ID ARPC2_BOVIN Reviewed; 300 AA. AC Q3MHR7; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 134. DE RecName: Full=Actin-related protein 2/3 complex subunit 2; DE AltName: Full=Arp2/3 complex 34 kDa subunit; DE Short=p34-ARC; GN Name=ARPC2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF THE ARP2/3 COMPLEX. RX PubMed=11721045; DOI=10.1126/science.1066333; RA Robinson R.C., Turbedsky K., Kaiser D.A., Marchand J.-B., Higgs H.N., RA Choe S., Pollard T.D.; RT "Crystal structure of Arp2/3 complex."; RL Science 294:1679-1684(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF THE ARP2/3 COMPLEX WITH BOUND RP ATP. RX PubMed=15505213; DOI=10.1073/pnas.0407149101; RA Nolen B.J., Littlefield R.S., Pollard T.D.; RT "Crystal structures of actin-related protein 2/3 complex with bound ATP or RT ADP."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15627-15632(2004). CC -!- FUNCTION: Actin-binding component of the Arp2/3 complex, a multiprotein CC complex that mediates actin polymerization upon stimulation by CC nucleation-promoting factor (NPF). The Arp2/3 complex mediates the CC formation of branched actin networks in the cytoplasm, providing the CC force for cell motility. Seems to contact the mother actin filament. In CC addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 CC complex also promotes actin polymerization in the nucleus, thereby CC regulating gene transcription and repair of damaged DNA. The Arp2/3 CC complex promotes homologous recombination (HR) repair in response to CC DNA damage by promoting nuclear actin polymerization, leading to drive CC motility of double-strand breaks (DSBs). CC {ECO:0000250|UniProtKB:O15144}. CC -!- SUBUNIT: Component of the Arp2/3 complex composed of ACTR2/ARP2, CC ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC CC and ARPC5/p16-ARC (PubMed:11721045, PubMed:15505213). Interacts with CC SHANK3; the interaction probably mediates the association of SHANK3 CC with the Arp2/3 complex (By similarity). Interacts with DNAI3; this CC interaction reduces binding of the Arp2/3 complex to the VCA domain of CC nucleation promoting factors (By similarity). CC {ECO:0000250|UniProtKB:P61160, ECO:0000250|UniProtKB:Q9CVB6, CC ECO:0000269|PubMed:11721045, ECO:0000269|PubMed:15505213}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:O15144}. Cell projection CC {ECO:0000250|UniProtKB:O15144}. Synapse, synaptosome CC {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus {ECO:0000250|UniProtKB:O15144}. CC -!- SIMILARITY: Belongs to the ARPC2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC105136; AAI05137.1; -; mRNA. DR RefSeq; NP_001029885.1; NM_001034713.2. DR PDB; 1K8K; X-ray; 2.00 A; D=1-300. DR PDB; 1TYQ; X-ray; 2.55 A; D=1-300. DR PDB; 1U2V; X-ray; 2.55 A; D=1-300. DR PDB; 2P9I; X-ray; 2.46 A; D=1-300. DR PDB; 2P9K; X-ray; 2.59 A; D=1-300. DR PDB; 2P9L; X-ray; 2.65 A; D=1-300. DR PDB; 2P9N; X-ray; 2.85 A; D=1-300. DR PDB; 2P9P; X-ray; 2.90 A; D=1-300. DR PDB; 2P9S; X-ray; 2.68 A; D=1-300. DR PDB; 2P9U; X-ray; 2.75 A; D=1-300. DR PDB; 3DXK; X-ray; 2.70 A; D=1-300. DR PDB; 3DXM; X-ray; 2.85 A; D=1-300. DR PDB; 3RSE; X-ray; 2.65 A; D=1-300. DR PDB; 3UKR; X-ray; 2.48 A; D=1-300. DR PDB; 3UKU; X-ray; 2.75 A; D=1-300. DR PDB; 3ULE; X-ray; 2.50 A; D=1-300. DR PDB; 4JD2; X-ray; 3.08 A; D=1-300. DR PDB; 4XEI; X-ray; 3.87 A; D=1-300. DR PDB; 4XF2; X-ray; 5.00 A; D/W=1-300. DR PDB; 6DEC; X-ray; 4.60 A; D/K=1-300. DR PDB; 7JPN; EM; 3.24 A; D=1-300. DR PDB; 7T5Q; EM; 3.40 A; D=1-300. DR PDB; 7TPT; EM; 3.90 A; D=1-300. DR PDB; 8TAH; EM; 2.89 A; D=1-300. DR PDBsum; 1K8K; -. DR PDBsum; 1TYQ; -. DR PDBsum; 1U2V; -. DR PDBsum; 2P9I; -. DR PDBsum; 2P9K; -. DR PDBsum; 2P9L; -. DR PDBsum; 2P9N; -. DR PDBsum; 2P9P; -. DR PDBsum; 2P9S; -. DR PDBsum; 2P9U; -. DR PDBsum; 3DXK; -. DR PDBsum; 3DXM; -. DR PDBsum; 3RSE; -. DR PDBsum; 3UKR; -. DR PDBsum; 3UKU; -. DR PDBsum; 3ULE; -. DR PDBsum; 4JD2; -. DR PDBsum; 4XEI; -. DR PDBsum; 4XF2; -. DR PDBsum; 6DEC; -. DR PDBsum; 7JPN; -. DR PDBsum; 7T5Q; -. DR PDBsum; 7TPT; -. DR PDBsum; 8TAH; -. DR AlphaFoldDB; Q3MHR7; -. DR EMDB; EMD-25707; -. DR EMDB; EMD-41135; -. DR SMR; Q3MHR7; -. DR BioGRID; 197405; 2. DR DIP; DIP-29792N; -. DR IntAct; Q3MHR7; 4. DR STRING; 9913.ENSBTAP00000069123; -. DR PaxDb; 9913-ENSBTAP00000013707; -. DR PeptideAtlas; Q3MHR7; -. DR Ensembl; ENSBTAT00000013707.3; ENSBTAP00000013707.2; ENSBTAG00000010386.3. DR Ensembl; ENSBTAT00000070600.1; ENSBTAP00000069123.1; ENSBTAG00000010386.3. DR GeneID; 540838; -. DR KEGG; bta:540838; -. DR CTD; 10109; -. DR VEuPathDB; HostDB:ENSBTAG00000010386; -. DR VGNC; VGNC:55326; ARPC2. DR eggNOG; KOG2826; Eukaryota. DR GeneTree; ENSGT00390000016794; -. DR HOGENOM; CLU_059439_2_0_1; -. DR InParanoid; Q3MHR7; -. DR OMA; FRSYFHY; -. DR OrthoDB; 1275887at2759; -. DR TreeFam; TF315006; -. DR Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-BTA-3928662; EPHB-mediated forward signaling. DR Reactome; R-BTA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-BTA-8856828; Clathrin-mediated endocytosis. DR EvolutionaryTrace; Q3MHR7; -. DR Proteomes; UP000009136; Chromosome 2. DR Bgee; ENSBTAG00000010386; Expressed in blood and 104 other cell types or tissues. DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0030041; P:actin filament polymerization; IEA:InterPro. DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central. DR Gene3D; 3.30.1460.20; -; 2. DR InterPro; IPR007188; ARPC2. DR InterPro; IPR034666; ARPC2/4. DR PANTHER; PTHR12058:SF0; ACTIN-RELATED PROTEIN 2_3 COMPLEX SUBUNIT 2; 1. DR PANTHER; PTHR12058; ARP2/3 COMPLEX 34 KDA SUBUNIT; 1. DR Pfam; PF04045; P34-Arc; 1. DR SUPFAM; SSF69645; Arp2/3 complex subunits; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm; KW Cytoskeleton; Nucleus; Reference proteome; Synapse; Synaptosome. FT CHAIN 1..300 FT /note="Actin-related protein 2/3 complex subunit 2" FT /id="PRO_0000246170" FT MOD_RES 275 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:O15144" FT MOD_RES 295 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:O15144" FT HELIX 9..24 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 32..37 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 38..40 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 64..68 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 69..71 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 72..80 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 92..98 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 106..114 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 116..134 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 142..147 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 150..156 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 161..168 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 172..186 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:1U2V" FT STRAND 197..204 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 207..209 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 210..213 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 220..227 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 229..232 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 234..236 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 237..244 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 247..278 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:8TAH" SQ SEQUENCE 300 AA; 34349 MW; 60801D999BFBF947 CRC64; MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS LKFYKELQAH GADELLKRVY GSYLVNPESG YNVSLLYDLE NLPASKDSIV HQAGMLKRNC FASVFEKYFQ FQEEGKEGEN RAVIHYRDDE TMYVESKKDR VTVVFSTVFK DDDDVVIGKV FMQEFKEGRR ASHTAPQVLF SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNASARDNT INLIHTFRDY LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFSSR //