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Search results 501 to 560 out of 560 for Pmel

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Type Details Score
Publication
26694611 | -
First Author: Ho T
Year: 2016
Journal: J Biol Chem
Title: The Kringle-like Domain Facilitates Post-endoplasmic Reticulum Changes to Premelanosome Protein (PMEL) Oligomerization and Disulfide Bond Configuration and Promotes Amyloid Formation.
Volume: 291
Issue: 7
Pages: 3595-612
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Protein Domain
IPR046846 | PKAT_KLD
Type: Domain
Description: This is the Kringle-like domain (KLD) found in Melanocyte protein PMEL, Transmembrane glycoprotein NMB (GPNMB) and Transmembrane protein 130 (TMEM130), which is downstream the PKD domain. It contains six highly conserved cysteine residues that form the disulphide bonds of mature PMEL dimers and promotes PMEL functional amyloid formation [, ]. This domain is perfectly conserved in PMEL and GPNMB which suggests that GPNMB also forms dimers. PMEL and GPNMB, together with TMEM130 (its most ancient paralogue), have a conserved domain architecture and have been recently described as the PKAT (PKD- and KLD-Associated Transmembrane) protein family []. PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.
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Protein
Q9QY67
Organism: Mus musculus/domesticus
Length: 236  
Fragment?: true
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Protein
Q9QY70
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
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Protein
Q3UE75
Organism: Mus musculus/domesticus
Length: 274  
Fragment?: true
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Protein Domain
IPR045219 | PKAT
Type: Family
Description: This family includes Melanocyte protein PMEL (also known as PMEL-17), Transmembrane glycoprotein NMB (GPNMB) and Transmembrane protein 130, previously described as melanocyte protein PMEL-17-related family. Regarding the highly conserved domain architecture of these family members, including the PKD, KLD and transmembrane (TM) domains, the name was updated and now referred to as PKD- and KLD-Associated Transmembrane (PKAT) protein family []. TMEM130 has been identified as the most ancient paralogue of PMEL and GPNMB.PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.
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Genotype
Genotype
Symbol: Gt(ROSA)26Sor/Gt(ROSA)26Sor<+> Pmel/Pmel<+>
Background: involves: 129S6/SvEvTac * C57BL/6NCrl
Zygosity: cn
Has Mutant Allele: true
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Protein
Q99P91
Organism: Mus musculus/domesticus
Length: 574  
Fragment?: false
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Protein
Q6NXM3
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: false
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Protein
Q3TWC7
Organism: Mus musculus/domesticus
Length: 574  
Fragment?: false
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Protein
Q8BVA0
Organism: Mus musculus/domesticus
Length: 526  
Fragment?: false
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Protein
Q3TAV1
Organism: Mus musculus/domesticus
Length: 574  
Fragment?: false
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Protein
Q3TBB0
Organism: Mus musculus/domesticus
Length: 574  
Fragment?: false
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Protein
Q3TXG7
Organism: Mus musculus/domesticus
Length: 574  
Fragment?: false
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Publication
21962903 | J:210084
First Author: van Niel G
Year: 2011
Journal: Dev Cell
Title: The tetraspanin CD63 regulates ESCRT-independent and -dependent endosomal sorting during melanogenesis.
Volume: 21
Issue: 4
Pages: 708-21
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Publication
26387950 | J:315405
First Author: van Niel G
Year: 2015
Journal: Cell Rep
Title: Apolipoprotein E Regulates Amyloid Formation within Endosomes of Pigment Cells.
Volume: 13
Issue: 1
Pages: 43-51
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Publication
24403535 | J:209399
First Author: Byrne KT
Year: 2014
Journal: J Immunol
Title: Autoimmune vitiligo does not require the ongoing priming of naive CD8 T cells for disease progression or associated protection against melanoma.
Volume: 192
Issue: 4
Pages: 1433-9
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Publication
37989423 | J:343644
First Author: Sarkar H
Year: 2024
Journal: Biochim Biophys Acta Mol Basis Dis
Title: Loss of REP1 impacts choroidal melanogenesis and vasculogenesis in choroideremia.
Volume: 1870
Issue: 2
Pages: 166963
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Publication
8179825 | J:17219
First Author: Maresh GA
Year: 1994
Journal: DNA Cell Biol
Title: Cloning and expression of the gene for the melanoma-associated ME20 antigen.
Volume: 13
Issue: 2
Pages: 87-95
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Publication
27742673 | J:236709
First Author: Scheffel MJ
Year: 2016
Journal: Cancer Res
Title: Efficacy of Adoptive T-cell Therapy Is Improved by Treatment with the Antioxidant N-Acetyl Cysteine, Which Limits Activation-Induced T-cell Death.
Volume: 76
Issue: 20
Pages: 6006-6016
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Publication
7663510 | -
First Author: Hughes J
Year: 1995
Journal: Nat Genet
Title: The polycystic kidney disease 1 (PKD1) gene encodes a novel protein with multiple cell recognition domains.
Volume: 10
Issue: 2
Pages: 151-60
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Publication
11076759 | J:65818
First Author: Hou L
Year: 2000
Journal: Development
Title: Signaling and transcriptional regulation in the neural crest-derived melanocyte lineage: interactions between KIT and MITF.
Volume: 127
Issue: 24
Pages: 5379-89
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Protein Domain
IPR000601 | PKD_dom
Type: Domain
Description: The polycystic kidney disease (PKD) domain is an 80-90 amino acid module originally found in 16 copies in the extracellular segment of polycystin-1, a large cell surface glycoprotein. Polycystin-1 is encoded by the PKD1 gene, which is mutated in autosomal dominant polycystic kidney disease (ADPKD).Although its function is unknown, it may be involved in protein-protein and protein-carbohydrate interactions based on its predicted domain structure. One or more copies of the PKD domain are also found in several other extracellular proteins from higher organisms, eubacteria, and archaebacteria. Singles copies of the PKD domain are found in the melanocytes heavily glycosylated cell-surface proteins Pmel 17, MMP and Nmp. Some bacterial collagenases and proteases also contain a single PKD domain adjacent to their catalytic domains, whereas four copies are present in the heavily glycosylated surface layer protein of archaebacteria []. The PKD modules are often observed, within a same protein sequence, in association with FnIII domains [].The most conserved motif is the WDFGDGS sequence that is found in the central part of many PKD domains and could play a structural role [, ]. Determination of the solution structure of the first PKD domain from human polycystin-1 has shown that the module is built from two β-sheet, one of three strands and one of four strands, which are packed face-to-face [].
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Protein Domain
IPR035986 | PKD_dom_sf
Type: Homologous_superfamily
Description: The polycystic kidney disease (PKD) domain is an 80-90 amino acid module originally found in 16 copies in the extracellular segment of polycystin-1, a large cell surface glycoprotein. Polycystin-1 is encoded by the PKD1 gene, which is mutated in autosomal dominant polycystic kidney disease (ADPKD).Although its function is unknown, it may be involved in protein-protein and protein-carbohydrate interactions based on its predicted domain structure. One or more copies of the PKD domain are also found in several other extracellular proteins from higher organisms, eubacteria, and archaebacteria. Singles copies of the PKD domain are found in the melanocytes heavily glycosylated cell-surface proteins Pmel 17, MMP and Nmp. Some bacterial collagenases and proteases also contain a single PKD domain adjacent to their catalytic domains, whereas four copies are present in the heavily glycosylated surface layer protein of archaebacteria []. The PKD modules are often observed, within a same protein sequence, in association with FnIII domains [].The most conserved motif is the WDFGDGS sequence that is found in the central part of many PKD domains and could play a structural role [, ]. Determination of the solution structure of the first PKD domain from human polycystin-1 has shown that the module is built from two β-sheet, one of three strands and one of four strands, which are packed face-to-face [].
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Protein
Q8BQQ0
Organism: Mus musculus/domesticus
Length: 349  
Fragment?: false
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Publication
10933504 | -
First Author: Callebaut I
Year: 2000
Journal: Protein Sci
Title: HYR, an extracellular module involved in cellular adhesion and related to the immunoglobulin-like fold.
Volume: 9
Issue: 7
Pages: 1382-90
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Protein
F6XYG6
Organism: Mus musculus/domesticus
Length: 217  
Fragment?: true
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Protein
Q8K135
Organism: Mus musculus/domesticus
Length: 1048  
Fragment?: false
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Protein
Q5SZV5
Organism: Mus musculus/domesticus
Length: 1081  
Fragment?: false
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Protein
Q5DU58
Organism: Mus musculus/domesticus
Length: 838  
Fragment?: true
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Protein
F2Z497
Organism: Mus musculus/domesticus
Length: 782  
Fragment?: false
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Protein
Q3UFC3
Organism: Mus musculus/domesticus
Length: 985  
Fragment?: true
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Protein
Z4YK56
Organism: Mus musculus/domesticus
Length: 1085  
Fragment?: false
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Publication
9889186 | -
First Author: Bycroft M
Year: 1999
Journal: EMBO J
Title: The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease.
Volume: 18
Issue: 2
Pages: 297-305
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Protein
Q9EPR5
Organism: Mus musculus/domesticus
Length: 1159  
Fragment?: false
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Protein
Q8VI51
Organism: Mus musculus/domesticus
Length: 1219  
Fragment?: false
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Protein
Q9JLC4
Organism: Mus musculus/domesticus
Length: 1167  
Fragment?: false
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Protein
Q1HL23
Organism: Mus musculus/domesticus
Length: 1148  
Fragment?: false
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Protein
Q8BSV0
Organism: Mus musculus/domesticus
Length: 1192  
Fragment?: false
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Protein
E9QQ02
Organism: Mus musculus/domesticus
Length: 1192  
Fragment?: false
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Protein
E9PYT6
Organism: Mus musculus/domesticus
Length: 1168  
Fragment?: false
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Protein
A0A1B0GRB7
Organism: Mus musculus/domesticus
Length: 1179  
Fragment?: false
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Protein
A0A1B0GT94
Organism: Mus musculus/domesticus
Length: 1148  
Fragment?: false
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Protein
A0A1B0GRN1
Organism: Mus musculus/domesticus
Length: 1168  
Fragment?: false
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Protein
Q1HL24
Organism: Mus musculus/domesticus
Length: 1179  
Fragment?: false
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Protein
Q1HL22
Organism: Mus musculus/domesticus
Length: 1219  
Fragment?: false
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Protein
A0A1B0GRC4
Organism: Mus musculus/domesticus
Length: 1192  
Fragment?: false
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Protein
E9QQ63
Organism: Mus musculus/domesticus
Length: 1179  
Fragment?: false
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Protein
Q1HL25
Organism: Mus musculus/domesticus
Length: 1168  
Fragment?: false
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Protein
Q8CHA4
Organism: Mus musculus/domesticus
Length: 1185  
Fragment?: true
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Protein
Q8R526
Organism: Mus musculus/domesticus
Length: 2615  
Fragment?: false
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Protein
A0A0A0MQK4
Organism: Mus musculus/domesticus
Length: 2521  
Fragment?: true
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Protein
Q8CB67
Organism: Mus musculus/domesticus
Length: 483  
Fragment?: false
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Protein
D3Z2B1
Organism: Mus musculus/domesticus
Length: 438  
Fragment?: false
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Protein
D3Z3A7
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: true
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Protein
O08852
Organism: Mus musculus/domesticus
Length: 4293  
Fragment?: false
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Protein
Q7TN88
Organism: Mus musculus/domesticus
Length: 2461  
Fragment?: false
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Protein
E9QPG2
Organism: Mus musculus/domesticus
Length: 2462  
Fragment?: false
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Protein
E9Q4D4
Organism: Mus musculus/domesticus
Length: 2461  
Fragment?: false
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Publication
19468303 | -
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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