ID ARPC5_BOVIN Reviewed; 151 AA. AC Q3SYX9; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 97. DE RecName: Full=Actin-related protein 2/3 complex subunit 5; DE AltName: Full=Arp2/3 complex 16 kDa subunit; DE Short=p16-ARC; GN Name=ARPC5; 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 (AUG-2005) 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: Component of the Arp2/3 complex, a multiprotein complex that CC mediates actin polymerization upon stimulation by nucleation-promoting CC factor (NPF). The Arp2/3 complex mediates the formation of branched CC actin networks in the cytoplasm, providing the force for cell motility. CC In 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:O15511}. 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:O15511}. Cell projection CC {ECO:0000250|UniProtKB:O15511}. Nucleus {ECO:0000250|UniProtKB:O15511}. CC -!- PTM: Polyubiquitinated by RNF128 with 'Lys-63'-linked chains, leading CC to proteasomal degradation. {ECO:0000250|UniProtKB:O15511}. CC -!- SIMILARITY: Belongs to the ARPC5 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; BC103337; AAI03338.1; -; mRNA. DR RefSeq; NP_001030524.1; NM_001035447.2. DR PDB; 1K8K; X-ray; 2.00 A; G=1-151. DR PDB; 1TYQ; X-ray; 2.55 A; G=1-151. DR PDB; 1U2V; X-ray; 2.55 A; G=1-151. DR PDB; 2P9I; X-ray; 2.46 A; G=1-151. DR PDB; 2P9K; X-ray; 2.59 A; G=1-151. DR PDB; 2P9L; X-ray; 2.65 A; G=1-151. DR PDB; 2P9N; X-ray; 2.85 A; G=1-151. DR PDB; 2P9P; X-ray; 2.90 A; G=1-151. DR PDB; 2P9S; X-ray; 2.68 A; G=1-151. DR PDB; 2P9U; X-ray; 2.75 A; G=1-151. DR PDB; 3DXK; X-ray; 2.70 A; G=1-151. DR PDB; 3DXM; X-ray; 2.85 A; G=1-151. DR PDB; 3RSE; X-ray; 2.65 A; G=1-151. DR PDB; 3UKR; X-ray; 2.48 A; G=1-151. DR PDB; 3UKU; X-ray; 2.75 A; G=1-151. DR PDB; 3ULE; X-ray; 2.50 A; G=1-151. DR PDB; 4JD2; X-ray; 3.08 A; G=1-151. DR PDB; 4XEI; X-ray; 3.87 A; G=1-151. DR PDB; 4XF2; X-ray; 5.00 A; G/Z=1-151. DR PDB; 6DEC; X-ray; 4.60 A; G/O=1-151. DR PDB; 7T5Q; EM; 3.40 A; G=1-151. DR PDB; 7TPT; EM; 3.90 A; G=1-151. 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; 7T5Q; -. DR PDBsum; 7TPT; -. DR AlphaFoldDB; Q3SYX9; -. DR EMDB; EMD-25707; -. DR EMDB; EMD-26063; -. DR SMR; Q3SYX9; -. DR DIP; DIP-29795N; -. DR IntAct; Q3SYX9; 2. DR STRING; 9913.ENSBTAP00000054193; -. DR PaxDb; 9913-ENSBTAP00000054193; -. DR PeptideAtlas; Q3SYX9; -. DR GeneID; 614345; -. DR KEGG; bta:614345; -. DR CTD; 10092; -. DR eggNOG; KOG3380; Eukaryota. DR InParanoid; Q3SYX9; -. DR OrthoDB; 7389at2759; -. DR EvolutionaryTrace; Q3SYX9; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0034314; P:Arp2/3 complex-mediated actin nucleation; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro. DR Gene3D; 1.25.40.190; Actin-related protein 2/3 complex subunit 5; 1. DR InterPro; IPR006789; ARPC5. DR InterPro; IPR036743; ARPC5_sf. DR PANTHER; PTHR12644:SF1; ACTIN-RELATED PROTEIN 2_3 COMPLEX SUBUNIT 5; 1. DR PANTHER; PTHR12644; ARP2/3 COMPLEX 16 KD SUBUNIT P16-ARC; 1. DR Pfam; PF04699; P16-Arc; 1. DR PIRSF; PIRSF039096; p16-ARC; 1. DR SUPFAM; SSF69103; Arp2/3 complex 16 kDa subunit ARPC5; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm; KW Cytoskeleton; Nucleus; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:O15511" FT CHAIN 2..151 FT /note="Actin-related protein 2/3 complex subunit 5" FT /id="PRO_0000246172" FT REGION 21..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..36 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:O15511" FT HELIX 10..12 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 16..19 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:2P9K" FT HELIX 39..47 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 51..58 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:2P9N" FT HELIX 69..85 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 91..96 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 100..114 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 121..145 FT /evidence="ECO:0007829|PDB:1K8K" SQ SEQUENCE 151 AA; 16230 MW; F39FB10DC68E6F79 CRC64; MSKNTVSSAR FRKVDVGEYD ENKFVDEEDG GDGQAGPDEG EVDSCLRQGN MTAALQAALK NPPINTKSQA VKDRAGSIVL KVLISFKAND IEKAVQSLDK NGVDLLMKYI YKGFESPSDN SSAVLLQWHE KALAAGGVGS IVRVLTARKT V //