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Information on EC 3.4.21.120 - oviductin
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3.4.21.120 oviductinSpecify your search results
Word Map
- 3.4.21.120
- fetal
- cirrhosis
- pregnancy
-
resect
- chorionic
- albumin
- women
- hepatocytes
- gonadotropin
-
ultrasound
- amniotic
-
carcinoembryonic
-
tomography
-
prenatal
-
postoperative
- metastases
- abdominal
-
preoperative
- yolk
-
portal
-
trimester
-
ultrasonography
- testicular
-
curative
- teratoma
-
amniocentesis
-
hepatectomy
-
child-pugh
-
cytokeratins
-
intrahepatic
- endoderm
-
chemoembolization
- estriol
- hepatoblastomas
-
unconjugated
- prothrombin
-
unresectable
-
milan
- trisomy
-
transarterial
-
hbsag
-
transcatheter
- seminoma
-
orchiectomy
-
spina
- culinaris
-
barcelona
-
radiofrequency
- papp-a
-
nuchal
The enzyme appears in viruses and cellular organisms
Reaction Schemes
preferential cleavage at Gly-Ser-Arg373-/- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
Synonyms
alpha-fetoprotein, oviductin, ovochymase, oviductin-1, oviductin-i, oviductal protease, ovochymase 2, gp43 processing protease, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-fetoprotein
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
hAFP
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
hOV-1
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
oviductal protease
oviductin
oviductin-I
ovochymase 2
oviductin-I
-
human oviductin (hOV-I) and human alpha-fetoprotein (hAFP) are chemically similar and immunologically identical molecules
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage at Gly-Ser-Arg373-/- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
-
-
-
-
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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
55 kDa glycoprotein + H2O
?
-
the oviductal protease selectively hydrolyzes in vitro the 84 kDa and the 55 kDa glycoproteins of the coelomic envelope
-
-
?
84 kDa glycoprotein + H2O
?
-
the oviductal protease selectively hydrolyzes in vitro the 84 kDa and the 55 kDa glycoproteins of the coelomic envelope
-
-
?
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
14% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
-
12% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin + H2O
Nalpha-tert-butoxycarbonylphenylalanylserylarginine + 7-amino-4-methylcoumarin
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin-7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Pyr-Gly-Arg-4-methylcoumarin-7-amide + H2O
Pyr-Gly-Arg + 7-amino-4-methylcoumarin
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
additional information
?
-
-
it is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
-
-
?
gp43 + H2O
gp41 + ?
oviductin alone is the oviductal factor responsible for converting the egg envelope to a sperm-penetrable form, via an increase in sperm binding. gp43 processing is the only requirement for envelope conversion
-
-
?
gp43 + H2O
gp41 + ?
-
preferential cleavage at Gly-Ser-Arg373-/-glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41. Processing of gp43 causes physical changes in the egg envelope which occurs during egg transit through the oxiduct
-
-
?
gp43 + H2O
gp41 + ?
-
preferential cleavage at Gly-Ser-Arg373-/-glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
-
-
?
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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
additional information
?
-
-
it is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
-
-
?
gp43 + H2O
gp41 + ?
oviductin alone is the oviductal factor responsible for converting the egg envelope to a sperm-penetrable form, via an increase in sperm binding. gp43 processing is the only requirement for envelope conversion
-
-
?
gp43 + H2O
gp41 + ?
-
preferential cleavage at Gly-Ser-Arg373-/-glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41. Processing of gp43 causes physical changes in the egg envelope which occurs during egg transit through the oxiduct
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
LiCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaF
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaNO3
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by iodoacetamide, E-64, pepstatin or 1,10-phenanthroline
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.058
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin
-
-
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin
-
-
-
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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
8
-
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-4-methylcoumarin-7-amide
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8.5
-
more than 90% of maximal activity at pH 7.5 and at pH 8.5, less than 30% of maximal activity below pH 6.5
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Rhinella arenarum, collected in Tucumán, Argentina, between May and October and housed at 25°C until used, gene OVCH2
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
endocytic compartments in the blastomeres of developing embryos
brenda
-
expressed in the chicken egg citelline membrane: using high-throughput, high-end LC-mass spectroscopy 137 proteins are identified. Specific components of the vitelline membrane not identified previously in other egg compartments include eight zona pellucida proteins, oviductin protease, and two ATPases
brenda
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endocytic compartments in the blastomeres of developing embryos
brenda
-
negligible expression during the first three months of postnatal cervical differentiation. Transcripts are minimally detectable in the cervives of 4-month-old juveniles. Strong expression in the endocervices of adults is eliminated by ovariectomy and restored by estrogen treatment
brenda
-
after its release into the lumen of the oviduct, oviductin becomes associated with the zona pellucida of post-ovulatory oocytes. In unfertilized oocytes, oviductin is also detected in membrane invaginations along the oolemma and in some vesicles within multivesicular bodies
brenda
-
it is speculated that receptors for hamster oviductin-1 are present at the apical cell surface of endometrial cells and that implantation of the developing blastocyst into the uterine wall is possible only following downregulation of these receptors
brenda
-
oviductin is detected over the microvilli and within multivesicular bodies
brenda
additional information
-
expression of the oviductin gene is confined strictly to nonciliated secretory cells
brenda
-
hamster oviduction is inhibitory to in vitro fertilization, but oocytes with cumulus intact maintain their fertilizing capacity in the presence of oviductin
brenda
-
in Golgi saccules and secretory granules of the non-ciliated oviduct cells. After its release into the lumen, oviductin becomes associated with the zona pellucida of post-ovulatory oocytes
brenda
-
oviductin mRNA expression remains constant throughout the estrous cycle. Production of oviductin is not regulated differentially during the estrous cycle. The oviduct contains several forms of oviductin at each stage of the estrous cycle, the native glycosylated form(s) of 160350 kDa, and several precursor forms of 70100 kDa
brenda
-
oviductins are targeted to the oocyte via the interaction of their chitinase-like domains with specific oligosaccharide moieties of the zona pellucida. Once localized to this structure, oviductin molecules would act as a protective shield around the oocyte and early embryo by virtue of their densely glycosylated mucin-type domains
brenda
-
oviductins are targeted to the oocyte via the interaction of their chitinase-like domains with specific oligosaccharide moieties of the zona pellucida. Once localized to this structure, oviductin molecules would act as a protective shield around the oocyte and early embryo by virtue of their densely glycosylated mucin-type domains
brenda
-
some of the oviductin associated with the zona pellucida appears to be internalized by blastomeres of the embryo and further processed through the endosomal/lysosomal pathway
brenda
additional information
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
brenda
additional information
-
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
brenda
additional information
-
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
-
brenda
additional information
tissue expression analysis of oviductin
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
translational products stored in the pars recta granules need to be processed to become a proteolytically active 66000 Da form
brenda
-
in unfertilized oocytes, oviductin is detected in membrane invaginations along the oolemma and in some vesicles within multivesicular bodies
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
evolution
phylogenetic relationship between Bufo arenarum oviductin and Mus musculus ovochymase 2, overview
evolution
phylogenetic relationship between Bufo arenarum oviductin and Mus musculus ovochymase 2, overview. Protease gene families involved in reproduction and host defense played a role during the evolution of some mammalian species. Thus, the absence of ovochymase 2 RNA transcripts in oviduct might be one of the signs of the transition from a primitive fertilization mode (external fertilization) to a more complex form (internal fertilization)
evolution
-
phylogenetic relationship between Bufo arenarum oviductin and Mus musculus ovochymase 2, overview. Protease gene families involved in reproduction and host defense played a role during the evolution of some mammalian species. Thus, the absence of ovochymase 2 RNA transcripts in oviduct might be one of the signs of the transition from a primitive fertilization mode (external fertilization) to a more complex form (internal fertilization)
-
physiological function
oviductin, a serine protease with trypsin-like substrate specificity, hydrolyzes two kinds of egg envelope glycoproteins, gp84 and gp55, in the pars recta portion of the oviduct, thereby converting the egg to a penetrable state
physiological function
ovochymase 2 might produce proteolytic changes in the zona pellucida similar to the action of amphibian oviductin, which can play a role in embryo attachment to the uterine wall during implantation
physiological function
-
an anti-ovochymase antibody inhibits elevation of the vitelline coat at a late stage of oogenesis, during the period when selfsterility is acquired
physiological function
-
ovochymase 2 might produce proteolytic changes in the zona pellucida similar to the action of amphibian oviductin, which can play a role in embryo attachment to the uterine wall during implantation
-
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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). OVCH2_BUFJA
974
0
107648
Swiss-Prot
Secretory Pathway (Reliability: 2)
OVCH2_RHIAE
980
0
108566
Swiss-Prot
Secretory Pathway (Reliability: 2)
OVCH2_XENLA
1004
0
110612
Swiss-Prot
Secretory Pathway (Reliability: 2)
E1AW56_MOUSE
152
0
16503
TrEMBL
other Location (Reliability: 3)
A0A6J8DP85_MYTCO
1007
0
111988
TrEMBL
Secretory Pathway (Reliability: 4)
A0A7R8CLG5_LEPSM
406
0
46273
TrEMBL
other Location (Reliability: 3)
A0A7R8CMJ3_LEPSM
212
0
23275
TrEMBL
Secretory Pathway (Reliability: 4)
A0A7R8CRD6_LEPSM
409
0
46609
TrEMBL
other Location (Reliability: 3)
A0A8B6D533_MYTGA
2222
0
249017
TrEMBL
other Location (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
oviductin is a multi-domain protein with a protease domain at the N-terminal region followed by two CUB domains and toward the C-terminal region another protease domain, which lacks an active histidine site, and one CUB domain
additional information
-
oviductin is a multi-domain protein with a protease domain at the N-terminal region followed by two CUB domains and toward the C-terminal region another protease domain, which lacks an active histidine site, and one CUB domain
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
contains terminal alpha-D-GalNAc and either terminal alpha-D-NeuAc or non-terminal beta-D-(GlcNAc)2 residues. Both the alpha- and beta-forms are sulphated on O-linked oligosaccharide side chains but are not phosphorylated. The hamster oviductin polymorphism is a consequence of different glycosylation patterns and not the polypeptide chain itself. Hamster oviductin is mostly O-glycosylated and contains a few N-linked oligosaccharide side chains (approx. 10 kDa). It is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
glycoprotein
-
glycosylation of hamster oviductin appears to be differentially regulated during the estrous cycle
glycoprotein
-
polymorphism in the heavily O-glycosylated region of hamster oviductin
glycoprotein
-
the mature MOGP contained three potential N-linked glycosylation sites and 24 possible O-linked glycosylation sites
glycoprotein
-
the mature MOGP contained three potential N-linked glycosylation sites and 24 possible O-linked glycosylation sites
-
proteolytic modification
translational products stored in the pars recta granules need to be processed to become a proteolytically active 66000 Da form. Extensive posttranslational processing for activation of proteolytic activity. Oviductin translated as 107.6-kDa precursors are processed both N- and C-terminally to give rise to a 66-kDa active form comprising a serine protease and two CUB domains
proteolytic modification
protease is translated as the N terminus of an unusual mosaic protein. It is proposed that during post-translational proteolytic processing of the mosaic oviductin glycoprotein, the processed N-terminal protease domain is released coupled to two C-terminal CUB domains and constitutes the enzymatically active protease molecule
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively stable to rapid freezing in the presence of 20% glycerol. 90% of the activity remains after each freeze-thaw cycle
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene OVCH2, DNA and amino acid sequence determination and analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Malette, B.; Bleau, G.
Biochemical characterization of hamster oviductin as a sulphated zona pellucida-binding glycoprotein
Biochem. J.
295
437-445
1993
Mesocricetus auratu