ARPC3

Actin related protein 2/3 complex, subunit 3, 21kDa
PDB rendering based on 1k8k.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1k8k​, 1tyq​, 1u2v​, 2p9i​, 2p9k​, 2p9l​, 2p9n​, 2p9p​, 2p9s​, 2p9u​
Identifiers
Symbols	ARPC3 ; ARC21; p21-Arc
External IDs	OMIM: 604225 MGI: 1928375 HomoloGene: 4178 GeneCards: ARPC3 Gene
Gene ontology Molecular function • structural constituent of cytoskeleton • protein binding • actin filament binding Cellular component • cytosol • Arp2/3 protein complex • focal adhesion • actin cytoskeleton • membrane • lamellipodium • extracellular exosome Biological process • movement of cell or subcellular component • small GTPase mediated signal transduction • axon guidance • Arp2/3 complex-mediated actin nucleation • Fc-gamma receptor signaling pathway involved in phagocytosis • innate immune response • ephrin receptor signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10094	56378
Ensembl	ENSG00000111229	ENSMUSG00000029465
UniProt	O15145	Q9JM76
RefSeq (mRNA)	NM_001278556	NM_019824
RefSeq (protein)	NP_001265485	NP_062798
Location (UCSC)	Chr 12: 110.43 – 110.45 Mb	Chr 5: 122.39 – 122.41 Mb
PubMed search

ARP2/3 complex ARPC3 (21 kDa) subunit
crystal structure of arp2/3 complex with bound adp and calcium
Identifiers
Symbol	P21-Arc
Pfam	PF04062
InterPro	IPR007204
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Actin-related protein 2/3 complex subunit 3 is a protein that in humans is encoded by the ARPC3 gene.^[1][2][3]

This gene encodes one of seven subunits of the Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p21 subunit, has yet to be determined.^[3]

References

1. Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (Aug 1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". J Cell Biol 138 (2): 375–84. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.
2. Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (Jan 1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem J 328 (1): 105–12. PMC 1218893. PMID 9359840.
3. "Entrez Gene: ARPC3 actin related protein 2/3 complex, subunit 3, 21kDa".

Further reading

• Welch MD, Iwamatsu A, Mitchison TJ (1997). "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes.". Nature 385 (6613): 265–9. doi:10.1038/385265a0. PMID 9000076.
• Marchand JB, Kaiser DA, Pollard TD, Higgs HN (2001). "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex.". Nat. Cell Biol. 3 (1): 76–82. doi:10.1038/35050590. PMID 11146629.
• Zhao X, Yang Z, Qian M, Zhu X (2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub.". Biochem. Biophys. Res. Commun. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.
• Robinson RC, Turbedsky K, Kaiser DA; et al. (2001). "Crystal structure of Arp2/3 complex.". Science 294 (5547): 1679–84. doi:10.1126/science.1066333. PMID 11721045.
• Gournier H, Goley ED, Niederstrasser H; et al. (2002). "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity.". Mol. Cell 8 (5): 1041–52. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
• Andersen JS, Lyon CE, Fox AH; et al. (2002). "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• 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.
• 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.
• Andersen JS, Lam YW, Leung AK; et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Dubois T, Paléotti O, Mironov AA; et al. (2005). "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics.". Nat. Cell Biol. 7 (4): 353–64. doi:10.1038/ncb1244. PMID 15793564.
• Stelzl U, Worm U, Lalowski M; et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome.". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
• Ewing RM, Chu P, Elisma F; et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links

• ARPC3 human gene location in the UCSC Genome Browser.
• ARPC3 human gene details in the UCSC Genome Browser.