EXOC5

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)
End	57,268,905 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	49,304,110 bp
RNA expression pattern
	Top expressed in
	ganglionic eminence; ; corpus callosum; ; inferior ganglion of vagus nerve; ; Achilles tendon; ; subthalamic nucleus; ; secondary oocyte; ; medulla oblongata; ; superior vestibular nucleus; ; postcentral gyrus; ; islet of Langerhans;
	Top expressed in
	hand; ; superior cervical ganglion; ; medial ganglionic eminence; ; medullary collecting duct; ; foot; ; cumulus cell; ; renal corpuscle; ; neural tube; ; Paneth cell; ; blood;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein N-terminus binding ; 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
	10640
	105504
	ENSG00000070367
	ENSMUSG00000061244
	O00471
	Q3TPX4
	NM_006544
	NM_207214
	NP_006535
	NP_997097
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 30, 2024

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

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]

Related Research Articles

ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety of cellular functions that are frequently involved in trafficking of biological membranes and transmembrane protein cargo. ARF6 has specifically been implicated in endocytosis of plasma membrane proteins and also, to a lesser extent, plasma membrane protein recycling.

The exocyst is an octameric protein complex involved in vesicle trafficking, specifically the tethering and spatial targeting of post-Golgi vesicles to the plasma membrane prior to vesicle fusion. It is implicated in a number of cell processes, including exocytosis, cell migration, and growth.

MHC Class II molecules are a class of major histocompatibility complex (MHC) molecules normally found only on professional antigen-presenting cells such as dendritic cells, mononuclear phagocytes, some endothelial cells, thymic epithelial cells, and B cells. These cells are important in initiating immune responses.

AP-2 complex subunit mu is a protein that in humans is encoded by the AP2M1 gene.

Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.

AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene.

Ras-related protein Ral-A (RalA) is a protein that in humans is encoded by the RALA gene on chromosome 7. This protein is one of two paralogs of the Ral protein, the other being RalB, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers.

RalA-binding protein 1 is a protein that in humans is encoded by the RALBP1 gene.

Exocyst complex component 4 is a protein that in humans is encoded by the EXOC4 gene.

Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.

Exocyst complex component 2 is a protein that in humans is encoded by the EXOC2 gene.

Ras-related protein Ral-B (RalB) is a protein that in humans is encoded by the RALB gene on chromosome 2. This protein is one of two paralogs of the Ral protein, the other being RalA, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers.

Exocyst complex component 7 is a protein that in humans is encoded by the EXOC7 gene. It was formerly known as Exo70.

Exocyst complex component 3 is a protein that in humans is encoded by the EXOC3 gene.

Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 is a protein that in humans is encoded by the ASAP2 gene.

AP-2 complex subunit sigma is a protein that in humans is encoded by the AP2S1 gene.

Exocyst complex component 1 is a protein that in humans is encoded by the EXOC1 gene.

RalBP1-associated Eps domain-containing protein 2 is a protein that in humans is encoded by the REPS2 gene.

Exocyst complex component 8 is a protein that in humans is encoded by the EXOC8 gene.

Exocyst complex component 6 is a protein that in humans is encoded by the EXOC6 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000070367 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000061244 - 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.
↑ 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. S2CID 43733804.
1 2 "Entrez Gene: EXOC5 exocyst complex component 5".
↑ 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.

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 978-0-12-364637-8. 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. Bibcode:1997PNAS...9414438K. 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. Bibcode:2003Natur.422..629I. doi:10.1038/nature01533. hdl: 2027.42/62982 . PMID 12687004. S2CID 4395760.
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. S2CID 27764390.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000070367 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid9119050-5] 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. S2CID 43733804.

[entrez-6] 1 2 "Entrez Gene: EXOC5 exocyst complex component 5".

[pmid14662749-7] 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.

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EXOC5

Contents

Function

Interactions

Related Research Articles

References

Further reading