ABCA4

From Wikipedia, the free encyclopedia


ATP-binding cassette, sub-family A (ABC1), member 4
Identifiers
Symbol(s) ABCA4; ABC10; ABCR; ARMD2; CORD3; DKFZp781N1972; FFM; RMP; RP19; STGD; STGD1
External IDs OMIM: 601691 MGI: 109424 HomoloGene: 298
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 24 11304
Ensembl ENSG00000198691 ENSMUSG00000028125
Uniprot P78363 Q3TLK5
Refseq NM_000350 (mRNA)
NP_000341 (protein)		 NM_007378 (mRNA)
NP_031404 (protein)
Location Chr 1: 94.23 - 94.36 Mb Chr 3: 122.04 - 122.17 Mb
Pubmed search [1] [2]

ATP-binding cassette, sub-family A (ABC1), member 4, also known as ABCA4, is a human gene.[1]

The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intracellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ABC1 subfamily. Members of the ABC1 subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes. This protein is a retina-specific ABC transporter with N-retinylidene-PE as a substrate. It is expressed exclusively in retina photoreceptor cells, indicating the gene product mediates transport of an essental molecule across the photoreceptor cell membrane. Mutations in this gene are found in patients diagnosed with Stargardt disease and are associated with retinitis pigmentosa-19 and macular degeneration age-related 2.[1]

Contents

[edit] See also

[edit] References

  1. ^ a b Entrez Gene: ABCA4 ATP-binding cassette, sub-family A (ABC1), member 4.

[edit] Further reading

  • MacDonald IM (2006). "Genetic aspects of age-related macular degeneration.". Can. J. Ophthalmol. 40 (3): 288–92. doi:10.1139/i05-002. PMID 15947798. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548. 
  • Allikmets R, Singh N, Sun H, et al. (1997). "A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy.". Nat. Genet. 15 (3): 236–46. doi:10.1038/ng0397-236. PMID 9054934. 
  • Martínez-Mir A, Bayés M, Vilageliu L, et al. (1997). "A new locus for autosomal recessive retinitis pigmentosa (RP19) maps to 1p13-1p21.". Genomics 40 (1): 142–6. PMID 9070931. 
  • Azarian SM, Travis GH (1997). "The photoreceptor rim protein is an ABC transporter encoded by the gene for recessive Stargardt's disease (ABCR).". FEBS Lett. 409 (2): 247–52. PMID 9202155. 
  • Sun H, Nathans J (1997). "Stargardt's ABCR is localized to the disc membrane of retinal rod outer segments.". Nat. Genet. 17 (1): 15–6. doi:10.1038/ng0997-15. PMID 9288089. 
  • Allikmets R (1997). "A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy.". Nat. Genet. 17 (1): 122. doi:10.1038/ng0997-122a. PMID 9288113. 
  • Allikmets R, Shroyer NF, Singh N, et al. (1997). "Mutation of the Stargardt disease gene (ABCR) in age-related macular degeneration.". Science 277 (5333): 1805–7. PMID 9295268. 
  • Martínez-Mir A, Paloma E, Allikmets R, et al. (1998). "Retinitis pigmentosa caused by a homozygous mutation in the Stargardt disease gene ABCR.". Nat. Genet. 18 (1): 11–2. doi:10.1038/ng0198-11. PMID 9425888. 
  • Cremers FP, van de Pol DJ, van Driel M, et al. (1998). "Autosomal recessive retinitis pigmentosa and cone-rod dystrophy caused by splice site mutations in the Stargardt's disease gene ABCR.". Hum. Mol. Genet. 7 (3): 355–62. PMID 9466990. 
  • Nasonkin I, Illing M, Koehler MR, et al. (1998). "Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 and identification of novel mutations in Stargardt's disease.". Hum. Genet. 102 (1): 21–6. PMID 9490294. 
  • Gerber S, Rozet JM, van de Pol TJ, et al. (1998). "Complete exon-intron structure of the retina-specific ATP binding transporter gene (ABCR) allows the identification of novel mutations underlying Stargardt disease.". Genomics 48 (1): 139–42. doi:10.1006/geno.1997.5164. PMID 9503029. 
  • Azarian SM, Megarity CF, Weng J, et al. (1998). "The human photoreceptor rim protein gene (ABCR): genomic structure and primer set information for mutation analysis.". Hum. Genet. 102 (6): 699–705. PMID 9703434. 
  • Rozet JM, Gerber S, Souied E, et al. (1998). "Spectrum of ABCR gene mutations in autosomal recessive macular dystrophies.". Eur. J. Hum. Genet. 6 (3): 291–5. doi:10.1038/sj.ejhg/5200221. PMID 9781034. 
  • Lewis RA, Shroyer NF, Singh N, et al. (1999). "Genotype/Phenotype analysis of a photoreceptor-specific ATP-binding cassette transporter gene, ABCR, in Stargardt disease.". Am. J. Hum. Genet. 64 (2): 422–34. PMID 9973280. 
  • Sun H, Molday RS, Nathans J (1999). "Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, the photoreceptor-specific ATP-binding cassette transporter responsible for Stargardt disease.". J. Biol. Chem. 274 (12): 8269–81. PMID 10075733. 
  • Maugeri A, van Driel MA, van de Pol DJ, et al. (2000). "The 2588G-->C mutation in the ABCR gene is a mild frequent founder mutation in the Western European population and allows the classification of ABCR mutations in patients with Stargardt disease.". Am. J. Hum. Genet. 64 (4): 1024–35. PMID 10090887. 
  • Fishman GA, Stone EM, Grover S, et al. (1999). "Variation of clinical expression in patients with Stargardt dystrophy and sequence variations in the ABCR gene.". Arch. Ophthalmol. 117 (4): 504–10. PMID 10206579. 
  • Körschen HG, Beyermann M, Müller F, et al. (1999). "Interaction of glutamic-acid-rich proteins with the cGMP signalling pathway in rod photoreceptors.". Nature 400 (6746): 761–6. doi:10.1038/23468. PMID 10466724. 
  • Zhang K, Garibaldi DC, Kniazeva M, et al. (1999). "A novel mutation in the ABCR gene in four patients with autosomal recessive Stargardt disease.". Am. J. Ophthalmol. 128 (6): 720–4. PMID 10612508. 

[edit] External links


 This membrane protein-related article is a stub. You can help Wikipedia by expanding it.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

v • d • e
Membrane proteins, carrier proteins: membrane transport proteins
ABC-transporter
A1, A2, A3, A4, A7, A8, A12, B1

B2-3, B2, B3, B4, B5, B6, B7, B9, B11

C1, C2, C3, C4, C5, C6, C8, C8-9, C10, C13, C11

D1, D2, D3, D4, E1, F1, F2

G1, G2, G4, Sterolin (G5, G8)
Solute carrier
1A1-7, 1A1, 1A2, 1A3, 1A4, 1A5, 2A1, 2A2, 2A3, 2A4, 2A5, 2A6, 2A8, 2A9, 2A10, 2A12, 3A1, 3A2, 4A1, 4A2, 4A3, 4A4, 4A5, 4A7, 4A8, 4A11, 5A1-2, 5A1, 5A3, 5A5, 5A8, 6A1, 6A2, 6A3, 6A4, 6A5, 6A8, 6A9, 6A19, 7A1, 7A2, 7A3, 7A4, 7A5, 7A7, 7A8, 7A9, 7A11, 8A1-3, 9A1, 9A2, 9A3, 9A3R1, 9A3R2, 9A5, 9A6, 9A8, 10A1, 10A2, 10A3, 10A7, 11A1, 11A2, 11A3, 12A1-2, 12A3, 12A4, 12A5, 12A6, 12A7, 14A1, 13A3, 14A2, 15A1, 15A2, 16A1, 16A2, 16A3, 16A4, 17A1, 17A5, 17A6-8, 17A7, 18A1, 18A2, 18A3, 19A1, 19A2, 19A3, 20A1, 20A2, 22A1, 22A2, 22A3, 22A4, 22A5, 22A6, 22A7, 22A9, 22A11, 22A12, 22A18, 23A1, 23A2, 24A1-2, 24A5, 25A1, 25A3, 25A4, 25A4-6, 25A8, 25A10, 25A11, 25A12, 25A13, 25A14, 25A15, 25A17, 25A19, 25A20, 25A27, 25A31, 25A37, 25A39, 26A2, 26A3, 26A4, 26A5, 26A6, 26A7, 26A8, 27A1, 27A2, 27A3, 27A4, 28A1, 28A2, 29A1, 29A2, 29A4, 30A4, 30A7, 30A8, 31A1, 31A2, 32A1, 34A1, 34A2, 34A3, 35A1, 35A2, 35B2, 35B4, 35C1, 36A1, 37A4, 38A2, 38A3, 39A1, 39A2, 39A3, 39A4, 39A6, 39A7, 40A1, 43A1 44A1, 44A2, 44A4, 45A2, O1A2, O1B1, O1B3, O2B1, O431, O4A1
Monosaccharide
Other