AP3D1

From Wikipedia, the free encyclopedia

Adaptor-related protein complex 3, delta 1 subunit

Identifiers

AP3D1; ADTD; hBLVR

External IDs

OMIM: 607246 MGI: 107734 HomoloGene: 2926

Gene ontology
Molecular Function:	• transporter activity • binding
Cellular Component:	• Golgi apparatus
Biological Process:	• eye pigment biosynthetic process • intracellular protein transport • antigen processing and presentation • antigen processing and presentation, exogenous lipid antigen via MHC class Ib • positive regulation of NK T cell differentiation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001077523 (mRNA)
NP_001070991 (protein)

NM_007460 (mRNA)
NP_031486 (protein)

Location

Chr 19: 2.05 - 2.1 Mb

Chr 10: 80.11 - 80.15 Mb

Pubmed search

[1]

[2]

Adaptor-related protein complex 3, delta 1 subunit, also known as AP3D1, is a human gene.^[1]

AP3D1 is a subunit of the AP3 adaptor-like complex, which is not associated with clathrin. The AP3D1 subunit is implicated in intracellular biogenesis and trafficking of pigment granules and possibly platelet dense granules and neurotransmitter vesicles.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit.

[edit] Further reading

Simpson F, Peden AA, Christopoulou L, Robinson MS (1997). "Characterization of the adaptor-related protein complex, AP-3.". J. Cell Biol. 137 (4): 835–45. PMID 9151686.
Ooi CE, Moreira JE, Dell'Angelica EC, et al. (1997). "Altered expression of a novel adaptin leads to defective pigment granule biogenesis in the Drosophila eye color mutant garnet.". EMBO J. 16 (15): 4508–18. doi:10.1093/emboj/16.15.4508. PMID 9303295.
Höning S, Sandoval IV, von Figura K (1998). "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3.". EMBO J. 17 (5): 1304–14. doi:10.1093/emboj/17.5.1304. PMID 9482728.
Kantheti P, Qiao X, Diaz ME, et al. (1998). "Mutation in AP-3 delta in the mocha mouse links endosomal transport to storage deficiency in platelets, melanosomes, and synaptic vesicles.". Neuron 21 (1): 111–22. PMID 9697856.
Rehling P, Darsow T, Katzmann DJ, Emr SD (2000). "Formation of AP-3 transport intermediates requires Vps41 function.". Nat. Cell Biol. 1 (6): 346–53. doi:10.1038/14037. PMID 10559961.
Craig HM, Reddy TR, Riggs NL, et al. (2000). "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif.". Virology 271 (1): 9–17. doi:10.1006/viro.2000.0277. PMID 10814565.
Crump CM, Xiang Y, Thomas L, et al. (2001). "PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic.". EMBO J. 20 (9): 2191–201. doi:10.1093/emboj/20.9.2191. PMID 11331585.
Austin C, Boehm M, Tooze SA (2002). "Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3.". Biochemistry 41 (14): 4669–77. PMID 11926829.
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.
Janvier K, Craig H, Hitchin D, et al. (2003). "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes.". J. Biol. Chem. 278 (10): 8725–32. doi:10.1074/jbc.M210115200. PMID 12486136.
Martinez-Arca S, Rudge R, Vacca M, et al. (2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs.". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 9011–6. doi:10.1073/pnas.1431910100. PMID 12853575.
Nie Z, Boehm M, Boja ES, et al. (2003). "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1.". Dev. Cell 5 (3): 513–21. PMID 12967569.
Salazar G, Love R, Werner E, et al. (2004). "The zinc transporter ZnT3 interacts with AP-3 and it is preferentially targeted to a distinct synaptic vesicle subpopulation.". Mol. Biol. Cell 15 (2): 575–87. doi:10.1091/mbc.E03-06-0401. PMID 14657250.
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.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
Lefrançois S, Janvier K, Boehm M, et al. (2004). "An ear-core interaction regulates the recruitment of the AP-3 complex to membranes.". Dev. Cell 7 (4): 619–25. doi:10.1016/j.devcel.2004.08.009. PMID 15469849.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Coleman SH, Van Damme N, Day JR, et al. (2005). "Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes.". J. Virol. 79 (4): 2066–78. doi:10.1128/JVI.79.4.2066-2078.2005. PMID 15681409.
Dong X, Li H, Derdowski A, et al. (2005). "AP-3 directs the intracellular trafficking of HIV-1 Gag and plays a key role in particle assembly.". Cell 120 (5): 663–74. doi:10.1016/j.cell.2004.12.023. PMID 15766529.
Theos AC, Tenza D, Martina JA, et al. (2006). "Functions of adaptor protein (AP)-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes.". Mol. Biol. Cell 16 (11): 5356–72. doi:10.1091/mbc.E05-07-0626. PMID 16162817.