AP3D1

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)
End	2,164,468 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	80,578,098 bp
RNA expression pattern
	Top expressed in
	anterior pituitary; ; parotid gland; ; cerebellar vermis; ; stromal cell of endometrium; ; pylorus; ; frontal pole; ; sural nerve; ; Brodmann area 10; ; pancreatic ductal cell; ; middle temporal gyrus;
	Top expressed in
	ventromedial nucleus; ; facial motor nucleus; ; arcuate nucleus; ; habenula; ; subiculum; ; medial dorsal nucleus; ; lateral hypothalamus; ; dorsal tegmental nucleus; ; superior colliculus; ; paraventricular nucleus of hypothalamus;
	More reference expression data
	; ; ; ;
	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 ; plasma 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
	8943
	11776
	ENSG00000065000
	ENSMUSG00000020198
	O14617
	O54774
	NM_001077523 ; NM_001261826 ; NM_003938 ; NM_001374799
	NM_007460
	NP_001248755 ; NP_003929 ; NP_001361728
	NP_031486
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 25, 2023

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

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]

Related Research Articles

AP-2 complex subunit mu is a protein that in humans is encoded by the AP2M1 gene.

AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene.

AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene.

AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene.

AP-2 complex subunit beta is a protein that in humans is encoded by the AP2B1 gene.

AP-1 complex subunit mu-2 is a protein that in humans is encoded by the AP1M2 gene.

AP-3 complex subunit beta-1 is a protein that in humans is encoded by the AP3B1 gene.

AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene.

AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene.

AP-3 complex subunit mu-1 is a protein that in humans is encoded by the AP3M1 gene.

AP-1 complex subunit sigma-2 is a protein that in humans is encoded by the AP1S2 gene.

Synergin gamma also known as AP1 subunit gamma-binding protein 1 (AP1GBP1) is a protein that in humans is encoded by the SYNRG gene.

AP-3 complex subunit sigma-2 is a protein that in humans is encoded by the AP3S2 gene.

AP-3 complex subunit sigma-1 is a protein that in humans is encoded by the AP3S1 gene.

AP-3 complex subunit beta-2 is a protein that in humans is encoded by the AP3B2 gene.

AP-4 complex subunit mu-1 is a protein that in humans is encoded by the AP4M1 gene.

AP-4 complex subunit epsilon-1 is a protein that in humans is encoded by the AP4E1 gene.

Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. These proteins are synthesized in the ribosomes, processed in the endoplasmic reticulum and transported from the Golgi apparatus to the trans-Golgi network, and from there via small carrier vesicles to their final destination compartment. The association between adaptins and clathrin are important for vesicular cargo selection and transporting. Clathrin coats contain both clathrin and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Therefore, adaptor proteins are responsible for the recruitment of cargo molecules into a growing clathrin-coated pits. The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), and the monomeric GGA adaptors. Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between 16% and 26% of their amino acid sequence.

The C-terminal domain ofBeta2-adaptin is a protein domain is involved in cell trafficking by aiding import and export of substances in and out of the cell.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000065000 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020198 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit".
↑ 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. Bibcode:2003PNAS..100.9011M. 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 .

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. S2CID 17237941.
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. S2CID 24932376.
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. S2CID 14528434.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000065000 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid9151686-5] 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.

[pmid9303295-6] 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.

[entrez-7] 1 2 "Entrez Gene: AP3D1 adaptor-related protein complex 3, delta 1 subunit".

[pmid12853575-8] 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. Bibcode:2003PNAS..100.9011M. doi: 10.1073/pnas.1431910100 . PMC 166429 . PMID 12853575.

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