Type |
Details |
Score |
Gene |
Type: |
gene |
Organism: |
chicken |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
93
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
285
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Kantardzhieva A |
Year: |
2005 |
Journal: |
Invest Ophthalmol Vis Sci |
Title: |
MPP5 recruits MPP4 to the CRB1 complex in photoreceptors. |
Volume: |
46 |
Issue: |
6 |
Pages: |
2192-201 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kantardzhieva A |
Year: |
2006 |
Journal: |
FEBS J |
Title: |
MPP3 is recruited to the MPP5 protein scaffold at the retinal outer limiting membrane. |
Volume: |
273 |
Issue: |
6 |
Pages: |
1152-65 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sterling N |
Year: |
2020 |
Journal: |
Hum Mol Genet |
Title: |
De novo variants in MPP5 cause global developmental delay and behavioral changes. |
Volume: |
29 |
Issue: |
20 |
Pages: |
3388-3401 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
675
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
675
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Stöhr H |
Year: |
2005 |
Journal: |
J Comp Neurol |
Title: |
Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate with Veli3 at distinct intercellular junctions of the neurosensory retina. |
Volume: |
481 |
Issue: |
1 |
Pages: |
31-41 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Publication |
First Author: |
Yamaguchi M |
Year: |
2010 |
Journal: |
Mech Dev |
Title: |
Mutations in N-cadherin and a Stardust homolog, Nagie oko, affect cell-cycle exit in zebrafish retina. |
Volume: |
127 |
Issue: |
5-6 |
Pages: |
247-64 |
|
•
•
•
•
•
|
Publication |
First Author: |
Bulgakova NA |
Year: |
2010 |
Journal: |
Mol Biol Cell |
Title: |
Antagonistic functions of two stardust isoforms in Drosophila photoreceptor cells. |
Volume: |
21 |
Issue: |
22 |
Pages: |
3915-25 |
|
•
•
•
•
•
|
Publication |
First Author: |
Park B |
Year: |
2011 |
Journal: |
J Neurosci |
Title: |
PALS1 is essential for retinal pigment epithelium structure and neural retina stratification. |
Volume: |
31 |
Issue: |
47 |
Pages: |
17230-41 |
|
•
•
•
•
•
|
Publication |
First Author: |
Das S |
Year: |
2017 |
Journal: |
J Cell Biol |
Title: |
Stardust, the Janus-faced partner of Crumbs. |
Volume: |
216 |
Issue: |
5 |
Pages: |
1219-1221 |
|
•
•
•
•
•
|
Publication |
First Author: |
Carvalho G |
Year: |
2011 |
Journal: |
PLoS One |
Title: |
Participation of the cell polarity protein PALS1 to T-cell receptor-mediated NF-κB activation. |
Volume: |
6 |
Issue: |
3 |
Pages: |
e18159 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
MPP5, also called PALS1 (protein associated with Lin7) or Nagie oko protein in zebrafish []or Stardust in Drosophila [], is a scaffolding protein which associates with Crumbs homologue 1 (CRB1), CRB2, or CRB3 through its PDZ domain and with PALS1-associated tight junction protein (PATJ) or multi-PDZ domain protein 1 (MUPP1) through its L27 domain []. The resulting tri-protein complexes are core proteins of the Crumb complex, which localizes at tight junctions or subapical regions, and is involved in the maintenance of apical-basal polarity in epithelial cells and the morphogenesis and function of photoreceptor cells []. MPP5 is critical for the proper stratification of the retina and is also expressed in T lymphocytes where it is important for TCR-mediated activation of NFkB []. Drosophila Stardust exists in several isoforms, some of which show opposing functions in photoreceptor cells, which suggests that the relative ratio of different Crumbs complexes regulates photoreceptor homeostasis []. MPP5 belongs to the membrane-associated guanylate kinase (MAGUK) p55 subfamily.The membrane-associated guanylate kinase (MAGUK) p55 subfamily (also known as MPP subfamily) members include the Drosophila Stardust protein and its vertebrate homologues, MPP1-7. They contain the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, they also contain the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains []. MPP2-7 have two additional L27 domains at their N terminus. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Gosens I |
Year: |
2007 |
Journal: |
Exp Cell Res |
Title: |
FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity complex. |
Volume: |
313 |
Issue: |
19 |
Pages: |
3959-70 |
|
•
•
•
•
•
|
Publication |
First Author: |
Gosens I |
Year: |
2007 |
Journal: |
Hum Mol Genet |
Title: |
MPP1 links the Usher protein network and the Crumbs protein complex in the retina. |
Volume: |
16 |
Issue: |
16 |
Pages: |
1993-2003 |
|
•
•
•
•
•
|
Publication |
First Author: |
Dudak A |
Year: |
2011 |
Journal: |
Eur J Cell Biol |
Title: |
Membrane palmitoylated proteins regulate trafficking and processing of nectins. |
Volume: |
90 |
Issue: |
5 |
Pages: |
365-75 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the SH3 domain of MPP3, which is a scaffolding protein that colocalizes with MPP5 and CRB1 at the subapical region adjacent to adherens junctions and may function in photoreceptor polarity. It interacts with some nectins and regulates their trafficking and processing. Nectins are cell-cell adhesion proteins involved in the establishment apical-basal polarity at cell adhesion sites []. MPP3 belongs to the membrane-associated guanylate kinase (MAGUK) p55 subfamily. The membrane-associated guanylate kinase (MAGUK) p55 subfamily (also known as MPP subfamily) members include the Drosophila Stardust protein and its vertebrate homologues, MPP1-7. They contain the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, they also contain the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains []. MPP2-7 have two additional L27 domains at their N terminus. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the SH3 domain []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Stöhr H |
Year: |
2001 |
Journal: |
Genomics |
Title: |
Cloning and characterization of the human retina-specific gene MPP4, a novel member of the p55 subfamily of MAGUK proteins. |
Volume: |
74 |
Issue: |
3 |
Pages: |
377-84 |
|
•
•
•
•
•
|
Publication |
First Author: |
te Velthuis AJ |
Year: |
2007 |
Journal: |
BMC Evol Biol |
Title: |
Molecular evolution of the MAGUK family in metazoan genomes. |
Volume: |
7 |
|
Pages: |
129 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
568
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
585
|
Fragment?: |
false |
|
•
•
•
•
•
|