RAB5A

Ras-related protein Rab-5A is a protein that in humans is encoded by the RAB5A gene.[5][6]

RAB5A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1N6H, 1N6I, 1N6K, 1N6L, 1N6N, 1N6O, 1N6P, 1N6R, 1R2Q, 1TU3, 1TU4, 3MJH, 4Q9U
Identifiers
Aliases	RAB5A, RAB5, member RAS oncogene family
External IDs	OMIM: 179512 MGI: 105926 HomoloGene: 68142 GeneCards: RAB5A
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3p24.3 Start 19,947,097 bp[1] End 19,985,175 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17 C|17 27.82 cM Start 53,479,234 bp[2] End 53,507,680 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GDP binding • GTP binding • GO:0001948 protein binding • GTPase activity • guanyl nucleotide binding Cellular component • cytoplasm • axon terminus • endosome • cell projection • membrane • synaptic vesicle • melanosome • ruffle • cell membrane • endocytic vesicle • axon • neuronal cell body • terminal bouton • dendrite • somatodendritic compartment • early endosome • phagocytic vesicle • actin cytoskeleton • membrane raft • cytoplasmic side of early endosome membrane • extracellular exosome • cytoplasmic vesicle • phagocytic vesicle membrane • cytosol • endosome membrane • clathrin-coated vesicle membrane • early endosome membrane • early phagosome • postsynaptic early endosome • anchored component of synaptic vesicle membrane Biological process • regulation of endocytosis • regulation of filopodium assembly • endocytosis • blood coagulation • receptor internalization involved in canonical Wnt signaling pathway • regulation of autophagosome assembly • synaptic vesicle recycling • early endosome to late endosome transport • transport • protein transport • positive regulation of exocytosis • regulation of synaptic vesicle exocytosis • regulation of endosome size • viral RNA genome replication • phagocytosis • phosphatidylinositol biosynthetic process • membrane organization • post-translational modification • intracellular protein transport • Rab protein signal transduction • regulation of long-term neuronal synaptic plasticity • amyloid-beta clearance by transcytosis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5868	271457
Ensembl	ENSG00000144566	ENSMUSG00000017831
UniProt	P20339	Q9CQD1
RefSeq (mRNA)	NM_004162 NM_001292048	NM_025887
RefSeq (protein)	NP_001278977 NP_004153	NP_080163
Location (UCSC)	Chr 3: 19.95 – 19.99 Mb	Chr 17: 53.48 – 53.51 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

RAB5A localizes to early endosomes where it is involved in the recruitment of RAB7A and the maturation of these compartments to late endosomes.[7] It drives the maturation of endosomes by transporting vacuolar (H+)-ATPases (V-ATPases) from trans-Golgi network to endocytic vesicles.[8]

Interactions

RAB5A has been shown to interact with:

• CHML,[9][10]
• RABEP1,[11][12][13][14]
• SDCBP,[15] and
• ZFYVE20[16]

References

1. GRCh38: Ensembl release 89: ENSG00000144566 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000017831 - 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, Touchot N, Tavitian A, Berger R (Feb 1991). "Chromosome assignment of four RAS-related RAB genes". Human Genetics. 86 (4): 350–4. doi:10.1007/BF00201831. PMID 1999336. S2CID 30730416.
6. "Entrez Gene: RAB5A RAB5A, member RAS oncogene family".
7. Huotari J, Helenius A (Aug 2011). "Endosome maturation". The EMBO Journal. 30 (17): 3481–500. doi:10.1038/emboj.2011.286. PMC 3181477. PMID 21878991.
8. Zhang C, Li A, Zhang X, Xiao H (Mar 2011). "A novel TIP30 protein complex regulates EGF receptor signaling and endocytic degradation". The Journal of Biological Chemistry. 286 (11): 9373–81. doi:10.1074/jbc.M110.207720. PMC 3058969. PMID 21252234.
9. Anant JS, Desnoyers L, Machius M, Demeler B, Hansen JC, Westover KD, Deisenhofer J, Seabra MC (Sep 1998). "Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex". Biochemistry. 37 (36): 12559–68. doi:10.1021/bi980881a. PMID 9730828.
10. Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (Jan 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". The Journal of Biological Chemistry. 269 (3): 2111–7. PMID 8294464.
11. Xiao GH, Shoarinejad F, Jin F, Golemis EA, Yeung RS (Mar 1997). "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". The Journal of Biological Chemistry. 272 (10): 6097–100. doi:10.1074/jbc.272.10.6097. PMID 9045618.
12. Vitale G, Rybin V, Christoforidis S, Thornqvist P, McCaffrey M, Stenmark H, Zerial M (Apr 1998). "Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5". The EMBO Journal. 17 (7): 1941–51. doi:10.1093/emboj/17.7.1941. PMC 1170540. PMID 9524117.
13. Stenmark H, Vitale G, Ullrich O, Zerial M (Nov 1995). "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion". Cell. 83 (3): 423–32. doi:10.1016/0092-8674(95)90120-5. PMID 8521472. S2CID 18768939.
14. Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T (Nov 2001). "Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER". FEBS Letters. 508 (2): 201–9. doi:10.1016/s0014-5793(01)02993-3. PMID 11718716. S2CID 21545088.
15. Tomoda T, Kim JH, Zhan C, Hatten ME (Mar 2004). "Role of Unc51.1 and its binding partners in CNS axon outgrowth". Genes & Development. 18 (5): 541–58. doi:10.1101/gad.1151204. PMC 374236. PMID 15014045.
16. Nielsen E, Christoforidis S, Uttenweiler-Joseph S, Miaczynska M, Dewitte F, Wilm M, Hoflack B, Zerial M (Oct 2000). "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain". The Journal of Cell Biology. 151 (3): 601–12. doi:10.1083/jcb.151.3.601. PMC 2185588. PMID 11062261.

Further reading

• Bucci C, Parton RG, Mather IH, Stunnenberg H, Simons K, Hoflack B, Zerial M (Sep 1992). "The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway". Cell. 70 (5): 715–28. doi:10.1016/0092-8674(92)90306-W. PMID 1516130.
• Zahraoui A, Touchot N, Chardin P, Tavitian A (Jul 1989). "The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion". The Journal of Biological Chemistry. 264 (21): 12394–401. PMID 2501306.
• Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA (Dec 1994). "Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A". Proceedings of the National Academy of Sciences of the United States of America. 91 (25): 11963–7. doi:10.1073/pnas.91.25.11963. PMC 45356. PMID 7991565.
• Cremers FP, Armstrong SA, Seabra MC, Brown MS, Goldstein JL (Jan 1994). "REP-2, a Rab escort protein encoded by the choroideremia-like gene". The Journal of Biological Chemistry. 269 (3): 2111–7. PMID 8294464.
• Stenmark H, Vitale G, Ullrich O, Zerial M (Nov 1995). "Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion". Cell. 83 (3): 423–32. doi:10.1016/0092-8674(95)90120-5. PMID 8521472. S2CID 18768939.
• Vita F, Soranzo MR, Borelli V, Bertoncin P, Zabucchi G (Sep 1996). "Subcellular localization of the small GTPase Rab5a in resting and stimulated human neutrophils". Experimental Cell Research. 227 (2): 367–73. doi:10.1006/excr.1996.0286. PMID 8831575.
• Xiao GH, Shoarinejad F, Jin F, Golemis EA, Yeung RS (Mar 1997). "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis". The Journal of Biological Chemistry. 272 (10): 6097–100. doi:10.1074/jbc.272.10.6097. PMID 9045618.
• Simonsen A, Lippé R, Christoforidis S, Gaullier JM, Brech A, Callaghan J, Toh BH, Murphy C, Zerial M, Stenmark H (Jul 1998). "EEA1 links PI(3)K function to Rab5 regulation of endosome fusion". Nature. 394 (6692): 494–8. doi:10.1038/28879. PMID 9697774. S2CID 4305220.
• Anant JS, Desnoyers L, Machius M, Demeler B, Hansen JC, Westover KD, Deisenhofer J, Seabra MC (Sep 1998). "Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex". Biochemistry. 37 (36): 12559–68. doi:10.1021/bi980881a. PMID 9730828.
• Bucci C, Chiariello M, Lattero D, Maiorano M, Bruni CB (May 1999). "Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1)". Biochemical and Biophysical Research Communications. 258 (3): 657–62. doi:10.1006/bbrc.1999.0651. PMID 10329441.
• Callaghan J, Nixon S, Bucci C, Toh BH, Stenmark H (Oct 1999). "Direct interaction of EEA1 with Rab5b". European Journal of Biochemistry / FEBS. 265 (1): 361–6. doi:10.1046/j.1432-1327.1999.00743.x. PMID 10491193.
• Shisheva A, Chinni SR, DeMarco C (Sep 1999). "General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications". Biochemistry. 38 (36): 11711–21. doi:10.1021/bi990200r. PMID 10512627.
• Masuda ES, Luo Y, Young C, Shen M, Rossi AB, Huang BC, Yu S, Bennett MK, Payan DG, Scheller RH (Mar 2000). "Rab37 is a novel mast cell specific GTPase localized to secretory granules". FEBS Letters. 470 (1): 61–4. doi:10.1016/S0014-5793(00)01288-6. PMID 10722846. S2CID 38218555.
• Hoffenberg S, Liu X, Nikolova L, Hall HS, Dai W, Baughn RE, Dickey BF, Barbieri MA, Aballay A, Stahl PD, Knoll BJ (Aug 2000). "A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion". The Journal of Biological Chemistry. 275 (32): 24661–9. doi:10.1074/jbc.M909600199. PMID 10818110.
• Nielsen E, Christoforidis S, Uttenweiler-Joseph S, Miaczynska M, Dewitte F, Wilm M, Hoflack B, Zerial M (Oct 2000). "Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain". The Journal of Cell Biology. 151 (3): 601–12. doi:10.1083/jcb.151.3.601. PMC 2185588. PMID 11062261.
• Hartley JL, Temple GF, Brasch MA (Nov 2000). "DNA cloning using in vitro site-specific recombination". Genome Research. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
• Lanzetti L, Rybin V, Malabarba MG, Christoforidis S, Scita G, Zerial M, Di Fiore PP (Nov 2000). "The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5". Nature. 408 (6810): 374–7. doi:10.1038/35042605. PMID 11099046. S2CID 4405293.
• Wolf RM, Wilkes JJ, Chao MV, Resh MD (Oct 2001). "Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte differentiation". Journal of Neurobiology. 49 (1): 62–78. doi:10.1002/neu.1066. PMID 11536198.
• Seachrist JL, Laporte SA, Dale LB, Babwah AV, Caron MG, Anborgh PH, Ferguson SS (Jan 2002). "Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion". The Journal of Biological Chemistry. 277 (1): 679–85. doi:10.1074/jbc.M109022200. PMID 11682489.