EXOC5

Exocyst complex component 5 is a protein that in humans is encoded by the EXOC5 gene.[5][6]

EXOC5
Identifiers
Aliases	EXOC5, HSEC10, PRO1912, SEC10, SEC10L1, SEC10P, exocyst complex component 5
External IDs	OMIM: 604469 MGI: 2145645 HomoloGene: 38195 GeneCards: EXOC5
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q22.3 Start 57,200,507 bp[1] End 57,268,905 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14|14 C1 Start 49,004,090 bp[2] End 49,066,653 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • Ral GTPase binding • protein N-terminus binding • GO:0001948 protein binding Cellular component • cytoplasm • cytosol • exocyst • midbody Biological process • protein transport • vesicle docking • post-Golgi vesicle-mediated transport • exocytosis • Golgi to plasma membrane transport • establishment of planar polarity • homeostasis of number of cells within a tissue • protein localization to plasma membrane • epithelial cell apoptotic process • non-motile cilium assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10640	105504
Ensembl	ENSG00000070367	ENSMUSG00000061244
UniProt	O00471	Q3TPX4
RefSeq (mRNA)	NM_006544	NM_207214
RefSeq (protein)	NP_006535	NP_997097
Location (UCSC)	Chr 14: 57.2 – 57.27 Mb	Chr 14: 49 – 49.07 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is a component of the exocyst complex, a multiple protein complex essential for targeting exocytic vesicles to specific docking sites on the plasma membrane. Though best characterized in yeast, the component proteins and functions of exocyst complex have been demonstrated to be highly conserved in higher eukaryotes. At least eight components of the exocyst complex, including this protein, are found to interact with the actin cytoskeletal remodeling and vesicle transport machinery. The complex is also essential for the biogenesis of epithelial cell surface polarity.[6]

Interactions

EXOC5 has been shown to interact with Arf6.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000070367 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000061244 - 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. Guo W, Roth D, Gatti E, De Camilli P, Novick P (Apr 1997). "Identification and characterization of homologues of the Exocyst component Sec10p". FEBS Lett. 404 (2–3): 135–9. doi:10.1016/S0014-5793(97)00109-9. PMID 9119050.
6. "Entrez Gene: EXOC5 exocyst complex component 5".
7. Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C, Camonis J, Chavrier P (Dec 2003). "ARF6 controls post-endocytic recycling through its downstream exocyst complex effector". J. Cell Biol. 163 (5): 1111–21. doi:10.1083/jcb.200305029. PMC 2173613. PMID 14662749.

Further reading

• Hsu SC, TerBush D, Abraham M, Guo W (2004). "The exocyst complex in polarized exocytosis". Int. Rev. Cytol. International Review of Cytology. 233: 243–65. doi:10.1016/S0074-7696(04)33006-8. ISBN 9780123646378. PMID 15037366.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Kee Y, Yoo JS, Hazuka CD, Peterson KE, Hsu SC, Scheller RH (1998). "Subunit structure of the mammalian exocyst complex". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14438–43. doi:10.1073/pnas.94.26.14438. PMC 25013. PMID 9405631.
• Hsu SC, Hazuka CD, Roth R, Foletti DL, Heuser J, Scheller RH (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments". Neuron. 20 (6): 1111–22. doi:10.1016/S0896-6273(00)80493-6. PMID 9655500.
• Brymora A, Valova VA, Larsen MR, Roufogalis BD, Robinson PJ (2001). "The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene". J. Biol. Chem. 276 (32): 29792–7. doi:10.1074/jbc.C100320200. PMID 11406615.
• Polzin A, Shipitsin M, Goi T, Feig LA, Turner TJ (2002). "Ral-GTPase influences the regulation of the readily releasable pool of synaptic vesicles". Mol. Cell. Biol. 22 (6): 1714–22. doi:10.1128/MCB.22.6.1714-1722.2002. PMC 135608. PMID 11865051.
• Inoue M, Chang L, Hwang J, Chiang SH, Saltiel AR (2003). "The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin" (PDF). Nature. 422 (6932): 629–33. doi:10.1038/nature01533. hdl:2027.42/62982. PMID 12687004.
• Moskalenko S, Tong C, Rosse C, Mirey G, Formstecher E, Daviet L, Camonis J, White MA (2004). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. doi:10.1074/jbc.M308702200. PMID 14525976.
• Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C, Camonis J, Chavrier P (2004). "ARF6 controls post-endocytic recycling through its downstream exocyst complex effector". J. Cell Biol. 163 (5): 1111–21. doi:10.1083/jcb.200305029. PMC 2173613. PMID 14662749.
• Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R, Guegler K, Rao MS, Mandalam R, Lebkowski J, Stanton LW (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.