RAB11A

Ras-related protein Rab-11A is a protein that in humans is encoded by the RAB11A gene.^[5][6]

RAB11A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1OIV, 1OIW, 1OIX, 1YZK, 2D7C, 2GZD, 2GZH, 2HV8, 4C4P, 4D0L, 4D0M, 4LWZ, 4LX0, 4UJ3, 4UJ4, 4UJ5, 5C4G, 5C46, 5EUQ
Identifiers
Aliases	RAB11A, YL8, member RAS oncogene family
External IDs	OMIM: 605570; MGI: 1858202; HomoloGene: 37903; GeneCards: RAB11A; OMA:RAB11A - orthologs
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q22.31 Start 65,726,054 bp[1] End 65,891,989 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 C Start 64,622,581 bp[2] End 64,645,040 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gingival epithelium oral cavity mucosa of pharynx vulva amniotic fluid skin of thigh right adrenal gland right adrenal cortex rectum gallbladder Top expressed in lip granulocyte superior surface of tongue esophagus right kidney corneal stroma embryo superior frontal gyrus atrioventricular valve ventricular zone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding GTP binding myosin V binding GTPase activity microtubule binding syntaxin binding protein binding Cellular component extracellular exosome transport vesicle cytoplasm mitochondrion multivesicular body trans-Golgi network Golgi apparatus cytosol kinetochore microtubule axon spindle pole membrane centrosome perinuclear region of cytoplasm plasma membrane cleavage furrow cytoplasmic vesicle membrane cytoplasmic vesicle vesicle endosome phagocytic vesicle recycling endosome recycling endosome membrane postsynaptic recycling endosome microtubule organizing center protein-containing complex intracellular membrane-bounded organelle Schaffer collateral - CA1 synapse glutamatergic synapse intracellular anatomical structure Biological process regulation of vesicle-mediated transport positive regulation of G2/M transition of mitotic cell cycle multivesicular body assembly cell cycle astral microtubule organization regulation of long-term neuronal synaptic plasticity establishment of protein localization to membrane cytokinesis positive regulation of axon extension establishment of vesicle localization renal water homeostasis regulation of multivesicular body size establishment of protein localization to organelle neuron projection development protein localization to plasma membrane plasma membrane to endosome transport mitotic spindle assembly regulation of protein transport protein transport mitotic metaphase plate congression exosomal secretion vesicle-mediated transport positive regulation of epithelial cell migration melanosome transport ciliary basal body-plasma membrane docking positive regulation of protein localization to plasma membrane neurotransmitter receptor transport, endosome to postsynaptic membrane post-translational protein modification transport intracellular protein transport exocytosis regulation of cytokinesis Rab protein signal transduction vesicle-mediated transport in synapse amyloid-beta clearance by transcytosis small GTPase mediated signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8766 53869 Ensembl ENSG00000103769 ENSMUSG00000004771 UniProt P62491 P62492 RefSeq (mRNA) NM_004663 NM_001206836 NM_017382 RefSeq (protein) NP_001193765 NP_004654 NP_059078 Location (UCSC) Chr 15: 65.73 – 65.89 Mb Chr 9: 64.62 – 64.65 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene belongs to the small GTPase superfamily, Rab family. It is associated with both constitutive and regulated secretory pathways, and may be involved in protein transport.^[7]

Rab-11a controls intracellular trafficking of the innate immune receptor TLR4, and thereby also receptor signaling^[8]

Interactions

RAB11A has been shown to interact with:

• RAB11FIP1,^[9][10][11]
• RAB11FIP2,^[12][9][13]
• RAB11FIP3,^[9]
• RAB11FIP4,^[14] and
• RAB11FIP5^[9][13][15]
• Moesin^[16]

References

1. GRCh38: Ensembl release 89: ENSG00000103769 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000004771 – 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. Drivas GT, Shih A, Coutavas EE, D'Eustachio P, Rush MG (January 1991). "Identification and characterization of a human homolog of the Schizosaccharomyces pombe ras-like gene YPT-3". Oncogene. 6 (1): 3–9. PMID 1704119.
6. Gromov PS, Celis JE, Hansen C, Tommerup N, Gromova I, Madsen P (June 1998). "Human rab11a: transcription, chromosome mapping and effect on the expression levels of host GTP-binding proteins". FEBS Letters. 429 (3): 359–64. doi:10.1016/S0014-5793(98)00607-3. PMID 9662449.
7. "Entrez Gene: RAB11A RAB11A, member RAS oncogene family".
8. Husebye H, Aune MH, Stenvik J, Samstad E, Skjeldal F, Halaas O, Nilsen NJ, Stenmark H, Latz E, Lien E, Mollnes TE, Bakke O, Espevik T (October 2010). "The Rab11a GTPase controls Toll-like receptor 4-induced activation of interferon regulatory factor-3 on phagosomes". Immunity. 33 (4): 583–96. doi:10.1016/j.immuni.2010.09.010. PMC 10733841. PMID 20933442.
9. Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, Kumar R, Navarre J, Chan EK, Lapierre LA, Goldenring JR (October 2001). "Identification and characterization of a family of Rab11-interacting proteins". The Journal of Biological Chemistry. 276 (42): 39067–75. doi:10.1074/jbc.M104831200. PMID 11495908.
10. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
11. Lindsay AJ, Hendrick AG, Cantalupo G, Senic-Matuglia F, Goud B, Bucci C, McCaffrey MW (April 2002). "Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein". The Journal of Biological Chemistry. 277 (14): 12190–9. doi:10.1074/jbc.M108665200. PMID 11786538.
12. Lindsay AJ, McCaffrey MW (July 2002). "Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain". The Journal of Biological Chemistry. 277 (30): 27193–9. doi:10.1074/jbc.M200757200. PMID 11994279.
13. Prekeris R, Davies JM, Scheller RH (October 2001). "Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins". The Journal of Biological Chemistry. 276 (42): 38966–70. doi:10.1074/jbc.M106133200. PMID 11481332.
14. Wallace DM, Lindsay AJ, Hendrick AG, McCaffrey MW (December 2002). "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells". Biochemical and Biophysical Research Communications. 299 (5): 770–9. doi:10.1016/s0006-291x(02)02720-1. PMID 12470645.
15. Prekeris R, Klumperman J, Scheller RH (December 2000). "A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes". Molecular Cell. 6 (6): 1437–48. doi:10.1016/s1097-2765(00)00140-4. PMID 11163216.
16. Ramel D, Wang X, Laflamme C, Montell DJ, Emery G (March 2013). "Rab11 regulates cell–cell communication during collective cell movements". Nature Cell Biology. 15 (3): 317–324. doi:10.1038/ncb2681. ISSN 1465-7392. PMC 4006229. PMID 23376974.

Further reading

• Sakurada K, Uchida K, Yamaguchi K, Aisaka K, Ito S, Ohmori T, Takeyama Y, Ueda T, Hori Y, Ohyanagi H (June 1991). "Molecular cloning and characterization of a ras p21-like GTP-binding protein (24KG) from rat liver". Biochemical and Biophysical Research Communications. 177 (3): 1224–32. doi:10.1016/0006-291X(91)90672-T. PMID 1711847.
• Gromov P, Celis JE (July 1998). "Rab11a is modified in vivo by isoprenoid geranylgeranyl". Electrophoresis. 19 (10): 1803–7. doi:10.1002/elps.1150191043. PMID 9719562. S2CID 25570226.
• Zeng J, Ren M, Gravotta D, De Lemos-Chiarandini C, Lui M, Erdjument-Bromage H, Tempst P, Xu G, Shen TH, Morimoto T, Adesnik M, Sabatini DD (March 1999). "Identification of a putative effector protein for rab11 that participates in transferrin recycling". Proceedings of the National Academy of Sciences of the United States of America. 96 (6): 2840–5. Bibcode:1999PNAS...96.2840Z. doi:10.1073/pnas.96.6.2840. PMC 15856. PMID 10077598.
• Dumanchin C, Czech C, Campion D, Cuif MH, Poyot T, Martin C, Charbonnier F, Goud B, Pradier L, Frebourg T (July 1999). "Presenilins interact with Rab11, a small GTPase involved in the regulation of vesicular transport". Human Molecular Genetics. 8 (7): 1263–9. doi:10.1093/hmg/8.7.1263. PMID 10369872.
• Mammoto A, Ohtsuka T, Hotta I, Sasaki T, Takai Y (September 1999). "Rab11BP/Rabphilin-11, a downstream target of rab11 small G protein implicated in vesicle recycling". The Journal of Biological Chemistry. 274 (36): 25517–24. doi:10.1074/jbc.274.36.25517. PMID 10464283.
• Shisheva A, Chinni SR, DeMarco C (September 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.
• Prekeris R, Klumperman J, Scheller RH (December 2000). "A Rab11/Rip11 protein complex regulates apical membrane trafficking via recycling endosomes". Molecular Cell. 6 (6): 1437–48. doi:10.1016/S1097-2765(00)00140-4. PMID 11163216.
• Lapierre LA, Kumar R, Hales CM, Navarre J, Bhartur SG, Burnette JO, Provance DW, Mercer JA, Bähler M, Goldenring JR (June 2001). "Myosin vb is associated with plasma membrane recycling systems". Molecular Biology of the Cell. 12 (6): 1843–57. doi:10.1091/mbc.12.6.1843. PMC 37346. PMID 11408590.
• Prekeris R, Davies JM, Scheller RH (October 2001). "Identification of a novel Rab11/25 binding domain present in Eferin and Rip proteins". The Journal of Biological Chemistry. 276 (42): 38966–70. doi:10.1074/jbc.M106133200. PMID 11481332.
• Hales CM, Griner R, Hobdy-Henderson KC, Dorn MC, Hardy D, Kumar R, Navarre J, Chan EK, Lapierre LA, Goldenring JR (October 2001). "Identification and characterization of a family of Rab11-interacting proteins". The Journal of Biological Chemistry. 276 (42): 39067–75. doi:10.1074/jbc.M104831200. PMID 11495908.
• Lindsay AJ, Hendrick AG, Cantalupo G, Senic-Matuglia F, Goud B, Bucci C, McCaffrey MW (April 2002). "Rab coupling protein (RCP), a novel Rab4 and Rab11 effector protein". The Journal of Biological Chemistry. 277 (14): 12190–9. doi:10.1074/jbc.M108665200. PMID 11786538.
• Lindsay AJ, McCaffrey MW (July 2002). "Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain". The Journal of Biological Chemistry. 277 (30): 27193–9. doi:10.1074/jbc.M200757200. PMID 11994279.
• Scales SJ, Hesser BA, Masuda ES, Scheller RH (August 2002). "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly". The Journal of Biological Chemistry. 277 (31): 28271–9. doi:10.1074/jbc.M204929200. PMID 12145319.
• Band AM, Ali H, Vartiainen MK, Welti S, Lappalainen P, Olkkonen VM, Kuismanen E (November 2002). "Endogenous plasma membrane t-SNARE syntaxin 4 is present in rab11 positive endosomal membranes and associates with cortical actin cytoskeleton". FEBS Letters. 531 (3): 513–9. doi:10.1016/S0014-5793(02)03605-0. PMID 12435603. S2CID 24295732.
• Roosterman D, Schmidlin F, Bunnett NW (May 2003). "Rab5a and rab11a mediate agonist-induced trafficking of protease-activated receptor 2". American Journal of Physiology. Cell Physiology. 284 (5): C1319–29. doi:10.1152/ajpcell.00540.2002. PMID 12540381. S2CID 13263412.
• Tani K, Shibata M, Kawase K, Kawashima H, Hatsuzawa K, Nagahama M, Tagaya M (April 2003). "Mapping of functional domains of gamma-SNAP". The Journal of Biological Chemistry. 278 (15): 13531–8. doi:10.1074/jbc.M213205200. PMID 12554740.