ARPC4_BOVIN
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 03-AUG-2022, entry version 112.
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 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 AlphaFoldDB; Q148J6; -.
DR SMR; Q148J6; -.
DR DIP; DIP-29794N; -.
DR IntAct; Q148J6; 2.
DR STRING; 9913.ENSBTAP00000010469; -.
DR PaxDb; Q148J6; -.
DR PRIDE; Q148J6; -.
DR Ensembl; ENSBTAT00000070990; ENSBTAP00000064283; ENSBTAG00000007964.
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; 1351067at2759; -.
DR TreeFam; TF105621; -.
DR Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-BTA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR EvolutionaryTrace; Q148J6; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000007964; Expressed in monocyte and 102 other 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 GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR Gene3D; 3.30.1460.20; -; 1.
DR InterPro; IPR034666; ARPC2/4.
DR InterPro; IPR008384; ARPC4.
DR PANTHER; PTHR22629; PTHR22629; 1.
DR Pfam; PF05856; ARPC4; 1.
DR PIRSF; PIRSF039100; ARPC4; 1.
DR SUPFAM; SSF69645; SSF69645; 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
