AP3D1

AP-3 complex subunit delta-1 is a protein that in humans is encoded by the AP3D1 gene.[5][6][7]

AP3D1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4AFI
Identifiers
Aliases	AP3D1, ADTD, hBLVR, adaptor related protein complex 3 delta 1 subunit, HPS10, adaptor related protein complex 3 subunit delta 1
External IDs	OMIM: 607246 MGI: 107734 HomoloGene: 2926 GeneCards: AP3D1
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.3 Start 2,100,988 bp[1] End 2,164,468 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 C1|10 39.72 cM Start 80,706,956 bp[2] End 80,742,264 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transporter activity Cellular component • cytoplasm • Golgi apparatus • membrane • Golgi membrane • axon • lysosomal membrane • terminal bouton • membrane coat • endosome membrane • axon cytoplasm • AP-3 adaptor complex • presynaptic endosome • cell membrane • presynapse • postsynapse • glutamatergic synapse Biological process • protein localization to organelle • protein localization to membrane • antigen processing and presentation • eye pigment biosynthetic process • anterograde axonal transport • melanosome organization • synaptic vesicle membrane organization • endosome to melanosome transport • protein transport • regulation of sequestering of zinc ion • antigen processing and presentation, exogenous lipid antigen via MHC class Ib • positive regulation of NK T cell differentiation • anterograde synaptic vesicle transport • intracellular protein transport • vesicle-mediated transport • synaptic vesicle budding from endosome • neurotransmitter receptor transport, postsynaptic endosome to lysosome • transport • protein targeting to vacuole • Golgi to vacuole transport • vesicle-mediated transport in synapse Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	8943	11776
Ensembl	ENSG00000065000	ENSMUSG00000020198
UniProt	O14617	O54774
RefSeq (mRNA)	NM_001077523 NM_001261826 NM_003938 NM_001374799	NM_007460
RefSeq (protein)	NP_001248755 NP_003929 NP_001361728	NP_031486
Location (UCSC)	Chr 19: 2.1 – 2.16 Mb	Chr 10: 80.71 – 80.74 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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][7]

Interactions

AP3D1 has been shown to interact with SYBL1.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000065000 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020198 - 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. Simpson F, Peden AA, Christopoulou L, Robinson MS (May 1997). "Characterization of the adaptor-related protein complex, AP-3". The Journal of Cell Biology. 137 (4): 835–45. doi:10.1083/jcb.137.4.835. PMC 2139840. PMID 9151686.
6. Ooi CE, Moreira JE, Dell'Angelica EC, Poy G, Wassarman DA, Bonifacino JS (Aug 1997). "Altered expression of a novel adaptin leads to defective pigment granule biogenesis in the Drosophila eye color mutant garnet". The EMBO Journal. 16 (15): 4508–18. doi:10.1093/emboj/16.15.4508. PMC 1170077. PMID 9303295.
7. "Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit".
8. Martinez-Arca S, Rudge R, Vacca M, Raposo G, Camonis J, Proux-Gillardeaux V, Daviet L, Formstecher E, Hamburger A, Filippini F, D'Esposito M, Galli T (Jul 2003). "A dual mechanism controlling the localization and function of exocytic v-SNAREs". Proceedings of the National Academy of Sciences of the United States of America. 100 (15): 9011–6. doi:10.1073/pnas.1431910100. PMC 166429. PMID 12853575.

External links

• Human AP3D1 genome location and AP3D1 gene details page in the UCSC Genome Browser.

Further reading

• Höning S, Sandoval IV, von Figura K (Aug 1998). "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3". The EMBO Journal. 17 (5): 1304–14. doi:10.1093/emboj/17.5.1304. PMC 1170479. PMID 9482728.
• Kantheti P, Qiao X, Diaz ME, Peden AA, Meyer GE, Carskadon SL, Kapfhamer D, Sufalko D, Robinson MS, Noebels JL, Burmeister M (Jul 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. doi:10.1016/S0896-6273(00)80519-X. PMID 9697856.
• Rehling P, Darsow T, Katzmann DJ, Emr SD (2000). "Formation of AP-3 transport intermediates requires Vps41 function". Nature Cell Biology. 1 (6): 346–53. doi:10.1038/14037. PMID 10559961.
• Craig HM, Reddy TR, Riggs NL, Dao PP, Guatelli JC (May 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, Gu F, Austin C, Tooze SA, Thomas G (May 2001). "PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic". The EMBO Journal. 20 (9): 2191–201. doi:10.1093/emboj/20.9.2191. PMC 125242. PMID 11331585.
• Austin C, Boehm M, Tooze SA (Apr 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. doi:10.1021/bi016064j. PMID 11926829.
• Janvier K, Craig H, Hitchin D, Madrid R, Sol-Foulon N, Renault L, Cherfils J, Cassel D, Benichou S, Guatelli J (Mar 2003). "HIV-1 Nef stabilizes the association of adaptor protein complexes with membranes". The Journal of Biological Chemistry. 278 (10): 8725–32. doi:10.1074/jbc.M210115200. PMID 12486136.
• Nie Z, Boehm M, Boja ES, Vass WC, Bonifacino JS, Fales HM, Randazzo PA (Sep 2003). "Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1". Developmental Cell. 5 (3): 513–21. doi:10.1016/S1534-5807(03)00234-X. PMID 12967569.
• Salazar G, Love R, Werner E, Doucette MM, Cheng S, Levey A, Faundez V (Feb 2004). "The zinc transporter ZnT3 interacts with AP-3 and it is preferentially targeted to a distinct synaptic vesicle subpopulation". Molecular Biology of the Cell. 15 (2): 575–87. doi:10.1091/mbc.E03-06-0401. PMC 329249. PMID 14657250.
• Lefrançois S, Janvier K, Boehm M, Ooi CE, Bonifacino JS (Oct 2004). "An ear-core interaction regulates the recruitment of the AP-3 complex to membranes". Developmental Cell. 7 (4): 619–25. doi:10.1016/j.devcel.2004.08.009. PMID 15469849.
• Coleman SH, Van Damme N, Day JR, Noviello CM, Hitchin D, Madrid R, Benichou S, Guatelli JC (Feb 2005). "Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes". Journal of Virology. 79 (4): 2066–78. doi:10.1128/JVI.79.4.2066-2078.2005. PMC 546596. PMID 15681409.
• Dong X, Li H, Derdowski A, Ding L, Burnett A, Chen X, Peters TR, Dermody TS, Woodruff E, Wang JJ, Spearman P (Mar 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, Hurbain I, Peden AA, Sviderskaya EV, Stewart A, Robinson MS, Bennett DC, Cutler DF, Bonifacino JS, Marks MS, Raposo G (2006). "Functions of adaptor protein (AP)-3 and AP-1 in tyrosinase sorting from endosomes to melanosomes". Molecular Biology of the Cell. 16 (11): 5356–72. doi:10.1091/mbc.E05-07-0626. PMC 1266432. PMID 16162817.