ATP-binding cassette, sub-family A (ABC1), member 7
Identifiers
Symbols ABCA7; ABCA-SSN; ABCX
External IDs OMIM605414 MGI1351646 HomoloGene22783 GeneCards: ABCA7 Gene
RNA expression pattern
PBB GE ABCA7 219577 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 10347 27403
Ensembl ENSG00000064687 ENSMUSG00000035722
UniProt Q8IZY2 Q91V24
RefSeq (mRNA) NM_019112.3 NM_013850.1
RefSeq (protein) NP_061985.2 NP_038878.1
Location (UCSC) Chr 19:
1.04 – 1.07 Mb
Chr 10:
79.46 – 79.48 Mb
PubMed search [1] [2]

ATP-binding cassette sub-family A member 7 is a protein that in humans is encoded by the ABCA7 gene.[1]

Contents

Function [link]

The 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 intra-cellular membranes. ABC genes are divided into seven distinct subfamilies: ABC1, MDR/TAP, CFTR/MRP, ALD (adrenoleukodystrophy), OABP, GCN20, and 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 full transporter has been detected predominantly in myelo-lymphatic tissues with the highest expression in peripheral leukocytes, thymus, spleen, and bone marrow. The function of this protein is not yet known; however, the expression pattern suggests a role in lipid homeostasis in cells of the immune system. Alternative splicing of this gene results in two transcript variants.[1]

See also [link]

References [link]

Further reading [link]

  • Kaminski WE, Orsó E, Diederich W, et al. (2000). "Identification of a novel human sterol-sensitive ATP-binding cassette transporter (ABCA7).". Biochem. Biophys. Res. Commun. 273 (2): 532–8. DOI:10.1006/bbrc.2000.2954. PMID 10873640. 
  • Niwa M, Maruyama H, Fujimoto T, et al. (2001). "Affinity selection of cDNA libraries by lambda phage surface display.". Gene 256 (1–2): 229–36. DOI:10.1016/S0378-1119(00)00348-6. PMID 11054552. 
  • Kaminski WE, Piehler A, Schmitz G (2001). "Genomic organization of the human cholesterol-responsive ABC transporter ABCA7: tandem linkage with the minor histocompatibility antigen HA-1 gene". Biochem. Biophys. Res. Commun. 278 (3): 782–9. DOI:10.1006/bbrc.2000.3880. PMID 11095984. 
  • Tanaka AR, Ikeda Y, Abe-Dohmae S, et al. (2001). "Human ABCA1 contains a large amino-terminal extracellular domain homologous to an epitope of Sjögren's Syndrome". Biochem. Biophys. Res. Commun. 283 (5): 1019–25. DOI:10.1006/bbrc.2001.4891. PMID 11355874. 
  • Broccardo C, Osorio J, Luciani MF, et al. (2001). "Comparative analysis of the promoter structure and genomic organization of the human and mouse ABCA7 gene encoding a novel ABCA transporter". Cytogenet. Cell Genet. 92 (3–4): 264–70. DOI:10.1159/000056914. PMID 11435699. 
  • Iida A, Saito S, Sekine A, et al. (2002). "Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8, ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8". J. Hum. Genet. 47 (6): 285–310. DOI:10.1007/s100380200041. PMID 12111378. 
  • Wang N, Lan D, Gerbod-Giannone M, et al. (2003). "ATP-binding cassette transporter A7 (ABCA7) binds apolipoprotein A-I and mediates cellular phospholipid but not cholesterol efflux". J. Biol. Chem. 278 (44): 42906–12. DOI:10.1074/jbc.M307831200. PMID 12917409. 
  • Kielar D, Kaminski WE, Liebisch G, et al. (2003). "Adenosine triphosphate binding cassette (ABC) transporters are expressed and regulated during terminal keratinocyte differentiation: a potential role for ABCA7 in epidermal lipid reorganization". J. Invest. Dermatol. 121 (3): 465–74. DOI:10.1046/j.1523-1747.2003.12404.x. PMID 12925201. 
  • Abe-Dohmae S, Ikeda Y, Matsuo M, et al. (2004). "Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein". J. Biol. Chem. 279 (1): 604–11. DOI:10.1074/jbc.M309888200. PMID 14570867. 
  • Ikeda Y, Abe-Dohmae S, Munehira Y, et al. (2004). "Posttranscriptional regulation of human ABCA7 and its function for the apoA-I-dependent lipid release". Biochem. Biophys. Res. Commun. 311 (2): 313–8. DOI:10.1016/j.bbrc.2003.10.002. PMID 14592415. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. DOI:10.1038/ng1285. PMID 14702039. 
  • Fu GK, Wang JT, Yang J, et al. (2005). "Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes". Genomics 84 (1): 205–10. DOI:10.1016/j.ygeno.2004.01.011. PMID 15203218. 
  • Hayashi M, Abe-Dohmae S, Okazaki M, et al. (2005). "Heterogeneity of high density lipoprotein generated by ABCA1 and ABCA7". J. Lipid Res. 46 (8): 1703–11. DOI:10.1194/jlr.M500092-JLR200. PMID 15930518. 
  • Jehle AW, Gardai SJ, Li S, et al. (2006). "ATP-binding cassette transporter A7 enhances phagocytosis of apoptotic cells and associated ERK signaling in macrophages". J. Cell Biol. 174 (4): 547–56. DOI:10.1083/jcb.200601030. PMC 2064260. PMID 16908670. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2064260. 

External links [link]

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



https://wn.com/ABCA7

Human Genome Organisation

The Human Genome Organisation (HUGO) is an organization involved in the Human Genome Project, a project about mapping the human genome. HUGO was established in 1989 as an international organization, primarily to foster collaboration between genome scientists around the world. The HUGO Gene Nomenclature Committee (HGNC), sometimes referred to as "HUGO", is one of HUGO's most active committees and aims to assign a unique gene name and symbol to each human gene.

History

HUGO was established in late April 1988 at the first meeting dedicated to genome mapping at Cold Spring Harbor. The idea of starting the organization stemmed from a South African biologist by the name of Sydney Brenner, who is known for his significant contributions to work on the genetic code and other areas of molecular biology, as well as winning the Nobel prize in Physiology of Medicine in 2002. A Founding Council was elected at the meeting that total 42 scientists from 17 different countries. HUGO is grounded in Geneva Switzerland, and later went on to elect an additional 178 members, bringing the total up to 220.

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