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Information on EC 3.4.23.41 - yapsin 1
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3.4.23.41 yapsin 1Specify your search results
Word Map
- 3.4.23.41
-
prohormone
- granules
-
monobasic
- propeptide
-
aspartyl
-
pituitary
- cholecystokinin
-
non-anchored
-
tetrabasic
- parathyroid
- pepstatin
-
endoglycosidase
- acth
- zymogen
- pheromone
-
dibasic
- pro-opiomelanocortin
- proproteins
-
residue-specific
-
prohormone-processing
- synthesis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
Synonyms
yapsin 1, yeast aspartic protease 3, yeast aspartic protease, yap3 gene product, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aspartic protease yapsin I
-
-
-
-
aspartic proteinase 3
Kex2
Yap3 gene product
-
-
-
-
yeast aspartic protease
-
-
-
-
yeast aspartic protease 3
-
-
-
-
YPS1
YPS7
additional information
-
formerly termed yapsin 3, yeast aspartyl protease 3, or Yap3p, the enzyme belongs to the A1 peptidase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
cleavage is enhanced in substrates having additional basic residues flanking the P1 site
-
hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
cleaves at mono-, di-, and multi-basic cleavage sites
-
hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
205132-58-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
aminobenzoyl-Arg-Val-Lys-Arg-Gly-Leu-Ala-Tyr(NO2)-Asp-OH + H2O
?
-
-
?
anglerfish pro-somatostatin I
(Lys-) anglerfish somatostatin 14
-
-
-
?
anglerfish pro-somatostatin II
anglerfish somatostatin 28
-
-
-
?
human adrenocorticotropic hormone 1-39
human adrenocorticotropic hormone 1-15 + corticotropin-like intermediate lobe peptide 16-39
pre-elafin + H2O
elafin + ?
-
cleavage occurs C-terminal to a subset of single Lys residues
-
?
pro-alpha-mating factor + H2O
alpha-mating factor + pro-sequence of alpha-mating factor
-
processing
-
-
?
pro-somatostatin II + H2O
somatostatin-28 + pro-sequence of somatostatin-28
-
processing, cleavage after a single Arg residue
-
-
?
proopiomelanocortin
adrenocorticotropic hormone 1-39 + adrenocorticotropic hormone 1-14
-
-
-
?
human adrenocorticotropic hormone 1-39
human adrenocorticotropic hormone 1-15 + corticotropin-like intermediate lobe peptide 16-39
-
-
-
?
human adrenocorticotropic hormone 1-39
human adrenocorticotropic hormone 1-15 + corticotropin-like intermediate lobe peptide 16-39
-
-
-
?
human parathyroid hormone + H2O
?
-
proteolysis generates three fragments, one cleavage occurs at dibasic site R25/K26
-
?
human parathyroid hormone + H2O
?
-
proteolysis generates two fragments, cleavage occurs at dibasic site R25/K26
-
?
protein Scw4 + H2O
?
-
the enzyme cleaves behind the sequence Lys27-Asp28-Lys29-Arg30 of protein Scw4
-
-
?
protein Scw4 + H2O
?
-
the enzyme cleaves behind the sequence Lys27-Asp28-Lys29-Arg30 of protein Scw4
-
-
?
synthetic proalbumin
RGVFRR + DEAKSEVAW
-
substrate is representing the propeptide cleavage site RGVFRRDAHKSEVAW
-
?
additional information
?
-
-
the enzyme is involved in proteolysis of the secretory pathway, regulatory parameters, overview
-
-
?
additional information
?
-
-
the enzyme is required for cell wall integrity protecting the cells from lysis during environmental stress and morphogenesis, overview
-
-
?
additional information
?
-
-
the enzyme shows a preference for substrates with basic residues downstream as well as upstream of the scissile bond
-
-
?
additional information
?
-
-
the enzyme splits peptide bonds specifically after two basic amino acids, often preceded by two charged amino acids
-
-
?
additional information
?
-
-
the enzyme splits peptide bonds specifically after two basic amino acids, often preceded by two charged amino acids
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pre-elafin + H2O
elafin + ?
-
cleavage occurs C-terminal to a subset of single Lys residues
-
?
pro-alpha-mating factor + H2O
alpha-mating factor + pro-sequence of alpha-mating factor
-
processing
-
-
?
additional information
?
-
-
the enzyme is involved in proteolysis of the secretory pathway, regulatory parameters, overview
-
-
?
additional information
?
-
-
the enzyme is required for cell wall integrity protecting the cells from lysis during environmental stress and morphogenesis, overview
-
-
?
additional information
?
-
-
the enzyme splits peptide bonds specifically after two basic amino acids, often preceded by two charged amino acids
-
-
?
additional information
?
-
-
the enzyme splits peptide bonds specifically after two basic amino acids, often preceded by two charged amino acids
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Y1, a potent, competitive inhibitor that should serve as a powerful chemical tool for the study of the increasing number of yapsin-like enzymes
-
additional information
-
Y1, a potent, competitive inhibitor that should serve as a powerful chemical tool for the study of the increasing number of yapsin-like enzymes
-
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
localizes on the cell wall via glycosylphosphatidylinositol anchor
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
an enzyme-deficient mutant displays deregulated pH homeostasis
metabolism
physiological function
metabolism
replacement of the N-entrance loop of yapsin Yps1 generates a single chain endopeptidase that undergoes at pH 6.0 partial or at pH 3.0 complete pro-peptide removal. At both pH, the shedding activity of the chimeric endopeptidase, where the N-entrance loop is replaced by the pentapeptide GSVMD found in Yps3, toward Gas1 and itself is strongly and drastically increased, respectively. A direct correlation between endoproteolytic cleavage of this loop in native Yps1 and its shedding is observed. The Yps1-dependent shedding of model glycosylphosphatidylinositol proteins Gas1 and Yps1 is also stimulated by the absence of the O-mannosyltransferases, Pmt4 and Pmt2 respectively. Under these conditions, some Yps1-independent shedding is also observed
metabolism
-
replacement of the N-entrance loop of yapsin Yps1 generates a single chain endopeptidase that undergoes at pH 6.0 partial or at pH 3.0 complete pro-peptide removal. At both pH, the shedding activity of the chimeric endopeptidase, where the N-entrance loop is replaced by the pentapeptide GSVMD found in Yps3, toward Gas1 and itself is strongly and drastically increased, respectively. A direct correlation between endoproteolytic cleavage of this loop in native Yps1 and its shedding is observed. The Yps1-dependent shedding of model glycosylphosphatidylinositol proteins Gas1 and Yps1 is also stimulated by the absence of the O-mannosyltransferases, Pmt4 and Pmt2 respectively. Under these conditions, some Yps1-independent shedding is also observed
-
physiological function
complementation analysis of opsA and opsB in kexB mutants: overexpression of opsA or ops B (aspartyl proteases homologous to yeast yapsins YPS1/2) do not suppress the kexB mutation in Aspergillus oryzae or Aspergillus nidulans, although yapsins are multicopy suppressors for the yeast kex2 mutation
physiological function
deletion of the YPS genes generates only minor influence on the sensitivity to cell wall stress
physiological function
deletion of the YPS genes generates only minor influence on the sensitivity to cell wall stress. The sole disruption of YPS1 is sufficient in eliminating the aberrant proteolytic cleavage of recombinant proteins secreted by Hansenula polymorpha
physiological function
-
Yps1 is required for cell growth at elevated temperatures
physiological function
-
a Candida glabrata mutant lacking all 11 yapsins, possesses an enlarged vacuole and displays phenotypes similar to deficiency in vacuolar membrane ATPase with elevated metal ion susceptibility in an alkaline pH medium and diminished in vacuolar membrane ATPase activity. the mutant shows elevated polyphosphate levels and diminished cellular carboxypeptidase Y activity. A gross perturbation of cellular homoeostasis in the mutant lacking all yapsins, even in the absence of external stressors, is characterized by reduced levels of ATP and stress metabolites, elevated reactive oxygen species levels, cell surface abnormalities, and a constitutively activated protein kinase C signalling pathway. Isoform Yps1 is involved in the maintenance of ion homoeostasis under normal and calcineurin-inhibited conditions
physiological function
-
disruption of yapsin YPS7 gene confers the mutant cell increased resistance to cell wall perturbing reagents congo red, calcofluor white and sodium dodecyl sulfate. Mutant shows lower content of chitin and increased amounts of beta-1,3-glucan. Disruption of YPS7 gene causes a reduction of the chitin content in lateral cell wall. The inner layer of mutant cell wall, mainly composed of chitin and beta-1, 3-glucan, is much thicker than that in parental strain GS115. The mutant also exhibits increased osmotic resistance compared with the parental strain
physiological function
the enzyme is a potential virulence factor and involved in maturation of proteins and cell wall function
physiological function
-
the enzyme is required for cell wall maintenance, remodeling and cell-cell interactions. The enzyme is essential for survival in an acidic environment
physiological function
-
disruption of yapsin YPS7 gene confers the mutant cell increased resistance to cell wall perturbing reagents congo red, calcofluor white and sodium dodecyl sulfate. Mutant shows lower content of chitin and increased amounts of beta-1,3-glucan. Disruption of YPS7 gene causes a reduction of the chitin content in lateral cell wall. The inner layer of mutant cell wall, mainly composed of chitin and beta-1, 3-glucan, is much thicker than that in parental strain GS115. The mutant also exhibits increased osmotic resistance compared with the parental strain
-
physiological function
-
the enzyme is a potential virulence factor and involved in maturation of proteins and cell wall function
-
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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). YPS1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
569
0
60010
Swiss-Prot
Secretory Pathway (Reliability: 5)
MKC7_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
596
0
64269
Swiss-Prot
Secretory Pathway (Reliability: 1)
K0KF23_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
594
0
62472
TrEMBL
Secretory Pathway (Reliability: 2)
K0KD48_WICCF
Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL Y-1031 F-60-10)
576
0
61981
TrEMBL
Secretory Pathway (Reliability: 2)
W1QAF4_OGAPD
Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1)
576
1
60945
TrEMBL
Secretory Pathway (Reliability: 3)
A0A8J5BAX0_9ASCO
408
0
44290
TrEMBL
Secretory Pathway (Reliability: 1)
Q5J879_PICPA
599
0
62984
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25000
1 * 65000-850000, beta-subunit, + 1 * 25000, alpha-subunit. SDS-PAGE, highly glycosylated protein. x * 55000, calculated for mature protein
55000
1 * 65000-850000, beta-subunit, + 1 * 25000, alpha-subunit. SDS-PAGE, highly glycosylated protein. x * 55000, calculated for mature protein
57000
1 * 150000-200000, SDS-PAGE, highly glycosylated protein. 1 * 57000, calculated for mature protein
60000
-
x * 60000, non-glycosylated enzyme, 70000-150000, glycosylated enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
1 * 65000-850000, beta-subunit, + 1 * 25000, alpha-subunit. SDS-PAGE, highly glycosylated protein. x * 55000, calculated for mature protein
monomer
1 * 150000-200000, SDS-PAGE, highly glycosylated protein. 1 * 57000, calculated for mature protein
additional information
?
-
x * 60000, non-glycosylated enzyme, 70000-150000, glycosylated enzyme
additional information
-
alpha,beta, 1 * 66000-97000 + 1 * 31000, SDS-PAGE
additional information
-
three-dimensional structure determination and analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
proteolytic modification
sequence contains a N-terminal signal peptide
proteolytic modification
-
the 87000 Da pro-yapsin 1 is autocatalytically processed into two subunits, alpha, 18000 Da, and beta, 74000 Da, by cleavage at a loop region
proteolytic modification
-
proyapsin 1 processing by autocatalysis, autocatalytic cleavage in a loop structure resulting in two subunits, in vitro activation of the zymogen at pH 4.0
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D101E/DELTA37
-
inactive mutant enzyme, no processing of the 87000 Da Pro-yapsin
additional information
additional information
heterologous expression of YPS1 completely restores all of the growth defects of the Saccharomyces cerevisiae yps1-deletion strains
additional information
heterologous expression of YPS1 completely restores all of the growth defects of the Saccharomyces cerevisiae yps1-deletion strains
additional information
heterologous expression of YPS7 exhibits a limited complementation effect on the Saccharomyces cerevisiae yps7-deletion strain
additional information
heterologous expression of YPS7 exhibits a limited complementation effect on the Saccharomyces cerevisiae yps7-deletion strain
additional information
-
C-terinally truncated, regulation by C-terminus
additional information
-
C-terinally truncated, regulation by C-terminus
additional information
-
construction of yps1 null mutants, cell wall defective phenotype, overexpression results in suppression of caspofungin hypersensitivity, phenotype, detailed overview, complementation by yps1 homologous genes from Candida albicans and Candida glabra
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme lacking the GPI-anchor from yeast, purification using inhibitor RVSMIKNR affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of C-terminally truncated proyapsin I in baculovirus/Sf9 cells
-
gene yps1, DNA and amino acid sequence determination and analysis, expression of recombinant enzyme lacking the GPI-anchor in yeast cells
-
gene YPS1, expression of wild-type and mutant enzymes in yeast strains
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
heat-induced expression of YPS1 is regulated predominantly by the calcineurin-Crz1 pathway and partially by the Slt2 MAPK pathway. Loss of transcriptional induction in a calcineurin mutant is only observed for gene YPS1
-
YPS1 expression is significantly induced only by a subset of stressor agents, such as sodium dodecyl sulfate and tunicamycin
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
yapsin 1 displays specific immunoreactivity in the alpha-cells of human pancreatic islets
synthesis
synthesis
single disruption of either PEP4 gene or yapsin family member YPS1 gene leads to reduced degradation of recombinant human serum albumin and human parathyroid hormone upon expression in Pichia pastoris. In a PEP4YPS1 double disruptant, more than 80% of the human serum albumin and human parathyroid hormone secreted by the remains intact, after 72 h of incubation, in comparison to only 30% with the wild-type strain
synthesis
-
single disruption of either PEP4 gene or yapsin family member YPS1 gene leads to reduced degradation of recombinant human serum albumin and human parathyroid hormone upon expression in Pichia pastoris. In a PEP4YPS1 double disruptant, more than 80% of the human serum albumin and human parathyroid hormone secreted by the remains intact, after 72 h of incubation, in comparison to only 30% with the wild-type strain
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Olsen, V.; Cawley, N.X.; Loh, Y.P.
Yapsin1. Structure, biosynthesis, and specificity
Adv. Exp. Med. Biol.
436
315-319
1998
Saccharomyces cerevisiae
brenda
Kang, H.A.; Kim, S.J.; Choi, E.S.; Rhee, S.K.; Chung, B.H.
Efficient production of intact human parathyroid hormone in a Saccharomyces cerevisiae mutant deficient in yeast aspartic protease 3 (YAP3)
Appl. Microbiol. Biotechnol.
50
187-192
1998
Saccharomyces cerevisiae
brenda
Ledgerwood, E.C.; Brennan, S.O.; Cawley, N.X.; Loh, Y.P.; George, P.M.
Yeast aspartic protease 3 (Yap3) prefers substrates with basic residues in the P2, P1 and P2 positions
FEBS Lett.
383
67-71
1996
Saccharomyces cerevisiae
brenda
Cawley, N.X.; Olsen, V.; Zhang, C.F.; Chen, H.C.; Tan, M.; Loh, Y.P.
Activation and processing of non-anchored yapsin 1 (Yap3p)
J. Biol. Chem.
273
584-591
1998
Saccharomyces cerevisiae
brenda
Cawley, N.X.; Chen, H.C.; Beinfeld, M.C.; Loh, Y.P.
Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3
J. Biol. Chem.
271
4168-4176
1996
Saccharomyces cerevisiae
brenda
Cool, D.R.; Louie, C.Y.; Loh, Y.P.
Yeast aspartic protease 3 is sorted to secretory granules and activated to process proopiomelanocortin in PC12 cells
Endocrinology
137
5441-5446
1996
Saccharomyces cerevisiae
brenda
Cawley, N.X.; Wong, M.; Pu, L.P.; Tam, W.; Loh, Y.P.
Secretion of yeast aspartic protease 3 is regulated by its carboxy-terminal tail: characterization of secreted YAP3p
Biochemistry
34
7430-7437
1995
Saccharomyces cerevisiae
brenda
Cawley, N.X.; Noe, B.D.; Loh, Y.P.
Purified yeast aspartic protease 3 cleaves anglerfish pro-somatostatin I and II at di- and monobasic sites to generate somatostatin-14 and -28
FEBS Lett.
332
273-276
1993
Saccharomyces cerevisiae
brenda
Olsen, V.; Loh, Y.P.
In vivo processing of nonanchored Yapsin 1 (Yap3p)
Arch. Biochem. Biophys.
375
315-321
2000
Saccharomyces cerevisiae
brenda
Cawley, N.X.; Chino, M.; Maldonado, A.; Rodriguez, Y.M.; Loh, Y.P.; Ellman, J.A.
Synthesis and characterization of the first potent inhibitor of yapsin 1. Implications for the study of yapsin-like enzymes
J. Biol. Chem.
278
5523-5530
2003
Saccharomyces cerevisiae (P32329), Saccharomyces cerevisiae
brenda
Bourbonnais, Y.; Larouche, C.; Tremblay, G.M.
Production of full-length human pre-elafin, an elastase specific inhibitor, from yeast requires the absence of a functional yapsin 1 (Yps1p) endoprotease
Protein Expr. Purif.
20
485-491
2000
Saccharomyces cerevisiae
brenda
Krysan, D.J.; Ting, E.L.; Abeijon, C.; Kroos, L.; Fuller, R.S.
Yapsins are a family of aspartyl proteases required for cell wall integrity in Saccharomyces cerevisiae
Eukaryot. Cell
4
1364-1374
2005
Saccharomyces cerevisiae
brenda
Cawley, N.X.; Loh, Y.P.
Yapsin 1
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
128-131
2004
Saccharomyces cerevisiae
-
brenda
Mizutani, O.; Furukawa, K.; Ichiyanagi, S.; Matsuda, Y.; Tokuoka, M.; Fujioka, T.; Yamagata, Y.; Gomi, K.; Abe, K.
Alternative processing of proproteins in Aspergilli kexB gene disruptants under hyperosmotic conditions
Biosci. Biotechnol. Biochem.
73
40-46
2009
Aspergillus oryzae (Q8NKB5)
brenda
Miyazaki, T.; Izumikawa, K.; Yamauchi, S.; Inamine, T.; Nagayoshi, Y.; Saijo, T.; Seki, M.; Kakeya, H.; Yamamoto, Y.; Yanagihara, K.; Miyazaki, Y.; Yasuoka, A.; Kohno, S.
The glycosylphosphatidylinositol-linked aspartyl protease Yps1 is transcriptionally regulated by the calcineurin-Crz1 and Slt2 MAPK pathways in Candida glabrata
FEMS Yeast Res.
11
449-456
2011
[Candida] glabrata
brenda
Cawley, N.X.; Portela-Gomes, G.; Lou, H.; Loh, Y.P.
Yapsin 1 immunoreactivity in {alpha}-cells of human pancreatic islets: implications for the processing of human proglucagon by mammalian aspartic proteases
J. Endocrinol.
210
181-187
2011
Saccharomyces cerevisiae
brenda
Sohn, M.J.; Oh, D.B.; Kim, E.J.; Cheon, S.A.; Kwon, O.; Kim, J.Y.; Lee, S.Y.; Kang, H.A.
HpYPS1 and HpYPS7 encode functional aspartyl proteases localized at the cell surface in the thermotolerant methylotrophic yeast Hansenula polymorpha
Yeast
29
1-16
2012
Ogataea angusta (Q3L7F4), Ogataea angusta (Q5QT58)
brenda
Bairwa, G.; Rasheed, M.; Taigwal, R.; Sahoo, R.; Kaur, R.
GPI (glycosylphosphatidylinositol)-linked aspartyl proteases regulate vacuole homoeostasis in Candida glabrata
Biochem. J.
458
323-334
2014
[Candida] glabrata
brenda
Dube, A.K.; Belanger, M.; Gagnon-Arsenault, I.; Bourbonnais, Y.
N-terminal entrance loop of yeast Yps1 and O-glycosylation of substrates are determinant factors controlling the shedding activity of this GPI-anchored endopeptidase
BMC Microbiol.
15
50
2015
Saccharomyces cerevisiae (P32329), Saccharomyces cerevisiae ATCC 204508 (P32329)
brenda
Guan, B.; Lei, J.; Su, S.; Chen, F.; Duan, Z.; Chen, Y.; Gong, X.; Li, H.; Jin, J.
Absence of Yps7p, a putative glycosylphosphatidylinositol-linked aspartyl protease in Pichia pastoris, results in aberrant cell wall composition and increased osmotic stress resistance
FEMS Yeast Res.
12
969-979
2012
Komagataella pastoris, Komagataella pastoris GS115
brenda
Wu, M.; Shen, Q.; Yang, Y.; Zhang, S.; Qu, W.; Chen, J.; Sun, H.; Chen, S.
Disruption of YPS1 and PEP4 genes reduces proteolytic degradation of secreted HSA/PTH in Pichia pastoris GS115
J. Ind. Microbiol. Biotechnol.
40
589-599
2013
Komagataella pastoris (Q5J879), Komagataella pastoris GS115 (Q5J879)
brenda
Yang, X.; Cong, H.; Song, J.; Zhang, J.
Heterologous expression of an aspartic protease gene from biocontrol fungus Trichoderma asperellum in Pichia pastoris
World J. Microbiol. Biotechnol.
29
2087-2094
2013
Trichoderma asperellum
brenda
Grbavac, A.; Canak, I.; Stuparevic, I.; Teparic, R.; Mrsa, V.
Proteolytic processing of the Saccharomyces cerevisiae cell wall protein Scw4 regulates its activity and influences its covalent binding to glucan
Biochim. Biophys. Acta Mol. Cell Res.
1864
507-515
2017
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Cortes-Acosta, E.; Ibarra, J.; Ramirez-Saad, H.; Vargas-Mendoza, C.; Villa-Tanaca, L.; Hernandez-Rodriguez, C.
Polymorphism in the regulatory regions of genes CgYPS1 and CgYPS7 encoding yapsins in Candida glabrata is associated with changes in expression levels
FEMS Yeast Res.
17
fox077
2017
[Candida] glabrata (A0A1S7BH59), [Candida] glabrata CBS138 (A0A1S7BH59)
brenda
Rapala-Kozik, M.; Bochenska, O.; Zajac, D.; Karkowska-Kuleta, J.; Gogol, M.; Zawrotniak, M.; Kozik, A.
Extracellular proteinases of Candida species pathogenic yeasts
Mol. Oral Microbiol.
33
113-124
2018
[Candida] glabrata
brenda
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Release 2023.1 (January 2023)
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