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   25-MAY-2022, entry version 92.
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}.
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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   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   AlphaFoldDB; Q3SYX9; -.
DR   SMR; Q3SYX9; -.
DR   DIP; DIP-29795N; -.
DR   IntAct; Q3SYX9; 2.
DR   STRING; 9913.ENSBTAP00000054193; -.
DR   PaxDb; Q3SYX9; -.
DR   PeptideAtlas; Q3SYX9; -.
DR   PRIDE; Q3SYX9; -.
DR   GeneID; 614345; -.
DR   KEGG; bta:614345; -.
DR   CTD; 10092; -.
DR   eggNOG; KOG3380; Eukaryota.
DR   InParanoid; Q3SYX9; -.
DR   OrthoDB; 1565115at2759; -.
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; -; 1.
DR   InterPro; IPR006789; ARPC5.
DR   InterPro; IPR036743; ARPC5_sf.
DR   PANTHER; PTHR12644; PTHR12644; 1.
DR   Pfam; PF04699; P16-Arc; 1.
DR   PIRSF; PIRSF039096; p16-ARC; 1.
DR   SUPFAM; SSF69103; SSF69103; 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