ARPC2_BOVIN
ID ARPC2_BOVIN Reviewed; 300 AA.
AC Q3MHR7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Actin-related protein 2/3 complex subunit 2;
DE AltName: Full=Arp2/3 complex 34 kDa subunit;
DE Short=p34-ARC;
GN Name=ARPC2;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF THE 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 THE ARP2/3 COMPLEX WITH BOUND
RP 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. Seems to contact the mother actin filament. In
CC 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:O15144}.
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 (PubMed:11721045, PubMed:15505213). Interacts with
CC SHANK3; the interaction probably mediates the association of SHANK3
CC with the Arp2/3 complex (By similarity). Interacts with DNAI3; this
CC interaction reduces binding of the Arp2/3 complex to the VCA domain of
CC nucleation promoting factors (By similarity).
CC {ECO:0000250|UniProtKB:P61160, ECO:0000250|UniProtKB:Q9CVB6,
CC ECO:0000269|PubMed:11721045, ECO:0000269|PubMed:15505213}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O15144}. Cell projection
CC {ECO:0000250|UniProtKB:O15144}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:Q9CVB6}. Nucleus {ECO:0000250|UniProtKB:O15144}.
CC -!- SIMILARITY: Belongs to the ARPC2 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; BC105136; AAI05137.1; -; mRNA.
DR RefSeq; NP_001029885.1; NM_001034713.2.
DR PDB; 1K8K; X-ray; 2.00 A; D=1-300.
DR PDB; 1TYQ; X-ray; 2.55 A; D=1-300.
DR PDB; 1U2V; X-ray; 2.55 A; D=1-300.
DR PDB; 2P9I; X-ray; 2.46 A; D=1-300.
DR PDB; 2P9K; X-ray; 2.59 A; D=1-300.
DR PDB; 2P9L; X-ray; 2.65 A; D=1-300.
DR PDB; 2P9N; X-ray; 2.85 A; D=1-300.
DR PDB; 2P9P; X-ray; 2.90 A; D=1-300.
DR PDB; 2P9S; X-ray; 2.68 A; D=1-300.
DR PDB; 2P9U; X-ray; 2.75 A; D=1-300.
DR PDB; 3DXK; X-ray; 2.70 A; D=1-300.
DR PDB; 3DXM; X-ray; 2.85 A; D=1-300.
DR PDB; 3RSE; X-ray; 2.65 A; D=1-300.
DR PDB; 3UKR; X-ray; 2.48 A; D=1-300.
DR PDB; 3UKU; X-ray; 2.75 A; D=1-300.
DR PDB; 3ULE; X-ray; 2.50 A; D=1-300.
DR PDB; 4JD2; X-ray; 3.08 A; D=1-300.
DR PDB; 4XEI; X-ray; 3.87 A; D=1-300.
DR PDB; 4XF2; X-ray; 5.00 A; D/W=1-300.
DR PDB; 6DEC; X-ray; 4.60 A; D/K=1-300.
DR PDB; 7JPN; EM; 3.24 A; D=1-300.
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; Q3MHR7; -.
DR SMR; Q3MHR7; -.
DR BioGRID; 197405; 2.
DR DIP; DIP-29792N; -.
DR IntAct; Q3MHR7; 4.
DR STRING; 9913.ENSBTAP00000013707; -.
DR PaxDb; Q3MHR7; -.
DR PeptideAtlas; Q3MHR7; -.
DR PRIDE; Q3MHR7; -.
DR Ensembl; ENSBTAT00000013707; ENSBTAP00000013707; ENSBTAG00000010386.
DR Ensembl; ENSBTAT00000070600; ENSBTAP00000069123; ENSBTAG00000010386.
DR GeneID; 540838; -.
DR KEGG; bta:540838; -.
DR CTD; 10109; -.
DR VEuPathDB; HostDB:ENSBTAG00000010386; -.
DR VGNC; VGNC:55326; ARPC2.
DR eggNOG; KOG2826; Eukaryota.
DR GeneTree; ENSGT00390000016794; -.
DR HOGENOM; CLU_059439_2_0_1; -.
DR InParanoid; Q3MHR7; -.
DR OMA; GPYIVSP; -.
DR OrthoDB; 1345377at2759; -.
DR TreeFam; TF315006; -.
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; Q3MHR7; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000010386; Expressed in blood and 104 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; 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; -; 2.
DR InterPro; IPR007188; ARPC2.
DR InterPro; IPR034666; ARPC2/4.
DR PANTHER; PTHR12058; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
DR SUPFAM; SSF69645; SSF69645; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Nucleus; Reference proteome; Synapse; Synaptosome.
FT CHAIN 1..300
FT /note="Actin-related protein 2/3 complex subunit 2"
FT /id="PRO_0000246170"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15144"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O15144"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 116..134
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1U2V"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:1K8K"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1K8K"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:1K8K"
FT HELIX 247..278
FT /evidence="ECO:0007829|PDB:1K8K"
SQ SEQUENCE 300 AA; 34349 MW; 60801D999BFBF947 CRC64;
MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG DKTKVMVSIS
LKFYKELQAH GADELLKRVY GSYLVNPESG YNVSLLYDLE NLPASKDSIV HQAGMLKRNC
FASVFEKYFQ FQEEGKEGEN RAVIHYRDDE TMYVESKKDR VTVVFSTVFK DDDDVVIGKV
FMQEFKEGRR ASHTAPQVLF SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNASARDNT
INLIHTFRDY LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFSSR
