RAB8A

Ras-related protein Rab-8A is a protein that in humans is encoded by the RAB8A gene.

RAB8A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3QBT, 3TNF, 4LHV, 4LHW, 4LHX, 4LHY, 4LHZ, 4LI0
Identifiers
Aliases	RAB8A, MEL, RAB8, member RAS oncogene family
External IDs	OMIM: 165040; MGI: 96960; HomoloGene: 100934; GeneCards: RAB8A; OMA:RAB8A - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.11 Start 16,111,889 bp End 16,134,234 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8 B3.3|8 34.84 cM Start 72,915,044 bp End 72,937,748 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte mucosa of ileum bone marrow cells duodenum mucosa of sigmoid colon jejunal mucosa blood epithelium of colon granulocyte human penis Top expressed in granulocyte molar yolk sac tibiofemoral joint thymus duodenum right kidney epithelium of small intestine ventricular zone medial ganglionic eminence More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding GDP binding GTP binding myosin V binding protein binding protein kinase binding GTPase activity Cellular component cytoplasm ciliary basal body recycling endosome cytosol endosome centrosome phagocytic vesicle membrane Golgi apparatus cell projection membrane postsynaptic density synaptic vesicle Golgi membrane cilium ciliary base soma dendrite phagocytic vesicle centriole extracellular exosome cytoskeleton cytoplasmic vesicle extracellular matrix plasma membrane trans-Golgi network transport vesicle trans-Golgi network membrane dendritic spine recycling endosome membrane non-motile cilium secretory granule membrane midbody synapse glutamatergic synapse Biological process regulation of long-term neuronal synaptic plasticity regulation of protein transport axonogenesis vesicle docking involved in exocytosis protein secretion regulation of protein localization cell projection organization G2/M transition of mitotic cell cycle Golgi vesicle fusion to target membrane protein transport protein localization to plasma membrane cellular response to insulin stimulus cilium assembly ciliary basal body-plasma membrane docking neurotransmitter receptor transport to postsynaptic membrane regulation of autophagy autophagy post-translational protein modification regulation of exocytosis transport intracellular protein transport Rab protein signal transduction neurotransmitter receptor transport, endosome to postsynaptic membrane vesicle-mediated transport in synapse Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4218 17274 Ensembl ENSG00000167461 ENSMUSG00000003037 UniProt P61006 P55258 RefSeq (mRNA) NM_005370 NM_023126 RefSeq (protein) NP_005361 NP_005361.2 NP_075615 Location (UCSC) Chr 19: 16.11 – 16.13 Mb Chr 8: 72.92 – 72.94 Mb PubMed search
Wikidata
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Function

The protein encoded by this gene is a member of the RAS superfamily which are small GTP/GDP-binding proteins with an average size of 200 amino acids. The RAS-related proteins of the RAB/YPT family may play a role in the transport of proteins from the endoplasmic reticulum to the Golgi and the plasma membrane. This protein shares 97%, 96%, and 51% similarity with the dog RAB8, mouse MEL, and mouse YPT1 proteins, respectively and contains the 4 GTP/GDP-binding sites that are present in all the RAS proteins. The putative effector-binding site of this protein is similar to that of the RAB/YPT proteins. However, this protein contains a C-terminal CAAX motif that is characteristic of many RAS superfamily members but which is not found in YPT1 and the majority of RAB proteins. Although this gene was isolated as a transforming gene from a melanoma cell line, no linkage between MEL and malignant melanoma has been demonstrated. This oncogene is located 800 kb distal to MY09B on chromosome 19p13.1.

Interactions

RAB8A has been shown to interact with Optineurin and MAP4K2.

Further reading

• Newport J, Roemer MI (Mar 1975). "Comparative perinatal mortality under medical care foundations and other delivery models". Inquiry. 12 (1): 10–7. PMID 123217.
• Nimmo E, Padua RA, Hughes D, Brook JD, Williamson R, Johnson KJ (Mar 1989). "Confirmation and refinement of the localisation of the c-MEL locus on chromosome 19 by physical and genetic mapping". Human Genetics. 81 (4): 382–4. doi:10.1007/BF00283697. PMID 2564840. S2CID 25002878.
• Zahraoui A, Joberty G, Arpin M, Fontaine JJ, Hellio R, Tavitian A, Louvard D (Jan 1994). "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells". The Journal of Cell Biology. 124 (1–2): 101–15. doi:10.1083/jcb.124.1.101. PMC 2119893. PMID 8294494.
• Joberty G, Tavitian A, Zahraoui A (Sep 1993). "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif". FEBS Letters. 330 (3): 323–8. doi:10.1016/0014-5793(93)80897-4. PMID 8375503. S2CID 29047580.
• Ren M, Zeng J, De Lemos-Chiarandini C, Rosenfeld M, Adesnik M, Sabatini DD (May 1996). "In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase". Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 5151–5. Bibcode:1996PNAS...93.5151R. doi:10.1073/pnas.93.10.5151. PMC 39423. PMID 8643544.
• Bähler M, Kehrer I, Gordon L, Stoffler HE, Olsen AS (Jul 1997). "Physical mapping of human myosin-IXB (MYO9B), the human orthologue of the rat myosin myr 5, to chromosome 19p13.1". Genomics. 43 (1): 107–9. doi:10.1006/geno.1997.4776. PMID 9226381.
• Wilson AL, Erdman RA, Castellano F, Maltese WA (Aug 1998). "Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases". The Biochemical Journal. 333 (Pt 3): 497–504. doi:10.1042/bj3330497. PMC 1219609. PMID 9677305.
• Bao S, Zhu J, Garvey WT (Nov 1998). "Cloning of Rab GTPases expressed in human skeletal muscle: studies in insulin-resistant subjects". Hormone and Metabolic Research. 30 (11): 656–62. doi:10.1055/s-2007-978953. PMID 9918381. S2CID 23540699.
• 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.
• Hattula K, Peränen J (2001). "FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis". Current Biology. 10 (24): 1603–6. Bibcode:2000CBio...10.1603H. doi:10.1016/S0960-9822(00)00864-2. PMID 11137014. S2CID 12836037.
• Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (Mar 2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". The Journal of Biological Chemistry. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.
• Hattula K, Furuhjelm J, Arffman A, Peränen J (Sep 2002). "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport". Molecular Biology of the Cell. 13 (9): 3268–80. doi:10.1091/mbc.E02-03-0143. PMC 124888. PMID 12221131.
• Fukuda M (Apr 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". The Journal of Biological Chemistry. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
• Lau AS, Mruk DD (Apr 2003). "Rab8B GTPase and junction dynamics in the testis". Endocrinology. 144 (4): 1549–63. doi:10.1210/en.2002-220893. PMID 12639940.
• Linder MD, Uronen RL, Hölttä-Vuori M, van der Sluijs P, Peränen J, Ikonen E (Jan 2007). "Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells". Molecular Biology of the Cell. 18 (1): 47–56. doi:10.1091/mbc.E06-07-0575. PMC 1751315. PMID 17050734.