3.4.21.120: oviductin
This is an abbreviated version!
For detailed information about oviductin, go to the full flat file.
Word Map on EC 3.4.21.120
-
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
- 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
Reaction
preferential cleavage at Gly-Ser-Arg373-/- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41 =
Synonyms
alpha-fetoprotein, Gp43 processing protease, hAFP, Harore.CG.MTP2014.S89.g15383, hOV-1, oviductal protease, oviductin, oviductin-1, oviductin-I, ovochymase, ovochymase 2
ECTree
3.4.21.120 oviductinAdvanced search results
results (
results (Source Tissue
Source Tissue on EC 3.4.21.120 - oviductin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
-
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
-
endocytic compartments in the blastomeres of developing embryos
-
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
-
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
-
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
-
oviductin is detected over the microvilli and within multivesicular bodies
additional information
-
expression of the oviductin gene is confined strictly to nonciliated secretory cells
-
hamster oviduction is inhibitory to in vitro fertilization, but oocytes with cumulus intact maintain their fertilizing capacity in the presence of oviductin
-
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
-
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
-
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
-
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
-
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
additional information
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
additional information
-
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
additional information
-
analysis of ovochymase 2 expression in the mouse reproductive tract, no expression in the oviduct
-
