS J.
274
3482-3491
2007
Mus musculus
brenda
Billova, S.; Galanopoulou, A.S.; Seidah, N.G.; Qiu, X.; Kumar, U.
Immunohistochemical expression and colocalization of somatostatin, carboxypeptidase-E and prohormone convertases 1 and 2 in rat brain
Neuroscience
147
403-418
2007
Rattus norvegicus
brenda
Espinosa, V.P.; Ferrini, M.; Shen, X.; Lutfy, K.; Nillni, E.A.; Friedman, T.C.
Cellular colocalization and coregulation between hypothalamic pro-TRH and prohormone convertases in hypothyroidism
Am. J. Physiol. Endocrinol. Metab.
292
E175-E186
2007
Rattus norvegicus
brenda
Wideman, R.D.; Covey, S.D.; Webb, G.C.; Drucker, D.J.; Kieffer, T.J.
A switch from prohormone convertase (PC)-2 to PC1/3 expression in transplanted alpha-cells is accompanied by differential processing of proglucagon and improved glucose homeostasis in mice
Diabetes
56
2744-2752
2007
Mus musculus
brenda
Lloyd, D.J.; Bohan, S.; Gekakis, N.
Obesity, hyperphagia and increased metabolic efficiency in Pc1 mutant mice
Hum. Mol. Genet.
15
1884-1893
2006
Homo sapiens, Mus musculus, Mus musculus C57BL/6
brenda
Farooqi, I.S.; Volders, K.; Stanhope, R.; Heuschkel, R.; White, A.; Lank, E.; Keogh, J.; ORahilly, S.; Creemers, J.W.
Hyperphagia and early-onset obesity due to a novel homozygous missense mutation in prohormone convertase 1/3
J. Clin. Endocrinol. Metab.
92
3369-3373
2007
Homo sapiens
brenda
Lou, H.; Smith, A.M.; Coates, L.C.; Cawley, N.X.; Loh, Y.P.; Birch, N.P.
The transmembrane domain of the prohormone convertase PC3: a key motif for targeting to the regulated secretory pathway
Mol. Cell. Endocrinol.
267
17-25
2007
Rattus norvegicus, Mus musculus
brenda
Marandi, M.; Mowla, S.J.; Tavallaei, M.; Yaghoobi, M.M.; Jafarnejad, S.M.
Proprotein convertases 1 and 2 (PC1 and PC2) are expressed in neurally differentiated rat bone marrow stromal stem cells (BMSCs)
Neurosci. Lett.
420
198-203
2007
Rattus norvegicus
brenda
Rehfeld, J.F.; Zhu, X.; Norrbom, C.; Bundgaard, J.R.; Johnsen, A.H.; Nielsen, J.E.; Vikesaa, J.; Stein, J.; Dey, A.; Steiner, D.F.; Friis-Hansen, L.
Prohormone convertases 1/3 and 2 together orchestrate the site-specific cleavages of progastrin to release gastrin-34 and gastrin-17
Biochem. J.
415
35-43
2008
Mus musculus
brenda
Lankat-Buttgereit, B.; Mueller, S.; Schmidt, H.; Parhofer, K.G.; Gress, T.M.; Goeke, R.
Knockdown of Pdcd4 results in induction of proprotein convertase 1/3 and potent secretion of chromogranin A and secretogranin II in a neuroendocrine cell line
Biol. Cell
100
703-715
2008
Homo sapiens
brenda
Garruti, G.; Cotecchia, S.; Giampetruzzi, F.; Giorgino, F.; Giorgino, R.
Neuroendocrine deregulation of food intake, adipose tissue and the gastrointestinal system in obesity and metabolic syndrome
J. Gastrointestin. Liver Dis.
17
193-198
2008
Homo sapiens
brenda
Fox, D.L.; Good, D.J.
Nescient helix-loop-helix 2 interacts with signal transducer and activator of transcription 3 to regulate transcription of prohormone convertase 1/3
Mol. Endocrinol.
22
1438-1448
2008
Mus musculus
brenda
Espinosa, V.P.; Liu, Y.; Ferrini, M.; Anghel, A.; Nie, Y.; Tripathi, P.V.; Porche, R.; Jansen, E.; Stuart, R.C.; Nillni, E.A.; Lutfy, K.; Friedman, T.C.
Differential regulation of prohormone convertase 1/3, prohormone convertase 2 and phosphorylated cyclic-AMP-response element binding protein by short-term and long-term morphine treatment: implications for understanding the "switch" to opiate addiction
Neuroscience
156
788-799
2008
Rattus norvegicus, Homo sapiens
brenda
Zhou, J.; Cai, Z.H.
Molecular cloning and characterization of prohormone convertase 1 gene in abalone (Haliotis diversicolor supertexta)
Comp. Biochem. Physiol. B
155
331-339
2010
Haliotis diversicolor supertexta
brenda
Sun, J.; Zhang, C.; Fang, X.; Lei, C.; Lan, X.; Chen, H.
Novel single nucleotide polymorphisms of the caprine PC1 gene and association with growth traits
Biochem. Genet.
48
779-788
2010
Capra hircus (D8V3M2)
brenda
Ozawa, A.; Peinado, J.R.; Lindberg, I.
Modulation of prohormone convertase 1/3 properties using site-directed mutagenesis
Endocrinology
151
4437-4445
2010
Mus musculus
brenda
Kilimnik, G.; Kim, A.; Steiner, D.; Friedman, T.; Hara, M.
Intraislet production of GLP-1 by activation of prohormone convertase 1/3 in pancreatic alpha-cells in mouse models of beta-cell regeneration
Islets
2
149-155
2010
Mus musculus
brenda
Zhan, S.; Zhou, A.; Lan, J.; Yang, T.
Proprotein convertase 1 mRNA and protein expression in ischemic rat cortex after reperfusion
Neural Regen. Res.
6
295-299
2011
Rattus norvegicus
-
brenda
Hiramoto, K.; Yamate, Y.; Kobayashi, H.; Ishii, M.; Sato, E.F.; Inoue, M.
Ultraviolet B irradiation of the mouse eye induces pigmentation of the skin more strongly than does stress loading, by increasing the levels of prohormone convertase 2 and alpha-melanocyte-stimulating hormone
Clin. Exp. Dermatol.
38
71-76
2013
Mus musculus (P63239)
brenda
Ozawa, S.; Katsuta, H.; Suzuki, K.; Takahashi, K.; Tanaka, T.; Sumitani, Y.; Nishida, S.; Yoshimoto, K.; Ishida, H.
Estimated proinsulin processing activity of prohormone convertase (PC) 1/3 rather than PC2 is decreased in pancreatic beta-cells of type 2 diabetic patients
Endocr. J.
61
607-614
2014
Homo sapiens (P29120)
brenda
Blanco, E.H.; Peinado, J.R.; Martin, M.G.; Lindberg, I.
Biochemical and cell biological properties of the human prohormone convertase 1/3 Ser357Gly mutation: a PC1/3 hypermorph
Endocrinology
155
3434-3447
2014
Homo sapiens (P29120)
brenda
Gagnon, H.; Refaie, S.; Gagnon, S.; Desjardins, R.; Salzet, M.; Day, R.
Proprotein convertase 1/3 (PC1/3) in the rat alveolar macrophage cell line NR8383: localization, trafficking and effects on cytokine secretion
PLoS ONE
8
e61557
2013
Rattus norvegicus
brenda
Wilschanski, M.; Abbasi, M.; Blanco, E.; Lindberg, I.; Yourshaw, M.; Zangen, D.; Berger, I.; Shteyer, E.; Pappo, O.; Bar-Oz, B.; Martin, M.G.; Elpeleg, O.
A novel familial mutation in the PCSK1 gene that alters the oxyanion hole residue of proprotein convertase 1/3 and impairs its enzymatic activity
PLoS ONE
9
e108878
2014
Homo sapiens (P29120)
brenda
Elferich, J.; Williamson, D.M.; David, L.L.; Shinde, U.
Determination of histidine pKa values in the propeptides of furin and proprotein convertase 1/3 using histidine hydrogen-deuterium exchange mass spectrometry
Anal. Chem.
87
7909-7917
2015
Homo sapiens (P29120)
brenda
Righi, A.; Faustini-Fustini, M.; Morandi, L.; Monti, V.; Asioli, S.; Mazzatenta, D.; Bacci, A.; Foschini, M.P.
The changing faces of corticotroph cell adenomas the role of prohormone convertase 1/3
Endocrine
56
286-297
2017
Homo sapiens (P29120)
brenda
Li, J.; Mao, Z.; Huang, J.; Xia, J.
PICK1 is essential for insulin production and the maintenance of glucose homeostasis
Mol. Biol. Cell
29
587-596
2018
Mus musculus
brenda
Duhamel, M.; Rodet, F.; Murgoci, A.N.; Desjardins, R.; Gagnon, H.; Wisztorski, M.; Fournier, I.; Day, R.; Salzet, M.
The proprotein convertase PC1/3 regulates TLR9 trafficking and the associated signaling pathways
Sci. Rep.
6
19360
2016
Mus musculus
brenda
Ramzy, A.; Asadi, A.; Kieffer, T.J.
Revisiting proinsulin processing evidence that human beta-cells process proinsulin with prohormone convertase (PC) 1/3 but not PC2
Diabetes
69
1451-1462
2020
Homo sapiens
brenda
Ni, Y.; Chen, X.; Sun, Y.; Pan, J.; Tang, C.; Yuan, T.
Modulation of PC1/3 activity by a rare double-site homozygous mutation
Front. Pediatr.
10
1026707
2022
Homo sapiens
brenda
Zhang, X.Y.; Liu, F.; Chen, Y.; Guo, W.C.; Zhang, Z.H.
Proprotein convertase 1/3-mediated down-regulation of brain-derived neurotrophic factor in cortical neurons induced by oxygen-glucose deprivation
Neural Regen. Res.
15
1066-1070
2020
Rattus norvegicus
brenda
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