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Search results 101 to 122 out of 122 for Vwde

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Type Details Score
Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Allele
Vwde<em1Smoc> | MGI:7293157
Name: von Willebrand factor D and EGF domains; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
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Strain
MGI:7718321 | C57BL/6JSmoc-Vwde<em1Smoc>/Smoc
Attribute String: coisogenic, endonuclease-mediated mutation, mutant strain
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Protein Domain
IPR058727 | Helical_Vwde
Type: Domain
Description: This domain is found in mouse von Willebrand factor D and EGF domain-containing protein (Vwde) and similar animal sequences. Vwde may play a role in initial ameloblast differentiation and is involved in the maturation of enamel mineralisation []. This domain is predicted to have an all-�� helical configuration and is often found associated with .
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Protein Domain
IPR057885 | Ig_VWDE
Type: Domain
Description: This predicted immunoglobulin (Ig) domain is found in VWDE and similar sequences. This domain is often found associated with and .von Willebrand factor D and EGF domain-containing protein (WWDE) is predicted to enable signalling receptor binding activity and to be active in the cell surface and extracellular region.
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Publication
35273390 | -
First Author: Stsiapanava A
Year: 2022
Journal: Nat Struct Mol Biol
Title: Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH.
Volume: 29
Issue: 3
Pages: 190-193
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Publication
15589826 | -
First Author: Yang H
Year: 2004
Journal: FEBS Lett
Title: Identification and characterization of D8C, a novel domain present in liver-specific LZP, uromodulin and glycoprotein 2, mutated in familial juvenile hyperuricaemic nephropathy.
Volume: 578
Issue: 3
Pages: 236-8
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Publication
22306318 | J:181913
First Author: Yan B
Year: 2012
Journal: FEBS Lett
Title: OIT3 deficiency impairs uric acid reabsorption in renal tubule.
Volume: 586
Issue: 6
Pages: 760-5
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Protein Domain
IPR057774 | D8C_UMOD/GP2/OIT3-like
Type: Domain
Description: This entry represents the D8C domain (cysteine-rich domain) found in UMOD, GP2, OIT3, VWDE and similar proteins mainly found in vertebrates.Uromodulin (UMOD), glycoprotein 2 (GP2) and oncoprotein-induced transcript 3 (OIT3) constitute a phylogenetically related protein family characterised by the presence of conserved zona pellucida (ZP) and D8C domains. These paralogue proteins exhibit organ-specific expression patterns and analogous biological functions. UMOD, predominantly expressed in the renal tubules, facilitates the formation of urinary casts and mediates host defence by binding to type 1 fimbriated bacteria. UMOD functions in biogenesis and organisation of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop and may serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF []. GP2, secreted from pancreatic acinar cells, functions similarly in the gastrointestinal tract, where it binds bacterial fimbriae and contributes to mucosal immunity and pancreatic plug formation in pathological states. OIT3, primarily expressed in hepatic tissue, shares structural homology with both UMOD and GP2, suggesting a comparable protective role in liver physiology. These proteins likely evolved from a common ancestral gene through duplication events, subsequently acquiring tissue-specific functions whilst maintaining their core protective mechanisms against microbial pathogens across different organ systems [, , ].
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Protein
Q6DFV8
Organism: Mus musculus/domesticus
Length: 926  
Fragment?: false
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Protein
A0A0N4SVZ4
Organism: Mus musculus/domesticus
Length: 1773  
Fragment?: false
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Publication
32815518 | -
   
First Author: Stanisich JJ
Year: 2020
Journal: Elife
Title: The cryo-EM structure of the human uromodulin filament core reveals a unique assembly mechanism.
Volume: 9
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Publication
33196145 | -
First Author: Stsiapanava A
Year: 2020
Journal: EMBO J
Title: Cryo-EM structure of native human uromodulin, a zona pellucida module polymer.
Volume: 39
Issue: 24
Pages: e106807
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Protein
Q9D733
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: false
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Protein
Q8R4V5
Organism: Mus musculus/domesticus
Length: 546  
Fragment?: false
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Protein
A0A0R4J0B9
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
A0A140LHP0
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
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Protein
Q0VDQ3
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
Q9D6X7
Organism: Mus musculus/domesticus
Length: 573  
Fragment?: false
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Protein
Q91X17
Organism: Mus musculus/domesticus
Length: 642  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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