RAB3A

RAB3A
Identifiers
Aliases	RAB3A, member RAS oncogene family
External IDs	OMIM: 179490; MGI: 97843; HomoloGene: 20629; GeneCards: RAB3A; OMA:RAB3A - orthologs
Gene location (Human)
Chr.	Chromosome 19 (human)
End	18,204,042 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	71,211,323 bp
RNA expression pattern
	Top expressed in
	right frontal lobe; ; right hemisphere of cerebellum; ; Brodmann area 9; ; prefrontal cortex; ; nucleus accumbens; ; amygdala; ; putamen; ; hypothalamus; ; cingulate gyrus; ; spinal ganglia;
	Top expressed in
	primary visual cortex; ; superior frontal gyrus; ; dentate gyrus of hippocampal formation granule cell; ; cerebellar cortex; ; central gray substance of midbrain; ; subiculum; ; dorsomedial hypothalamic nucleus; ; prefrontal cortex; ; habenula; ; primary motor cortex;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; ATPase binding; GTP binding; myosin V binding; protein C-terminus binding; 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; plasma membrane; clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; clathrin-sculpted acetylcholine transport vesicle membrane; axon; terminal bouton; acrosomal vesicle; intracellular organelle; clathrin-sculpted glutamate transport vesicle membrane; cytosol; secretory granule membrane; anchored component of synaptic vesicle membrane; vesicle; protein-containing complex; presynaptic active zone; secretory granule; perinuclear region of cytoplasm;
Biological process	respiratory system process; positive regulation of ATP-dependent 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; neurotransmitter secretion; positive regulation of regulated secretory pathway; exocytosis; neutrophil degranulation; post-translational protein 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
	5864
	19339
	ENSG00000105649
	ENSMUSG00000031840
	P20336
	P63011
	NM_002866
	NM_001166399; NM_009001; NM_001328047; NM_001378892; NM_001378893
	NP_002857; NP_002857.1
	NP_001159871; NP_001314976; NP_033027; NP_001365821; NP_001365822
	Wikidata
View/Edit Human	View/Edit Mouse

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.

Interactions

RAB3A has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000105649 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031840 – 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.
^ 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.
^ 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.
^ "Entrez Gene: RAB3A RAB3A, member RAS oncogene family".
^ ^a ^b 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.
^ 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. S2CID 155875.
^ "Protein unc-13 homolog A". UniProt.
^ 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. S2CID 15162326.
^ 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.
^ 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. doi:10.1016/S0021-9258(17)42142-9. PMID 8294464.
^ 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.

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. Bibcode:1991PNAS...88.6264K. 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. doi:10.1016/S0021-9258(18)63872-4. 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. Bibcode:1994PNAS...9111963F. 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. doi:10.1016/S0021-9258(20)80546-8. 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. S2CID 4359038.
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. S2CID 15162326.
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. S2CID 33119468.
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. S2CID 10990373.
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.

This article on a gene on human chromosome 19 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000105649 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid2687157-5] 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.

[pmid7532276-6] 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.

[entrez-7] "Entrez Gene: RAB3A RAB3A, member RAS oncogene family".

[pmid12578829-8] 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.

[pmid11343654-9] 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. S2CID 155875.

[10] "Protein unc-13 homolog A". UniProt.

[pmid10025402-11] 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. S2CID 15162326.

[pmid8636125-12] 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.

[pmid8294464-13] 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. doi:10.1016/S0021-9258(17)42142-9. PMID 8294464.

[pmid12535645-14] 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.

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Interactions

References

Further reading