ID ARPC4_BOVIN Reviewed; 168 AA. AC Q148J6; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 119. DE RecName: Full=Actin-related protein 2/3 complex subunit 4; DE AltName: Full=Arp2/3 complex 20 kDa subunit; DE Short=p20-ARC; GN Name=ARPC4; 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=Hereford; TISSUE=Basal ganglia; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 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 ARP2/3 COMPLEX WITH BOUND 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. In addition to its role in the cytoplasmic CC cytoskeleton, the Arp2/3 complex also promotes actin polymerization in CC the nucleus, thereby regulating gene transcription and repair of CC damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) CC repair in response to DNA damage by promoting nuclear actin CC polymerization, leading to drive motility of double-strand breaks CC (DSBs). {ECO:0000250|UniProtKB:P59998}. 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. {ECO:0000269|PubMed:11721045, CC ECO:0000269|PubMed:15505213}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P59998}. Cell projection CC {ECO:0000250|UniProtKB:P59998}. Nucleus {ECO:0000250|UniProtKB:P59998}. CC -!- SIMILARITY: Belongs to the ARPC4 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; BC118263; AAI18264.1; -; mRNA. DR RefSeq; NP_001069631.1; NM_001076163.1. DR PDB; 1K8K; X-ray; 2.00 A; F=1-168. DR PDB; 1TYQ; X-ray; 2.55 A; F=1-168. DR PDB; 1U2V; X-ray; 2.55 A; F=1-168. DR PDB; 2P9I; X-ray; 2.46 A; F=1-168. DR PDB; 2P9K; X-ray; 2.59 A; F=1-168. DR PDB; 2P9L; X-ray; 2.65 A; F=1-168. DR PDB; 2P9N; X-ray; 2.85 A; F=1-168. DR PDB; 2P9P; X-ray; 2.90 A; F=1-168. DR PDB; 2P9S; X-ray; 2.68 A; F=1-168. DR PDB; 2P9U; X-ray; 2.75 A; F=1-168. DR PDB; 3DXK; X-ray; 2.70 A; F=1-168. DR PDB; 3DXM; X-ray; 2.85 A; F=1-168. DR PDB; 3RSE; X-ray; 2.65 A; F=1-168. DR PDB; 3UKR; X-ray; 2.48 A; F=1-168. DR PDB; 3UKU; X-ray; 2.75 A; F=1-168. DR PDB; 3ULE; X-ray; 2.50 A; F=1-168. DR PDB; 4JD2; X-ray; 3.08 A; F=1-168. DR PDB; 4XEI; X-ray; 3.87 A; F=1-168. DR PDB; 4XF2; X-ray; 5.00 A; F/Y=1-168. DR PDB; 6DEC; X-ray; 4.60 A; F/N=1-168. DR PDB; 7JPN; EM; 3.24 A; F=1-168. DR PDB; 7T5Q; EM; 3.40 A; F=1-168. DR PDB; 7TPT; EM; 3.90 A; F=1-168. DR PDB; 8TAH; EM; 2.89 A; F=1-168. 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; Q148J6; -. DR EMDB; EMD-22416; -. DR EMDB; EMD-25707; -. DR EMDB; EMD-26063; -. DR EMDB; EMD-41135; -. DR SMR; Q148J6; -. DR DIP; DIP-29794N; -. DR IntAct; Q148J6; 2. DR STRING; 9913.ENSBTAP00000010469; -. DR PaxDb; 9913-ENSBTAP00000010469; -. DR Ensembl; ENSBTAT00000070990.1; ENSBTAP00000064283.1; ENSBTAG00000007964.4. DR GeneID; 539459; -. DR KEGG; bta:539459; -. DR CTD; 10093; -. DR VEuPathDB; HostDB:ENSBTAG00000007964; -. DR eggNOG; KOG1876; Eukaryota. DR GeneTree; ENSGT00390000016233; -. DR HOGENOM; CLU_084855_1_0_1; -. DR InParanoid; Q148J6; -. DR OMA; EAYLGEF; -. DR OrthoDB; 5473259at2759; -. DR TreeFam; TF105621; -. 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; Q148J6; -. DR Proteomes; UP000009136; Chromosome 22. DR Bgee; ENSBTAG00000007964; Expressed in monocyte and 102 other cell types or tissues. DR ExpressionAtlas; Q148J6; baseline and differential. DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB. DR GO; GO:0051015; F:actin filament binding; 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; -; 1. DR InterPro; IPR034666; ARPC2/4. DR InterPro; IPR008384; ARPC4. DR PANTHER; PTHR22629:SF0; ACTIN-RELATED PROTEIN 2_3 COMPLEX SUBUNIT 4; 1. DR PANTHER; PTHR22629; ARP2/3 COMPLEX 20 KD SUBUNIT; 1. DR Pfam; PF05856; ARPC4; 1. DR PIRSF; PIRSF039100; ARPC4; 1. DR SUPFAM; SSF69645; Arp2/3 complex subunits; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm; KW Cytoskeleton; Nucleus; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P59998" FT CHAIN 2..168 FT /note="Actin-related protein 2/3 complex subunit 4" FT /id="PRO_0000269565" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0000250|UniProtKB:P59998" FT HELIX 5..19 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 37..40 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 44..46 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 60..75 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 81..96 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:3UKR" FT STRAND 113..119 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 120..125 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 128..165 FT /evidence="ECO:0007829|PDB:1K8K" SQ SEQUENCE 168 AA; 19667 MW; 273CCB230AC703DF CRC64; MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VTISRNEKEK VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN FFILRRKPVE GYDISFLITN FHTEQMYKHK LVDFVIHFME EIDKEISEMK LSVNARARIV AEEFLKNF //