ACTR3

Actin-related protein 3 is a protein that in humans is encoded by the ACTR3 gene.[5]

ACTR3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2P9N, 1TYQ, 1U2V, 4JD2, 3DXK, 3UKU, 3UKR, 2P9P, 2P9K, 2P9U, 3ULE, 3RSE, 2P9S, 2P9I, 4XF2, 2P9L, 1K8K, 3DXM, 4XEI
Identifiers
Aliases	ACTR3, ARP3, ARP3 actin-related protein 3 homolog (yeast), ARP3 actin related protein 3 homolog, actin related protein 3
External IDs	OMIM: 604222 MGI: 1921367 HomoloGene: 68483 GeneCards: ACTR3
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q14.1 Start 113,890,063 bp[1] End 113,962,596 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 E2.3 Start 125,392,905 bp[2] End 125,435,727 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • structural constituent of cytoskeleton • nucleotide binding • actin binding • actin filament binding • ATP binding • GO:0001948 protein binding Cellular component • extracellular exosome • brush border • actin cytoskeleton • cytoplasm • cell projection • cytosol • lamellipodium • intercellular junction • membrane • focal adhesion • cytoskeleton • Arp2/3 complex Biological process • Fc-gamma receptor signaling pathway involved in phagocytosis • ephrin receptor signaling pathway • cilium morphogenesis • Arp2/3 complex-mediated actin nucleation • GO:0007126 meiotic cell cycle • spindle localization • asymmetric cell division • actin filament organization • cell projection organization • meiotic chromosome movement towards spindle pole • establishment or maintenance of cell polarity • movement of cell or subcellular component • meiotic cytokinesis • membrane organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10096	74117
Ensembl	ENSG00000115091	ENSMUSG00000026341
UniProt	P61158	Q99JY9
RefSeq (mRNA)	NM_001277140 NM_005721	NM_001205385 NM_001205386 NM_023735
RefSeq (protein)	NP_001264069 NP_005712	NP_001192314 NP_001192315 NP_076224
Location (UCSC)	Chr 2: 113.89 – 113.96 Mb	Chr 1: 125.39 – 125.44 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

The specific function of this gene has not yet been determined; however, the protein it encodes is known to be a major constituent of the ARP2/3 complex. This complex is located at the cell surface and is essential to cell shape and motility through lamellipodial actin assembly and protrusion.[6]

Interactions

ACTR3 has been shown to interact with Cortactin.[7][8]

References

1. GRCh38: Ensembl release 89: ENSG00000115091 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026341 - 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. Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (Jul 1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". The Journal of Cell Biology. 138 (2): 375–84. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.
6. "Entrez Gene: ACTR3 ARP3 actin-related protein 3 homolog (yeast)".
7. Weed SA, Karginov AV, Schafer DA, Weaver AM, Kinley AW, Cooper JA, Parsons JT (Oct 2000). "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". The Journal of Cell Biology. 151 (1): 29–40. doi:10.1083/jcb.151.1.29. PMC 2189811. PMID 11018051.
8. Di Ciano C, Nie Z, Szászi K, Lewis A, Uruno T, Zhan X, Rotstein OD, Mak A, Kapus A (Sep 2002). "Osmotic stress-induced remodeling of the cortical cytoskeleton". American Journal of Physiology. Cell Physiology. 283 (3): C850–65. doi:10.1152/ajpcell.00018.2002. PMID 12176742.

Further reading

• Welch MD, Iwamatsu A, Mitchison TJ (Jan 1997). "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes". Nature. 385 (6613): 265–9. Bibcode:1997Natur.385..265W. doi:10.1038/385265a0. PMID 9000076.
• Winter D, Podtelejnikov AV, Mann M, Li R (Jul 1997). "The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches". Current Biology. 7 (7): 519–29. doi:10.1016/S0960-9822(06)00223-5. PMID 9210376.
• Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (Nov 1997). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". The Biochemical Journal. 328 (1): 105–12. doi:10.1042/bj3280105. PMC 1218893. PMID 9359840.
• Ma L, Rohatgi R, Kirschner MW (Dec 1998). "The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42". Proceedings of the National Academy of Sciences of the United States of America. 95 (26): 15362–7. Bibcode:1998PNAS...9515362M. doi:10.1073/pnas.95.26.15362. PMC 28048. PMID 9860974.
• Machesky LM, Insall RH (1999). "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex". Current Biology. 8 (25): 1347–56. doi:10.1016/S0960-9822(98)00015-3. PMID 9889097.
• Suetsugu S, Miki H, Takenawa T (Jun 1999). "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex". Biochemical and Biophysical Research Communications. 260 (1): 296–302. doi:10.1006/bbrc.1999.0894. PMID 10381382.
• May RC, Hall ME, Higgs HN, Pollard TD, Chakraborty T, Wehland J, Machesky LM, Sechi AS (Jul 1999). "The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes". Current Biology. 9 (14): 759–62. doi:10.1016/S0960-9822(99)80337-6. PMID 10421578.
• Loisel TP, Boujemaa R, Pantaloni D, Carlier MF (Oct 1999). "Reconstitution of actin-based motility of Listeria and Shigella using pure proteins". Nature. 401 (6753): 613–6. Bibcode:1999Natur.401..613L. doi:10.1038/44183. PMID 10524632.
• Higgs HN, Blanchoin L, Pollard TD (Nov 1999). "Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization". Biochemistry. 38 (46): 15212–22. doi:10.1021/bi991843. PMID 10563804.
• Carlier MF, Nioche P, Broutin-L'Hermite I, Boujemaa R, Le Clainche C, Egile C, Garbay C, Ducruix A, Sansonetti P, Pantaloni D (Jul 2000). "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex". The Journal of Biological Chemistry. 275 (29): 21946–52. doi:10.1074/jbc.M000687200. PMID 10781580.
• Jay P, Bergé-Lefranc JL, Massacrier A, Roessler E, Wallis D, Muenke M, Gastaldi M, Taviaux S, Cau P, Berta P (May 2000). "ARP3beta, the gene encoding a new human actin-related protein, is alternatively spliced and predominantly expressed in brain neuronal cells". European Journal of Biochemistry / FEBS. 267 (10): 2921–8. doi:10.1046/j.1432-1327.2000.01306.x. PMID 10806390.
• Weed SA, Karginov AV, Schafer DA, Weaver AM, Kinley AW, Cooper JA, Parsons JT (Oct 2000). "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". The Journal of Cell Biology. 151 (1): 29–40. doi:10.1083/jcb.151.1.29. PMC 2189811. PMID 11018051.
• Prehoda KE, Scott JA, Mullins RD, Lim WA (Oct 2000). "Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex". Science. 290 (5492): 801–6. Bibcode:2000Sci...290..801P. doi:10.1126/science.290.5492.801. PMID 11052943.
• Marchand JB, Kaiser DA, Pollard TD, Higgs HN (Jan 2001). "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex". Nature Cell Biology. 3 (1): 76–82. doi:10.1038/35050590. PMID 11146629.
• Zhao X, Yang Z, Qian M, Zhu X (Jan 2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochemical and Biophysical Research Communications. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.
• Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD (Nov 2001). "Crystal structure of Arp2/3 complex". Science. 294 (5547): 1679–84. Bibcode:2001Sci...294.1679R. doi:10.1126/science.1066333. PMID 11721045.
• Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD (Nov 2001). "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity". Molecular Cell. 8 (5): 1041–52. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
• Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (Jan 2002). "Directed proteomic analysis of the human nucleolus". Current Biology. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• Kovacs EM, Goodwin M, Ali RG, Paterson AD, Yap AS (Mar 2002). "Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts". Current Biology. 12 (5): 379–82. doi:10.1016/S0960-9822(02)00661-9. PMID 11882288.

External links

• ACTR3 human gene location in the UCSC Genome Browser.
• ACTR3 human gene details in the UCSC Genome Browser.