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Search results 301 to 379 out of 379 for Abca4

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Type Details Score
Publication
16908670 | J:112621
First Author: Jehle AW
Year: 2006
Journal: J Cell Biol
Title: ATP-binding cassette transporter A7 enhances phagocytosis of apoptotic cells and associated ERK signaling in macrophages.
Volume: 174
Issue: 4
Pages: 547-56
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Protein
Q8CDR1
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
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Protein
A2AAW4
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: true
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Protein
Q9D4Y4
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
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Protein
Q06RJ2
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
A0A3Q4ECA2
Organism: Mus musculus/domesticus
Length: 214  
Fragment?: false
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Protein
Q8CEN1
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
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Protein
Q78XZ3
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: false
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Protein
Q8C623
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Publication
10075733 | -
First Author: Sun H
Year: 1999
Journal: J Biol Chem
Title: Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease.
Volume: 274
Issue: 12
Pages: 8269-81
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Publication
16540294 | -
First Author: Kaminski WE
Year: 2006
Journal: Biochim Biophys Acta
Title: ABC A-subfamily transporters: structure, function and disease.
Volume: 1762
Issue: 5
Pages: 510-24
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Protein Domain
IPR026082 | ABCA
Type: Family
Description: ATP-binding cassette transporters (ABC) are multipass transmembrane proteins that use the energy of ATP hydrolysis to transport substrates across membrane bilayers. Members of ABC transporter subfamily A are full-length transporters [], which consist of a single long polypeptide chain organised into two tandemly arranged halves. Each half contains a membrane-spanning domain (MSD) followed by a cytoplasmic nucleotide binding domain (NBD) []. Several members of this group have been shown to mediate the transport of a variety of physiologic lipid compounds, such as sterols, phospholipids and bile acids [, ].ABCA7 plays a role in clearance of apoptotic cells by affecting their phagocytosis []. In the human visual cycle, ABCA4 acts as an inward-directed retinoid flipase, retinoid substrates imported by ABCA4 from the extracellular or intradiscal (rod) membrane surfaces to the cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to the cytoplasmic surface, ATR is reduced to vitamin A by trans-retinol dehydrogenase (tRDH) and then transferred to the retinal pigment epithelium (RPE) where it is converted to 11-cis-retinal. ABCA4 may also play a role in photoresponse, removing ATR/NR-PE from the extracellular photoreceptor surfaces during bleach recovery []. It has been suggested that ABCA9 plays a role in monocyte differentiation and lipid homeostasis [].
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Publication
28882873 | J:269226
First Author: Trigueros-Motos L
Year: 2017
Journal: Arterioscler Thromb Vasc Biol
Title: ABCA8 Regulates Cholesterol Efflux and High-Density Lipoprotein Cholesterol Levels.
Volume: 37
Issue: 11
Pages: 2147-2155
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Protein
Q3TZM0
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Protein
Q8BZ38
Organism: Mus musculus/domesticus
Length: 719  
Fragment?: true
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Protein
A2A6R7
Organism: Mus musculus/domesticus
Length: 134  
Fragment?: true
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Protein
Q8BIS4
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
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Protein
Q8R1I3
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: true
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Protein
A2AEP6
Organism: Mus musculus/domesticus
Length: 181  
Fragment?: true
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Protein
Q8CJA1
Organism: Mus musculus/domesticus
Length: 148  
Fragment?: true
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Protein
Q8C137
Organism: Mus musculus/domesticus
Length: 839  
Fragment?: false
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Protein
Q3UF86
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
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Protein
Q3TMR1
Organism: Mus musculus/domesticus
Length: 142  
Fragment?: true
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Publication
8002831 | -
First Author: Weleber RG
Year: 1994
Journal: Arch Ophthalmol
Title: Stargardt's macular dystrophy.
Volume: 112
Issue: 6
Pages: 752-4
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Publication
1866151 | -
First Author: Fishman GA
Year: 1991
Journal: Ophthalmology
Title: Delayed rod dark adaptation in patients with Stargardt's disease.
Volume: 98
Issue: 6
Pages: 957-62
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Publication
12150964 | -
First Author: Piehler A
Year: 2002
Journal: Biochem Biophys Res Commun
Title: Molecular structure of a novel cholesterol-responsive A subclass ABC transporter, ABCA9.
Volume: 295
Issue: 2
Pages: 408-16
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Protein Domain
IPR005951 | ABCA4/ABCR
Type: Family
Description: The ABC transporter family is a group of membrane proteins that use the hydrolysis of ATP to power the translocation of a wide variety of substrates across cellular membranes. ABC transporters minimally consist of two conserved regions: a highly conserved nucleotide-binding domain (NBD) and a less conserved transmembrane domain (TMD). Eukaryotic ABC proteins are usually organised either as full transporters (containing two NBDs and two TMDs), or as half transporters (containing one NBD and one TMD), that have to form homo- or heterodimers in order to constitute a functional protein [].Retinal-specific ATP-binding cassette transporter ABCA4 (also known as the Rim protein, ABCR) is a eukaryotic protein belonging to the ABC-A subfamily of the ABC transporter family. In humans, ABCA4 is localised with opsin photopigments in outer segment disc membranes of rod and cone photoreceptor cells. It serves as an N-retinylidene-phosphatidylethanolamine and phosphatidylethanolamine importer []. Mutations in the ABCA4 gene cause Stargardt macular degeneration, a recessive disease characterised by the loss in central vision, progressive bilateral atrophy of photoreceptor and retinal pigment epithelial (RPE) cells, accumulation of fluorescent deposits in the macula, and a delay in dark adaptation [, ]. ABCR contains eight glycosylation sites. Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C-terminal half between transmembrane segment H7 and the second multi-spanning membrane domain. This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
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Publication
21554544 | J:190797
First Author: Pollock NL
Year: 2011
Journal: FEBS J
Title: The lipid translocase, ABCA4: seeing is believing.
Volume: 278
Issue: 18
Pages: 3204-14
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Publication
15550377 | J:96865
First Author: Kim WS
Year: 2005
Journal: J Biol Chem
Title: Abca7 null mice retain normal macrophage phosphatidylcholine and cholesterol efflux activity despite alterations in adipose mass and serum cholesterol levels.
Volume: 280
Issue: 5
Pages: 3989-95
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Publication
12706902 | J:83207
 
First Author: Barros SA
Year: 2003
Journal: Gene
Title: Molecular structure and characterization of a novel murine ABC transporter, Abca13.
Volume: 307
Pages: 191-200
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Publication
24791901 | J:229848
First Author: Sergouniotis PI
Year: 2014
Journal: Am J Hum Genet
Title: Biallelic variants in TTLL5, encoding a tubulin glutamylase, cause retinal dystrophy.
Volume: 94
Issue: 5
Pages: 760-9
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Publication
23008150 | J:202648
First Author: Leslie EJ
Year: 2012
Journal: Birth Defects Res A Clin Mol Teratol
Title: Expression and mutation analyses implicate ARHGAP29 as the etiologic gene for the cleft lip with or without cleft palate locus identified by genome-wide association on chromosome 1p22.
Volume: 94
Issue: 11
Pages: 934-42
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Protein
Q6PHB8
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
Q9CVK4
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: true
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Publication
11320094 | -
First Author: Bungert S
Year: 2001
Journal: J Biol Chem
Title: Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
Volume: 276
Issue: 26
Pages: 23539-46
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Protein
Q3TTQ3
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
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Protein
Q9JL37
Organism: Mus musculus/domesticus
Length: 204  
Fragment?: true
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Protein
Q8K441
Organism: Mus musculus/domesticus
Length: 1624  
Fragment?: false
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Protein
F6YSZ8
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: true
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Protein
Q6XBG1
Organism: Mus musculus/domesticus
Length: 1677  
Fragment?: false
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Protein
E9PWJ7
Organism: Mus musculus/domesticus
Length: 1678  
Fragment?: false
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Protein
E9QAF2
Organism: Mus musculus/domesticus
Length: 1677  
Fragment?: false
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Protein
Q8R420
Organism: Mus musculus/domesticus
Length: 1704  
Fragment?: false
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Protein
E9PX95
Organism: Mus musculus/domesticus
Length: 1733  
Fragment?: false
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Protein
Q5SSE9
Organism: Mus musculus/domesticus
Length: 5034  
Fragment?: false
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Protein
Q3TLK5
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
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Protein
E9PWH4
Organism: Mus musculus/domesticus
Length: 1668  
Fragment?: false
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Protein
E9Q8F8
Organism: Mus musculus/domesticus
Length: 1683  
Fragment?: false
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Protein
Q6XBG3
Organism: Mus musculus/domesticus
Length: 1683  
Fragment?: false
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Protein
Q6XBG2
Organism: Mus musculus/domesticus
Length: 1668  
Fragment?: false
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Protein
Q80XT2
Organism: Mus musculus/domesticus
Length: 1538  
Fragment?: true
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Protein
Q8BIR8
Organism: Mus musculus/domesticus
Length: 785  
Fragment?: false
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Protein
Q3TN91
Organism: Mus musculus/domesticus
Length: 778  
Fragment?: true
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Protein
Q6AXE3
Organism: Mus musculus/domesticus
Length: 1449  
Fragment?: false
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Publication
23103747 | J:198868
First Author: Coleman JA
Year: 2013
Journal: Biochim Biophys Acta
Title: Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport.
Volume: 1831
Issue: 3
Pages: 555-74
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Protein
Q8K442
Organism: Mus musculus/domesticus
Length: 1620  
Fragment?: false
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Protein
Q8K440
Organism: Mus musculus/domesticus
Length: 1620  
Fragment?: false
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Protein
Q8K449
Organism: Mus musculus/domesticus
Length: 1623  
Fragment?: false
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Protein
P41234
Organism: Mus musculus/domesticus
Length: 2434  
Fragment?: false
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Protein
Q8K448
Organism: Mus musculus/domesticus
Length: 1642  
Fragment?: false
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Protein
Q91V24
Organism: Mus musculus/domesticus
Length: 2159  
Fragment?: false
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Protein
P41233
Organism: Mus musculus/domesticus
Length: 2261  
Fragment?: false
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Protein
E9Q876
Organism: Mus musculus/domesticus
Length: 2595  
Fragment?: false
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Protein
B2RY21
Organism: Mus musculus/domesticus
Length: 2595  
Fragment?: false
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Protein
E9Q6G4
Organism: Mus musculus/domesticus
Length: 2167  
Fragment?: false
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Protein
Q8BPY1
Organism: Mus musculus/domesticus
Length: 1487  
Fragment?: true
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Protein
B7ZNA4
Organism: Mus musculus/domesticus
Length: 2167  
Fragment?: false
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Protein
A2AEP5
Organism: Mus musculus/domesticus
Length: 1194  
Fragment?: true
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Protein
A2AM56
Organism: Mus musculus/domesticus
Length: 1620  
Fragment?: false
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Protein
B2RY11
Organism: Mus musculus/domesticus
Length: 2595  
Fragment?: false
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Protein
A4PBQ7
Organism: Mus musculus/domesticus
Length: 1619  
Fragment?: false
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Protein
A2AJ26
Organism: Mus musculus/domesticus
Length: 2433  
Fragment?: false
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Protein
F8WGE3
Organism: Mus musculus/domesticus
Length: 1619  
Fragment?: false
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Protein
B2RWU5
Organism: Mus musculus/domesticus
Length: 2167  
Fragment?: false
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Protein
Q6ZPZ4
Organism: Mus musculus/domesticus
Length: 1416  
Fragment?: true
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Protein
A4PBQ8
Organism: Mus musculus/domesticus
Length: 1591  
Fragment?: false
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Publication
11441126 | -
First Author: Dean M
Year: 2001
Journal: J Lipid Res
Title: The human ATP-binding cassette (ABC) transporter superfamily.
Volume: 42
Issue: 7
Pages: 1007-17
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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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.

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Cambridge CB2 3EH, United Kingdom