RAB3A

Ras-related protein Rab-3A is a protein that in humans is encoded by the RAB3A gene.[5][6][7] It is involved in calcium-triggered exocytosis in neurons.

This article is about the human gene. For the hand gesture, see Rabia sign.

RAB3A
Identifiers
Aliases	RAB3A, member RAS oncogene family
External IDs	OMIM: 179490 MGI: 97843 HomoloGene: 20629 GeneCards: RAB3A
Gene location (Human) Chr. Chromosome 19 (human)[1] Band 19p13.11 Start 18,196,784 bp[1] End 18,204,042 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8 B3.3|8 34.15 cM Start 70,754,679 bp[2] End 70,758,677 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • ATPase binding • GTP binding • myosin V binding • protein C-terminus binding • GO:0001948 protein binding • ATPase activator activity • GTP-dependent protein binding • GTPase activity • GDP-dissociation inhibitor binding Cellular component • extracellular vesicle • endosome • clathrin-sculpted monoamine transport vesicle membrane • membrane • synaptic vesicle • cell membrane • clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane • clathrin-sculpted acetylcholine transport vesicle membrane • axon • terminal bouton • Acrosome • intracellular organelle • clathrin-sculpted glutamate transport vesicle membrane • cytosol • secretory granule membrane • anchored component of synaptic vesicle membrane • vesicle • macromolecular complex • presynaptic active zone • secretory granule • perinuclear region of cytoplasm Biological process • respiratory system process • positive regulation of ATPase activity • axonogenesis • lung development • synaptic vesicle exocytosis • regulation of short-term neuronal synaptic plasticity • evoked neurotransmitter secretion • mitochondrion organization • response to electrical stimulus • post-embryonic development • constitutive secretory pathway • maintenance of presynaptic active zone structure • glutamate secretion • regulation of exocytosis • regulation of synaptic vesicle fusion to presynaptic active zone membrane • neuromuscular synaptic transmission • synaptic vesicle recycling • sensory perception of touch • protein transport • positive regulation of exocytosis • synaptic vesicle maturation • GO:0010554 neurotransmitter secretion • positive regulation of regulated secretory pathway • exocytosis • neutrophil degranulation • post-translational modification • transport • intracellular protein transport • vesicle docking involved in exocytosis • protein secretion • Rab protein signal transduction • protein localization to plasma membrane • plasma membrane repair • regulation of synaptic vesicle priming • synaptic vesicle transport • acrosomal vesicle exocytosis • regulation of synaptic vesicle exocytosis • calcium ion regulated exocytosis • synaptic vesicle clustering Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5864	19339
Ensembl	ENSG00000105649	ENSMUSG00000031840
UniProt	P20336	P63011
RefSeq (mRNA)	NM_002866	NM_001166399 NM_009001 NM_001328047
RefSeq (protein)	NP_002857 NP_002857.1	NP_001159871 NP_001314976 NP_033027 NP_001365821 NP_001365822
Location (UCSC)	Chr 19: 18.2 – 18.2 Mb	Chr 8: 70.75 – 70.76 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

RAB3A has been shown to interact with:

• RIMS1,[8][9]
• UNC13A,[10]
• RPH3A,[8][11][12] and
• CHM.[13][14]

References

1. GRCh38: Ensembl release 89: ENSG00000105649 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031840 - 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. Rousseau-Merck MF, Zahraoui A, Bernheim A, Touchot N, Miglierina R, Tavitian A, Berger R (January 1990). "Chromosome mapping of the human ras-related rab3A gene to 19p13.2". Genomics. 5 (4): 694–8. doi:10.1016/0888-7543(89)90110-9. PMID 2687157.
6. Brondyk WH, McKiernan CJ, Fortner KA, Stabila P, Holz RW, Macara IG (March 1995). "Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A". Mol Cell Biol. 15 (3): 1137–43. doi:10.1128/MCB.15.3.1137. PMC 230335. PMID 7532276.
7. "Entrez Gene: RAB3A RAB3A, member RAS oncogene family".
8. Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
9. Betz A, Thakur P, Junge HJ, Ashery U, Rhee JS, Scheuss V, Rosenmund C, Rettig J, Brose N (April 2001). "Functional interaction of the active zone proteins Munc13-1 and RIM1 in synaptic vesicle priming". Neuron. 30 (1): 183–96. doi:10.1016/s0896-6273(01)00272-0. hdl:11858/00-001M-0000-0012-F596-C. PMID 11343654.
10. "Protein unc-13 homolog A". UniProt.
11. Ostermeier C, Brunger AT (February 1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402.
12. Weber E, Jilling T, Kirk KL (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". J. Biol. Chem. 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. PMID 8636125.
13. Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (January 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". J. Biol. Chem. 269 (3): 2111–7. PMID 8294464.
14. Pereira-Leal JB, Strom M, Godfrey RF, Seabra MC (January 2003). "Structural determinants of Rab and Rab Escort Protein interaction: Rab family motifs define a conserved binding surface". Biochem. Biophys. Res. Commun. 301 (1): 92–7. doi:10.1016/s0006-291x(02)02963-7. PMID 12535645.

Further reading

• Khosravi-Far R, Lutz RJ, Cox AD, Conroy L, Bourne JR, Sinensky M, Balch WE, Buss JE, Der CJ (1991). "Isoprenoid modification of rab proteins terminating in CC or CXC motifs". Proc. Natl. Acad. Sci. U.S.A. 88 (14): 6264–8. doi:10.1073/pnas.88.14.6264. PMC 52063. PMID 1648736.
• Zahraoui A, Touchot N, Chardin P, Tavitian A (1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion". J. Biol. Chem. 264 (21): 12394–401. PMID 2501306.
• Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA (1995). "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A". Proc. Natl. Acad. Sci. U.S.A. 91 (25): 11963–7. doi:10.1073/pnas.91.25.11963. PMC 45356. PMID 7991565.
• McKiernan CJ, Brondyk WH, Macara IG (1993). "The Rab3A GTPase interacts with multiple factors through the same effector domain. Mutational analysis of cross-linking of Rab3A to a putative target protein". J. Biol. Chem. 268 (32): 24449–52. PMID 8226995.
• Trask B, Fertitta A, Christensen M, Youngblom J, Bergmann A, Copeland A, de Jong P, Mohrenweiser H, Olsen A, Carrano A (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers". Genomics. 15 (1): 133–45. doi:10.1006/geno.1993.1021. PMID 8432525.
• Johannes L, Perez F, Laran-Chich MP, Henry JP, Darchen F (1996). "Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II". Eur. J. Biochem. 239 (2): 362–8. doi:10.1111/j.1432-1033.1996.0362u.x. PMID 8706741.
• Burton JL, Slepnev V, De Camilli PV (1997). "An evolutionarily conserved domain in a subfamily of Rabs is crucial for the interaction with the guanyl nucleotide exchange factor Mss4". J. Biol. Chem. 272 (6): 3663–8. doi:10.1074/jbc.272.6.3663. PMID 9013620.
• Geppert M, Goda Y, Stevens CF, Südhof TC (1997). "The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion". Nature. 387 (6635): 810–4. doi:10.1038/42954. PMID 9194562.
• Martincic I, Peralta ME, Ngsee JK (1997). "Isolation and characterization of a dual prenylated Rab and VAMP2 receptor". J. Biol. Chem. 272 (43): 26991–8. doi:10.1074/jbc.272.43.26991. PMID 9341137.
• Ostermeier C, Brunger AT (1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. PMID 10025402.
• Jung YJ, Lee TH, Lee JY, Kim JH, Park JB (1999). "Phosphatidic acid is important to the translocation of Rab3A from the cytosol to phospholipid membranes". NeuroReport. 10 (13): 2859–63. doi:10.1097/00001756-199909090-00029. PMID 10511453.
• Sullivan M, Olsen AS, Houslay MD (2000). "Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND". Cell. Signal. 11 (10): 735–42. doi:10.1016/S0898-6568(99)00037-6. PMID 10574328.
• Clabecq A, Henry JP, Darchen F (2000). "Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP". J. Biol. Chem. 275 (41): 31786–91. doi:10.1074/jbc.M003705200. PMID 10859313.
• Haynes LP, Evans GJ, Morgan A, Burgoyne RD (2001). "A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells". J. Biol. Chem. 276 (13): 9726–32. doi:10.1074/jbc.M006959200. PMID 11134008.
• Zhang Y, Luan Z, Liu A, Hu G (2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. 497 (2–3): 99–102. doi:10.1016/S0014-5793(01)02450-4. PMID 11377421.
• Luo HR, Saiardi A, Nagata E, Ye K, Yu H, Jung TS, Luo X, Jain S, Sawa A, Snyder SH (2001). "GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase". Neuron. 31 (3): 439–51. doi:10.1016/S0896-6273(01)00384-1. PMID 11516400.
• Piiper A, Leser J, Lutz MP, Beil M, Zeuzem S (2001). "Subcellular distribution and function of Rab3A-D in pancreatic acinar AR42J cells". Biochem. Biophys. Res. Commun. 287 (3): 746–51. doi:10.1006/bbrc.2001.5651. PMID 11563859.
• Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". J. Biol. Chem. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.