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Information on EC 3.4.21.107 - peptidase Do and Organism(s) Mus musculus and UniProt Accession Q9R118
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3.4.21.107 peptidase DoSpecify your search results
Word Map
- 3.4.21.107
- degeneration
-
macular
- cerebral
- retinal
- infarct
- neovascularization
- vessel
- parkinsonism
- leukoencephalopathy
-
arteriopathy
-
subcortical
-
carasil
- xiap
-
misfolded
- choroid
- osteoarthritis
- maculopathy
- preeclampsia
-
polypoidal
- pink1
-
acuity
- alopecia
-
drusen
- medicine
-
small-vessel
-
extracytoplasmic
-
amd-associated
-
notch3
- spondylosis
-
transmigration
-
ranibizumab
- biotechnology
- molecular biology
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-/-Val
Synonyms
htra1, htra2, htra3, htra4, serine protease htra1, high-temperature requirement a, htra protease, high temperature requirement a, serine protease htra, degp protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
protease do
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-
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CAS REGISTRY NUMBER
COMMENTARY
161108-11-8
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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
decorin + H2O
decorin peptide fragments
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the small leucine-rich proteoglycan is highly expressed in bone and regulates type I collagen fibril assembly
generation of fragments ranging from 150 to 75 kDa
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?
decorin + H2O
decorin peptide fragments
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a small leucine-rich proteoglycan, human substrate
generation of fragments ranging from 150 to 75 kDa
-
?
fibronectin + H2O
fibronectin peptide fragments
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a major noncollagenous component of mineralized bone matrix
generation of fragments ranging from 200 to 150 kDa
-
?
fibronectin + H2O
fibronectin peptide fragments
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human plasma-derived substrate
generation of fragments ranging from 200 to 150 kDa
-
?
matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
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the protein substrate is present in cartilage, bone, and arteries
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-
?
matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
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cleavage of MGP at the C terminus
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?
additional information
?
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HtrA is specific for mature mucosal mast cells
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-
?
additional information
?
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HtrA1 degrades specific matrix-associated proteins, HtrA1 inhibits mineral deposition by osteoblasts, the protease domain and the PDZ domain are essential for the inhibition of osteoblast mineralization by HtrA1, overview
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?
additional information
?
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HtrA1 is a secreted multidomain protein with serine protease activity
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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
decorin + H2O
decorin peptide fragments
-
the small leucine-rich proteoglycan is highly expressed in bone and regulates type I collagen fibril assembly
generation of fragments ranging from 150 to 75 kDa
-
?
fibronectin + H2O
fibronectin peptide fragments
-
a major noncollagenous component of mineralized bone matrix
generation of fragments ranging from 200 to 150 kDa
-
?
matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
-
the protein substrate is present in cartilage, bone, and arteries
-
-
?
additional information
?
-
-
HtrA is specific for mature mucosal mast cells
-
-
?
additional information
?
-
-
HtrA1 degrades specific matrix-associated proteins, HtrA1 inhibits mineral deposition by osteoblasts, the protease domain and the PDZ domain are essential for the inhibition of osteoblast mineralization by HtrA1, overview
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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
high level of enzyme expression in decidua capsularis specifically at the decidual-trophoblast interface where active involution occurs
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peritoneal, mucosal, and connective tissue-derived mast cells, the enzyme expression is highly up-regulated during mucosal mast cell differentiation, enzyme levels in mucosal mast cells are much higher compared to connective-tissue-type mast cells, expression and enzyme content analysis, overview
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HtrA1 especially expressed in giant cells during the early stages of placental development
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
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HTRA1 knockout mice display reduced blood vessel in retina and upregulation of growth differentiation factor 6
physiological function
-
HTRA1 plays a critical role in the regulation of angiogenesis via transforming growth factor-beta signaling
physiological function
antibody 94,obtained from a human antibody phage display library, forms a distinct macromolecular complex with HtrA1 and inhibits the enzymatic activity of recombinant and native HtrA1 forms. The 246-kDa complex between the HtrA1 catalytic domain trimer and Fab94 has a propeller-like organization with one Fab bound peripherally to each protomer. The antibody binds to the surface-exposed loops B and C of the catalytic domain. The the HtrA1 catalytic domain-IgG94 complex (636 kDa) is a cage-like structure with three centrally located IgG94 molecules coordinating two the HtrA1 catalytic domain trimers and the six active sites pointing into the cavity of the cage. In both complexes, all antigen-recognition regions bind one HtrA1 protomer and all protomers are bound by a antigen-recognition region
physiological function
HtrA1 is an osteoprotegerin-degrading enzyme. Inhibitory activity of osteoprotegerin on receptor activator of NF-kappaB ligand RANKL-induced osteoclastogenesis is suppressed by adding HtrA1 in RAW 264.7 cell cultures
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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downregulation of HtrA1 by siRNA increases osteoblast mineralization, HtrA1 overexpression inhibits osteoblast mineral deposition in vitro and prevents BMP-2-induced mineralization, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant HtrA1 from 293-EBNA cell culture medium partially by ultrafiltration and dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning from MC3T3-E1 cells and expression in avian myeloblastosis virus reverse transcriptase and oligo(dT) primers, overexpression in 2T3 osteoblasts and secretion of the recombinant enzyme to the cell culture medium, expression of HtrA1 in 293-EBNA cells using a mammalian episomal expression vector pCEP-His and secretion of recombinant enzyme to the culture medium
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the growth differentiation factor 6 age-related macular degeneration risk allele (rs6982567 A) is associated with 70% increased expression of HTRA1. The HTRA1 age-related macular degeneration risk allele (rs10490924 T) is associated with 94% increased HTRA1 expression
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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HtrA1 is developmentally regulated in the uterus and trophoblast during placental establishment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nie, G.; Li, Y.; Salamonsen, L.A.
Serine protease HtrA1 is developmentally regulated in trophoblast and uterine decidual cells during placental formation in the mouse
Dev. Dyn.
233
1102-1109
2005
Mus musculus
Hadfield, K.D.; Rock, C.F.; Inkson, C.A.; Dallas, S.L.; Sudre, L.; Wallis, G.A.; Boot-Handford, R.P.; Canfield, A.E.
HtrA1 inhibits mineral deposition by osteoblasts. Requirement for the protease and PDZ domains
J. Biol. Chem.
283
5928-5938
2008
Mus musculus
Gilicze, A.; Kohalmi, B.; Pocza, P.; Keszei, M.; Jaeger, J.; Gorbe, E.; Papp, Z.; Toth, S.; Falus, A.; Wiener, Z.
HtrA1 is a novel mast cell serine protease of mice and men
Mol. Immunol.
44
2961-2968
2007
Homo sapiens, Mus musculus, Mus musculus BALB/c
Zhang, L.; Lim, S.L.; Du, H.; Zhang, M.; Kozak, I.; Hannum, G.; Wang, X.; Ouyang, H.; Hughes, G.; Zhao, L.; Zhu, X.; Lee, C.; Su, Z.; Zhou, X.; Shaw, R.; Geum, D.; Wei, X.; Zhu, J.; Ideker, T.; Oka, C.; Wang, N.; Yang, Z.; Shaw, P.X.; Zhang, K.
HTRA1 regulates angiogenesis through TGF-beta family member GDF6
J. Biol. Chem.
287
1520-1526
2012
Mus musculus
Ciferri, C.; Lipari, M.T.; Liang, W.C.; Estevez, A.; Hang, J.; Stawicki, S.; Wu, Y.; Moran, P.; Elliott, M.; Eigenbrot, C.; Katschke, K.J.; van Lookeren Campagne, M.; Kirchhofer, D.
The trimeric serine protease HtrA1 forms a cage-like inhibition complex with an anti-HtrA1 antibody
Biochem. J.
472
169-181
2015
Mus musculus (Q9R118)
Ochiai, N.; Nakachi, Y.; Yokoo, T.; Ichihara, T.; Eriksson, T.; Yonemoto, Y.; Kato, T.; Ogata, H.; Fujimoto, N.; Kobayashi, Y.; Udagawa, N.; Kaku, S.; Ueki, T.; Okazaki, Y.; Takahashi, N.; Suda, T.
Murine osteoclasts secrete serine protease HtrA1 capable of degrading osteoprotegerin in the bone microenvironment
Commun. Biol.
2
86
2019
Mus musculus (Q9R118), Mus musculus
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