ARPC3

Protein-coding gene in humans
ARPC3
Available structures
PDBOrtholog 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
AliasesARPC3, ARC21, p21-Arc, actin related protein 2/3 complex subunit 3
External IDsOMIM: 604225; MGI: 1928375; HomoloGene: 4178; GeneCards: ARPC3; OMA:ARPC3 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for ARPC3
Genomic location for ARPC3
Band12q24.11Start110,434,823 bp[1]
End110,450,422 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for ARPC3
Genomic location for ARPC3
Band5|5 FStart122,529,941 bp[2]
End122,552,247 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • granulocyte

  • appendix

  • rectum

  • islet of Langerhans

  • gallbladder

  • right lung

  • mucosa of transverse colon

  • olfactory zone of nasal mucosa

  • smooth muscle tissue
Top expressed in
  • granulocyte

  • superior surface of tongue

  • mesenteric lymph nodes

  • stroma of bone marrow

  • endothelial cell of lymphatic vessel

  • right lung lobe

  • thymus

  • mucous cell of stomach

  • spleen

  • medial ganglionic eminence
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • actin filament binding
  • structural constituent of cytoskeleton
  • protein binding
  • actin binding
Cellular component
  • cytoplasm
  • cytosol
  • cell projection
  • membrane
  • focal adhesion
  • arp2/3 protein complex
  • actin cytoskeleton
  • extracellular exosome
  • cytoskeleton
  • lamellipodium
  • cell leading edge
  • filamentous actin
  • growth cone leading edge
  • nucleus
  • site of double-strand break
Biological process
  • Fc-gamma receptor signaling pathway involved in phagocytosis
  • ephrin receptor signaling pathway
  • regulation of actin filament polymerization
  • Arp2/3 complex-mediated actin nucleation
  • cellular response to nerve growth factor stimulus
  • membrane organization
  • actin polymerization-dependent cell motility
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10094

56378

Ensembl

ENSG00000111229

ENSMUSG00000029465

UniProt

O15145

Q9JM76

RefSeq (mRNA)

NM_001287222
NM_001278556

NM_019824

RefSeq (protein)

NP_001265485
NP_001274151

NP_062798

Location (UCSC)Chr 12: 110.43 – 110.45 MbChr 5: 122.53 – 122.55 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
ARP2/3 complex ARPC3 (21 kDa) subunit
crystal structure of arp2/3 complex with bound adp and calcium
Identifiers
SymbolP21-Arc
PfamPF04062
InterProIPR007204
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Actin-related protein 2/3 complex subunit 3 is a protein that in humans is encoded by the ARPC3 gene.[5][6][7]

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.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000111229 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029465 – 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 (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.
  6. ^ 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. doi:10.1042/bj3280105. PMC 1218893. PMID 9359840.
  7. ^ a b "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. Bibcode:1997Natur.385..265W. doi:10.1038/385265a0. PMID 9000076. S2CID 4358529.
  • 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. S2CID 30437883.
  • 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. Bibcode:2001Sci...294.1679R. doi:10.1126/science.1066333. PMID 11721045. S2CID 18088124.
  • 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. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
  • 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. Bibcode:2002PNAS...9916899M. 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. S2CID 23783563.
  • 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. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • 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. S2CID 37000096.
  • 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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  • 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

  • v
  • t
  • e
  • 1k8k: Crystal Structure of Arp2/3 Complex
    1k8k: Crystal Structure of Arp2/3 Complex
  • 1tyq: Crystal structure of Arp2/3 complex with bound ATP and calcium
    1tyq: Crystal structure of Arp2/3 complex with bound ATP and calcium
  • 1u2v: Crystal structure of Arp2/3 complex with bound ADP and calcium
    1u2v: Crystal structure of Arp2/3 complex with bound ADP and calcium
  • 2p9i: Crystal Structure of bovine Arp2/3 Complex co-crystallized with ADP and crosslinked with gluteraldehyde
    2p9i: Crystal Structure of bovine Arp2/3 Complex co-crystallized with ADP and crosslinked with gluteraldehyde
  • 2p9k: Crystal structure of bovine Arp2/3 complex co-crystallized with ATP and crosslinked with glutaraldehyde
    2p9k: Crystal structure of bovine Arp2/3 complex co-crystallized with ATP and crosslinked with glutaraldehyde
  • 2p9l: Crystal Structure of bovine Arp2/3 complex
    2p9l: Crystal Structure of bovine Arp2/3 complex
  • 2p9n: Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP
    2p9n: Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP
  • 2p9p: Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP
    2p9p: Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP
  • 2p9s: Structure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+
    2p9s: Structure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+
  • 2p9u: Crystal structure of bovine Arp2/3 complex co-crystallized with AMP-PNP and calcium
    2p9u: Crystal structure of bovine Arp2/3 complex co-crystallized with AMP-PNP and calcium


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