ARPC3_BOVIN
ID ARPC3_BOVIN Reviewed; 178 AA.
AC Q3T035;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Actin-related protein 2/3 complex subunit 3;
DE AltName: Full=Arp2/3 complex 21 kDa subunit;
DE Short=p21-ARC;
GN Name=ARPC3;
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=Liver;
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:O15145}.
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:O15145}. Cell projection
CC {ECO:0000250|UniProtKB:O15145}. Nucleus {ECO:0000250|UniProtKB:O15145}.
CC -!- SIMILARITY: Belongs to the ARPC3 family. {ECO:0000305}.
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DR EMBL; BC102590; AAI02591.1; -; mRNA.
DR RefSeq; NP_001029443.1; NM_001034271.2.
DR PDB; 1K8K; X-ray; 2.00 A; E=1-178.
DR PDB; 1TYQ; X-ray; 2.55 A; E=1-178.
DR PDB; 1U2V; X-ray; 2.55 A; E=1-178.
DR PDB; 2P9I; X-ray; 2.46 A; E=1-178.
DR PDB; 2P9K; X-ray; 2.59 A; E=1-178.
DR PDB; 2P9L; X-ray; 2.65 A; E=1-178.
DR PDB; 2P9N; X-ray; 2.85 A; E=1-178.
DR PDB; 2P9P; X-ray; 2.90 A; E=1-178.
DR PDB; 2P9S; X-ray; 2.68 A; E=1-178.
DR PDB; 2P9U; X-ray; 2.75 A; E=1-178.
DR PDB; 3DXK; X-ray; 2.70 A; E=1-178.
DR PDB; 3DXM; X-ray; 2.85 A; E=1-178.
DR PDB; 3RSE; X-ray; 2.65 A; E=1-178.
DR PDB; 3UKR; X-ray; 2.48 A; E=1-178.
DR PDB; 3UKU; X-ray; 2.75 A; E=1-178.
DR PDB; 3ULE; X-ray; 2.50 A; E=1-178.
DR PDB; 4JD2; X-ray; 3.08 A; E=1-178.
DR PDB; 4XEI; X-ray; 3.87 A; E=1-178.
DR PDB; 4XF2; X-ray; 5.00 A; E/X=1-178.
DR PDB; 6DEC; X-ray; 4.60 A; E/L=1-178.
DR PDB; 7JPN; EM; 3.24 A; E=1-178.
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; Q3T035; -.
DR SMR; Q3T035; -.
DR BioGRID; 163240; 2.
DR DIP; DIP-29793N; -.
DR IntAct; Q3T035; 2.
DR STRING; 9913.ENSBTAP00000007028; -.
DR PaxDb; Q3T035; -.
DR PeptideAtlas; Q3T035; -.
DR PRIDE; Q3T035; -.
DR Ensembl; ENSBTAT00000007028; ENSBTAP00000007028; ENSBTAG00000005345.
DR GeneID; 506596; -.
DR KEGG; bta:506596; -.
DR CTD; 10094; -.
DR VEuPathDB; HostDB:ENSBTAG00000005345; -.
DR VGNC; VGNC:53890; ARPC3.
DR eggNOG; KOG3155; Eukaryota.
DR GeneTree; ENSGT00390000018018; -.
DR HOGENOM; CLU_094365_1_0_1; -.
DR InParanoid; Q3T035; -.
DR OMA; TPSKWWL; -.
DR OrthoDB; 1451115at2759; -.
DR TreeFam; TF314598; -.
DR EvolutionaryTrace; Q3T035; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000005345; Expressed in monocyte and 103 other tissues.
DR ExpressionAtlas; Q3T035; 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:0005737; C:cytoplasm; IDA:AgBase.
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:0003779; F:actin binding; IEA:UniProtKB-KW.
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; 1.10.1760.10; -; 1.
DR InterPro; IPR007204; ARPC3.
DR InterPro; IPR036753; ARPC3_sf.
DR PANTHER; PTHR12391; PTHR12391; 1.
DR Pfam; PF04062; P21-Arc; 1.
DR PIRSF; PIRSF016315; ARP2/3_P21-Arc; 1.
DR SUPFAM; SSF69060; SSF69060; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..178
FT /note="Actin-related protein 2/3 complex subunit 3"
FT /id="PRO_0000246171"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15145"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15145"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15145"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O15145"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3RSE"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 63..82
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 112..116
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 123..148
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 162..165
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1K8K"
SQ SEQUENCE 178 AA; 20547 MW; 7149F598B48F0EAC CRC64;
MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK ANVFFKNYEI
KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI TNFPIPGEPG FPLNAIYAKP
ANKQEDEVMR AYLQQLRQET GLRLCEKVFD PQNDKPSKWW TCFVKRQFMN KSLSGPGQ
