ABCG1

From Wikipedia, the free encyclopedia

ATP-binding cassette, sub-family G (WHITE), member 1

Identifiers

ABCG1; ABC8; MGC34313; WHITE1

External IDs

OMIM: 603076 MGI: 107704 HomoloGene: 21022

Gene ontology
Molecular Function:	• nucleotide binding • ATP binding • L-tryptophan transmembrane transporter activity • purine nucleotide transmembrane transporter activity • transmembrane transporter activity • ATPase activity • ATPase activity, coupled to transmembrane movement of substances • protein dimerization activity
Cellular Component:	• membrane fraction • endoplasmic reticulum • integral to plasma membrane • membrane
Biological Process:	• lipid transport • cholesterol metabolic process • detection of hormone stimulus • response to organic substance • cholesterol homeostasis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004915 (mRNA)
NP_004906 (protein)

NM_009593 (mRNA)
NP_033723 (protein)

Location

Chr 21: 42.51 - 42.59 Mb

Chr 17: 30.78 - 30.84 Mb

Pubmed search

[1]

[2]

ATP-binding cassette, sub-family G (WHITE), member 1, also known as ABCG1, is a human gene.^[1]

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, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. It is involved in macrophage cholesterol and phospholipids transport, and may regulate cellular lipid homeostasis in other cell types. Several alternative splice variants have been identified.^[1]

1 See also
2 References
3 Further reading
4 External links

[edit] See also

ATP-binding cassette transporter

[edit] References

^ ^a ^b Entrez Gene: ABCG1 ATP-binding cassette, sub-family G (WHITE), member 1.

[edit] Further reading

Schmitz G, Langmann T, Heimerl S (2002). "Role of ABCG1 and other ABCG family members in lipid metabolism.". J. Lipid Res. 42 (10): 1513–20. PMID 11590207.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Chen H, Rossier C, Lalioti MD, et al. (1996). "Cloning of the cDNA for a human homologue of the Drosophila white gene and mapping to chromosome 21q22.3.". Am. J. Hum. Genet. 59 (1): 66–75. PMID 8659545.
Savary S, Denizot F, Luciani M, et al. (1996). "Molecular cloning of a mammalian ABC transporter homologous to Drosophila white gene.". Mamm. Genome 7 (9): 673–6. PMID 8703120.
Croop JM, Tiller GE, Fletcher JA, et al. (1997). "Isolation and characterization of a mammalian homolog of the Drosophila white gene.". Gene 185 (1): 77–85. PMID 9034316.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Klucken J, Büchler C, Orsó E, et al. (2000). "ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a regulator of macrophage cholesterol and phospholipid transport.". Proc. Natl. Acad. Sci. U.S.A. 97 (2): 817–22. PMID 10639163.
Venkateswaran A, Repa JJ, Lobaccaro JM, et al. (2000). "Human white/murine ABC8 mRNA levels are highly induced in lipid-loaded macrophages. A transcriptional role for specific oxysterols.". J. Biol. Chem. 275 (19): 14700–7. PMID 10799558.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
Berry A, Scott HS, Kudoh J, et al. (2001). "Refined localization of autosomal recessive nonsyndromic deafness DFNB10 locus using 34 novel microsatellite markers, genomic structure, and exclusion of six known genes in the region.". Genomics 68 (1): 22–9. doi:10.1006/geno.2000.6253. PMID 10950923.
Langmann T, Porsch-Ozcürümez M, Unkelbach U, et al. (2000). "Genomic organization and characterization of the promoter of the human ATP-binding cassette transporter-G1 (ABCG1) gene.". Biochim. Biophys. Acta 1494 (1-2): 175–80. PMID 11072082.
Lorkowski S, Rust S, Engel T, et al. (2001). "Genomic sequence and structure of the human ABCG1 (ABC8) gene.". Biochem. Biophys. Res. Commun. 280 (1): 121–31. doi:10.1006/bbrc.2000.4089. PMID 11162488.
Porsch-Ozcurumez M, Langmann T, Heimerl S, et al. (2001). "The zinc finger protein 202 (ZNF202) is a transcriptional repressor of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a modulator of cellular lipid efflux.". J. Biol. Chem. 276 (15): 12427–33. doi:10.1074/jbc.M100218200. PMID 11279031.
Lorkowski S, Kratz M, Wenner C, et al. (2001). "Expression of the ATP-binding cassette transporter gene ABCG1 (ABC8) in Tangier disease.". Biochem. Biophys. Res. Commun. 283 (4): 821–30. doi:10.1006/bbrc.2001.4863. PMID 11350058.
Kennedy MA, Venkateswaran A, Tarr PT, et al. (2001). "Characterization of the human ABCG1 gene: liver X receptor activates an internal promoter that produces a novel transcript encoding an alternative form of the protein.". J. Biol. Chem. 276 (42): 39438–47. doi:10.1074/jbc.M105863200. PMID 11500512.
Kaplan R, Gan X, Menke JG, et al. (2003). "Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via an LXR-independent pathway.". J. Lipid Res. 43 (6): 952–9. PMID 12032171.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
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.
Cserepes J, Szentpétery Z, Seres L, et al. (2004). "Functional expression and characterization of the human ABCG1 and ABCG4 proteins: indications for heterodimerization.". Biochem. Biophys. Res. Commun. 320 (3): 860–7. doi:10.1016/j.bbrc.2004.06.037. PMID 15240127.

[edit] External links

MeSH ABCG1+protein,+human

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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	GLUT1, GLUT2, GLUT3, GLUT4, GLUT5, GLUT6, GLUT8, GLUT9

Other	Amino acid (CD98) - Fatty acid (CD36) - Ion channels - Ion pumps - Mitochondrial membrane transport protein - Neurotransmitter transport proteins - Nuclear (Importin, Karyopherin)