GGA3

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1JPL, 1JUQ, 1LF8, 1P4U, 1WR6, 1YD8

Identifiers

Aliases

GGA3

External IDs

MGI: 2384159 HomoloGene: 121703 GeneCards: GGA3

Gene ontology
Molecular function	• protein binding • ADP-ribosylation factor binding
Cellular component	• endosome • trans-Golgi network • Golgi apparatus • endosome membrane • intracellular • membrane • clathrin adaptor complex
Biological process	• protein transport • cellular protein metabolic process • intracellular protein transport • positive regulation of protein catabolic process • vesicle-mediated transport • transport
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


23163


260302

Ensembl


ENSG00000125447


ENSMUSG00000020740

UniProt


Q9NZ52


Q8BMI3

RefSeq (mRNA)

NM_001172703 NM_001172704 NM_001291641 NM_001291642 NM_014001
NM_138619


NM_001252067 NM_173048

RefSeq (protein)

NP_001166174.1 NP_001166175.1 NP_001278570.1 NP_001278571.1 NP_054720.1
NP_619525.1


NP_766636.2

Location (UCSC)

Chr 17: 75.24 – 75.26 Mb

Chr 11: 115.58 – 115.6 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

ADP-ribosylation factor-binding protein GGA3 is a protein that in humans is encoded by the GGA3 gene.^[3]^[4]

This gene encodes a member of the Golgi-localized, gamma adaptin ear-containing, ARF-binding (GGA) family. This family includes ubiquitous coat proteins that regulate the trafficking of proteins between the trans-Golgi network and the lysosome. These proteins share an amino-terminal VHS domain which mediates sorting of the mannose 6-phosphate receptors at the trans-Golgi network. They also contain a carboxy-terminal region with homology to the ear domain of gamma-adaptins. Alternative splicing of this gene results in two transcript variants.^[5]

Interactions

GGA3 has been shown to interact with ARF1^[3]^[6] and ARF3.^[4]^[7]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 Dell'Angelica EC, Puertollano R, Mullins C, Aguilar RC, Vargas JD, Hartnell LM, Bonifacino JS (May 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". J Cell Biol. 149 (1): 81–94. doi:10.1083/jcb.149.1.81. PMC 2175099. PMID 10747089.
1 2 Boman AL, Zhang C, Zhu X, Kahn RA (Jul 2000). "A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi". Mol Biol Cell. 11 (4): 1241–55. doi:10.1091/mbc.11.4.1241. PMC 14844. PMID 10749927.
↑ "Entrez Gene: GGA3 golgi associated, gamma adaptin ear containing, ARF binding protein 3".
↑ Puertollano, R; Randazzo P A; Presley J F; Hartnell L M; Bonifacino J S (Apr 2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell. United States. 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. ISSN 0092-8674. PMID 11301005.
↑ Boman, Annette L; Salo Paul D; Hauglund Melissa J; Strand Nicole L; Rensink Shelly J; Zhdankina Olga (Sep 2002). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization". Mol. Biol. Cell. United States. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. ISSN 1059-1524. PMC 124144. PMID 12221117.

Nagase T, Seki N, Tanaka A, et al. (1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID 8590280.
Hirst J, Lui WW, Bright NA, et al. (2000). "A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome.". J. Cell Biol. 149 (1): 67–80. doi:10.1083/jcb.149.1.67. PMC 2175106. PMID 10747088.
Takatsu H, Yoshino K, Nakayama K (2000). "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin.". Biochem. Biophys. Res. Commun. 271 (3): 719–25. doi:10.1006/bbrc.2000.2700. PMID 10814529.
Puertollano R, Randazzo PA, Presley JF, et al. (2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN.". Cell. 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. PMID 11301005.
Puertollano R, Aguilar RC, Gorshkova I, et al. (2001). "Sorting of mannose 6-phosphate receptors mediated by the GGAs.". Science. 292 (5522): 1712–6. doi:10.1126/science.1060750. PMID 11387475.
Misra S, Puertollano R, Kato Y, et al. (2002). "Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains.". Nature. 415 (6874): 933–7. doi:10.1038/415933a. PMID 11859375.
Takatsu H, Yoshino K, Toda K, Nakayama K (2002). "GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors.". Biochem. J. 365 (Pt 2): 369–78. doi:10.1042/BJ20020428. PMC 1222692. PMID 11950392.
Kato Y, Misra S, Puertollano R, et al. (2002). "Phosphoregulation of sorting signal-VHS domain interactions by a direct electrostatic mechanism.". Nat. Struct. Biol. 9 (7): 532–6. doi:10.1038/nsb807. PMID 12032548.
Doray B, Bruns K, Ghosh P, Kornfeld SA (2002). "Autoinhibition of the ligand-binding site of GGA1/3 VHS domains by an internal acidic cluster-dileucine motif.". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 8072–7. doi:10.1073/pnas.082235699. PMC 123022. PMID 12060753.
Wasiak S, Legendre-Guillemin V, Puertollano R, et al. (2002). "Enthoprotin: a novel clathrin-associated protein identified through subcellular proteomics.". J. Cell Biol. 158 (5): 855–62. doi:10.1083/jcb.200205078. PMC 2173151. PMID 12213833.
Doray B, Ghosh P, Griffith J, et al. (2002). "Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network.". Science. 297 (5587): 1700–3. doi:10.1126/science.1075327. PMID 12215646.
Boman AL, Salo PD, Hauglund MJ, et al. (2003). "ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization.". Mol. Biol. Cell. 13 (9): 3078–95. doi:10.1091/mbc.E02-02-0078. PMC 124144. PMID 12221117.
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. PMC 139241. PMID 12477932.
Mattera R, Arighi CN, Lodge R, et al. (2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex.". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
Wakasugi M, Waguri S, Kametaka S, et al. (2003). "Predominant expression of the short form of GGA3 in human cell lines and tissues.". Biochem. Biophys. Res. Commun. 306 (3): 687–92. doi:10.1016/S0006-291X(03)01032-5. PMID 12810073.
He X, Zhu G, Koelsch G, et al. (2003). "Biochemical and structural characterization of the interaction of memapsin 2 (beta-secretase) cytosolic domain with the VHS domain of GGA proteins.". Biochemistry. 42 (42): 12174–80. doi:10.1021/bi035199h. PMID 14567678.
Ghosh P, Griffith J, Geuze HJ, Kornfeld S (2004). "Mammalian GGAs act together to sort mannose 6-phosphate receptors.". J. Cell Biol. 163 (4): 755–66. doi:10.1083/jcb.200308038. PMC 2173681. PMID 14638859.
Shiba Y, Katoh Y, Shiba T, et al. (2004). "GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination.". J. Biol. Chem. 279 (8): 7105–11. doi:10.1074/jbc.M311702200. PMID 14660606.

PDB gallery

1jpl: GGA3 VHS domain complexed with C-terminal peptide from cation-independent mannose 6-phosphate receptor

1juq: GGA3 VHS domain complexed with C-terminal peptide from cation-dependent Mannose 6-phosphate receptor

1lf8: Complex of GGA3-VHS Domain and CI-MPR C-terminal Phosphopeptide

1p4u: CRYSTAL STRUCTURE OF GGA3 GAE DOMAIN IN COMPLEX WITH RABAPTIN-5 PEPTIDE

1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin

1yd8: COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN

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GGA3

Interactions

References

Further reading