EXOC1

Exocyst complex component 1 is a protein that in humans is encoded by the EXOC1 gene.[5][6][7]

EXOC1
Identifiers
Aliases	EXOC1, BM-102, SEC3, SEC3L1, SEC3P, exocyst complex component 1
External IDs	OMIM: 607879 MGI: 2445020 HomoloGene: 41241 GeneCards: EXOC1
Gene location (Human) Chr. Chromosome 4 (human)[1] Band 4q12 Start 55,853,648 bp[1] End 55,905,086 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 C3.3|5 Start 76,529,311 bp[2] End 76,570,294 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GTP-Rho binding • phosphatidylinositol-4,5-bisphosphate binding • GO:0001948 protein binding Cellular component • cytoplasmic side of apical plasma membrane • cytosol • cell membrane • membrane • exocyst • cytoplasm • perinuclear region of cytoplasm • Flemming body Biological process • protein transport • exocyst localization • Golgi to plasma membrane transport • regulation of macroautophagy • phosphatidylinositol-mediated signaling • positive regulation of protein secretion • exocytosis • transport • GO:0022415 viral process • defense response to virus Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	55763	69940
Ensembl	ENSG00000090989	ENSMUSG00000036435
UniProt	Q9NV70	Q8R3S6
RefSeq (mRNA)	NM_001024924 NM_018261 NM_178237	NM_001289770 NM_001289771 NM_027270 NM_001359370 NM_001359372 NM_001359373
RefSeq (protein)	NP_001020095 NP_060731 NP_839955	NP_001276699 NP_001276700 NP_081546 NP_001346299 NP_001346301 NP_001346302
Location (UCSC)	Chr 4: 55.85 – 55.91 Mb	Chr 5: 76.53 – 76.57 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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 the 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. Alternatively spliced transcript variants encoding distinct isoforms have been described.[7]

References

1. GRCh38: Ensembl release 89: ENSG00000090989 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000036435 - 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. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Nov 2000). "Cloning and Functional Analysis of cDNAs with Open Reading Frames for 300 Previously Undefined Genes Expressed in CD34+ Hematopoietic Stem/Progenitor Cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
6. Brymora A, Valova VA, Larsen MR, Roufogalis BD, Robinson PJ (Aug 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.
7. "Entrez Gene: EXOC1 exocyst complex component 1".

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 978-0-12-364637-8. PMID 15037366.
• Kee Y, Yoo JS, Hazuka CD, et al. (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, et al. (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.
• Matern HT, Yeaman C, Nelson WJ, Scheller RH (2001). "The Sec6/8 complex in mammalian cells: Characterization of mammalian Sec3, subunit interactions, and expression of subunits in polarized cells". Proc. Natl. Acad. Sci. U.S.A. 98 (17): 9648–53. doi:10.1073/pnas.171317898. PMC 55506. PMID 11493706.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Inoue M, Chang L, Hwang J, et al. (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, et al. (2004). "Ral GTPases regulate exocyst assembly through dual subunit interactions". J. Biol. Chem. 278 (51): 51743–8. doi:10.1074/jbc.M308702200. PMID 14525976.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.