ABCD1

ABCD1 is a protein that transfers fatty acids into peroxisomes.

ABCD1
Identifiers
AliasesABCD1, ABC42, ALD, ALDP, AMN, ATP binding cassette subfamily D member 1
External IDsOMIM: 300371 MGI: 1349215 HomoloGene: 55426 GeneCards: ABCD1
Gene location (Human)
Chr.X chromosome (human)[1]
BandXq28Start153,724,856 bp[1]
End153,744,755 bp[1]
Orthologs
SpeciesHumanMouse
Entrez

215

11666

Ensembl

ENSG00000101986

ENSMUSG00000031378

UniProt

P33897

P48410

RefSeq (mRNA)

NM_000033

NM_007435

RefSeq (protein)

NP_000024

NP_031461

Location (UCSC)Chr X: 153.72 – 153.74 MbChr X: 73.72 – 73.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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 ALD subfamily, which is involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs in the organelle. All known peroxisomal ABC transporters are half transporters which require a partner half transporter molecule to form a functional homodimeric or heterodimeric transporter. This peroxisomal membrane protein is likely involved in the peroxisomal transport or catabolism of very long chain fatty acids.[5]

Clinical significance

Defects in this gene have been identified as the underlying cause of adrenoleukodystrophy, an X-chromosome recessively inherited demyelinating disorder of the nervous system.[5]

Model organisms

Model organisms have been used in the study of ABCD1 function. A conditional knockout mouse line, called Abcd1tm1a(EUCOMM)Wtsi[10][11] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[12][13][14]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[8][15] Twenty four tests were carried out on mutant mice but no significant abnormalities were observed.[8]

Interactions

ABCD1 has been shown to interact with PEX19.[16][17]

References
  1. GRCh38: Ensembl release 89: ENSG00000101986 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000031378 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: ABCD1 ATP-binding cassette, sub-family D (ALD), member 1".
  6. "Salmonella infection data for Abcd1". Wellcome Trust Sanger Institute.
  7. "Citrobacter infection data for Abcd1". Wellcome Trust Sanger Institute.
  8. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248): 0. doi:10.1111/j.1755-3768.2010.4142.x.
  9. Mouse Resources Portal, Wellcome Trust Sanger Institute.
  10. "International Knockout Mouse Consortium".
  11. "Mouse Genome Informatics".
  12. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (June 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  13. Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  14. Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  15. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  16. Mayerhofer PU, Kattenfeld T, Roscher AA, Muntau AC (March 2002). "Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly". Biochem. Biophys. Res. Commun. 291 (5): 1180–6. doi:10.1006/bbrc.2002.6568. PMID 11883941.
  17. Gloeckner CJ, Mayerhofer PU, Landgraf P, Muntau AC, Holzinger A, Gerber JK, Kammerer S, Adamski J, Roscher AA (April 2000). "Human adrenoleukodystrophy protein and related peroxisomal ABC transporters interact with the peroxisomal assembly protein PEX19p". Biochem. Biophys. Res. Commun. 271 (1): 144–50. doi:10.1006/bbrc.2000.2572. PMID 10777694.

Further reading

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