ID ARP2_BOVIN Reviewed; 394 AA. AC A7MB62; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Actin-related protein 2; DE AltName: Full=Actin-like protein 2; GN Name=ACTR2; Synonyms=ARP2; 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=Fetal skin; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (JUL-2007) 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). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF ARP2/3 COMPLEX WITH BOUND ATP. RX PubMed=17499050; DOI=10.1016/j.molcel.2007.04.017; RA Nolen B.J., Pollard T.D.; RT "Insights into the influence of nucleotides on actin family proteins from RT seven structures of Arp2/3 complex."; RL Mol. Cell 26:449-457(2007). CC -!- FUNCTION: ATP-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 pointed end of the CC daughter actin filament. In podocytes, required for the formation of CC lamellipodia downstream of AVIL and PLCE1 regulation. In addition to CC its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also CC promotes actin polymerization in the nucleus, thereby regulating gene CC transcription and repair of damaged DNA. The Arp2/3 complex promotes CC homologous recombination (HR) repair in response to DNA damage by CC promoting nuclear actin polymerization, leading to drive motility of CC double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P61160}. 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, PubMed:17499050). CC Interacts with AVIL (By similarity). {ECO:0000250|UniProtKB:P61160, CC ECO:0000269|PubMed:11721045, ECO:0000269|PubMed:15505213, CC ECO:0000269|PubMed:17499050}. CC -!- INTERACTION: CC A7MB62; Q95107: WASL; NbExp=2; IntAct=EBI-6162748, EBI-6162776; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P61160}. Cell projection CC {ECO:0000250|UniProtKB:P61160}. Nucleus {ECO:0000250|UniProtKB:P61160}. CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {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; BC151356; AAI51357.1; -; mRNA. DR RefSeq; NP_001095683.1; NM_001102213.1. DR PDB; 1K8K; X-ray; 2.00 A; B=1-394. DR PDB; 1TYQ; X-ray; 2.55 A; B=1-394. DR PDB; 1U2V; X-ray; 2.55 A; B=1-394. DR PDB; 2P9I; X-ray; 2.46 A; B=1-394. DR PDB; 2P9K; X-ray; 2.59 A; B=1-394. DR PDB; 2P9L; X-ray; 2.65 A; B=1-394. DR PDB; 2P9N; X-ray; 2.85 A; B=1-394. DR PDB; 2P9P; X-ray; 2.90 A; B=1-394. DR PDB; 2P9S; X-ray; 2.68 A; B=1-394. DR PDB; 2P9U; X-ray; 2.75 A; B=1-394. DR PDB; 3DXK; X-ray; 2.70 A; B=1-394. DR PDB; 3DXM; X-ray; 2.85 A; B=1-394. DR PDB; 3RSE; X-ray; 2.65 A; B=1-394. DR PDB; 3UKR; X-ray; 2.48 A; B=1-394. DR PDB; 3UKU; X-ray; 2.75 A; B=1-394. DR PDB; 3ULE; X-ray; 2.50 A; B=1-394. DR PDB; 4JD2; X-ray; 3.08 A; B=1-394. DR PDB; 4XEI; X-ray; 3.87 A; B=1-394. DR PDB; 4XF2; X-ray; 5.00 A; B/U=1-394. DR PDB; 6DEC; X-ray; 4.60 A; B/I=1-394. DR PDB; 7JPN; EM; 3.24 A; B=4-380. DR PDB; 7T5Q; EM; 3.40 A; B=1-394. DR PDB; 7TPT; EM; 3.90 A; B=1-394. DR PDB; 8TAH; EM; 2.89 A; B=1-394. 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 PDBsum; 7T5Q; -. DR PDBsum; 7TPT; -. DR PDBsum; 8TAH; -. DR AlphaFoldDB; A7MB62; -. DR EMDB; EMD-22416; -. DR EMDB; EMD-25707; -. DR EMDB; EMD-26063; -. DR EMDB; EMD-41135; -. DR SMR; A7MB62; -. DR BioGRID; 195053; 3. DR DIP; DIP-29789N; -. DR IntAct; A7MB62; 4. DR STRING; 9913.ENSBTAP00000062306; -. DR PaxDb; 9913-ENSBTAP00000012872; -. DR PeptideAtlas; A7MB62; -. DR Ensembl; ENSBTAT00000012872.6; ENSBTAP00000012872.6; ENSBTAG00000009761.6. DR GeneID; 538486; -. DR KEGG; bta:538486; -. DR CTD; 10097; -. DR VEuPathDB; HostDB:ENSBTAG00000009761; -. DR VGNC; VGNC:25586; ACTR2. DR eggNOG; KOG0677; Eukaryota. DR GeneTree; ENSGT00940000154556; -. DR InParanoid; A7MB62; -. DR OMA; WEDMQHL; -. DR OrthoDB; 176764at2759; -. DR Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-BTA-3928662; EPHB-mediated forward signaling. DR Reactome; R-BTA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-8856828; Clathrin-mediated endocytosis. DR EvolutionaryTrace; A7MB62; -. DR PRO; PR:A7MB62; -. DR Proteomes; UP000009136; Chromosome 11. DR Bgee; ENSBTAG00000009761; Expressed in monocyte and 106 other cell types or tissues. DR ExpressionAtlas; A7MB62; 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; ISS:UniProtKB. 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:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR PANTHER; PTHR11937:SF37; ACTIN-RELATED PROTEIN 2; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; ATP-binding; Cell projection; KW Cytoplasm; Cytoskeleton; Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..394 FT /note="Actin-related protein 2" FT /id="PRO_0000327246" FT BINDING 160..162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15505213, FT ECO:0000269|PubMed:17499050" FT BINDING 214..218 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15505213, FT ECO:0000269|PubMed:17499050" FT BINDING 305..310 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:15505213, FT ECO:0000269|PubMed:17499050" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P61160" FT MOD_RES 299 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P61160" FT MOD_RES 322 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P61160" FT STRAND 10..13 FT /evidence="ECO:0007829|PDB:2P9I" FT STRAND 15..21 FT /evidence="ECO:0007829|PDB:2P9I" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:2P9I" FT STRAND 36..40 FT /evidence="ECO:0007829|PDB:4JD2" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:7T5Q" FT HELIX 59..63 FT /evidence="ECO:0007829|PDB:4JD2" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:4JD2" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:4JD2" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:4JD2" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:8TAH" FT HELIX 84..93 FT /evidence="ECO:0007829|PDB:2P9I" FT TURN 95..98 FT /evidence="ECO:0007829|PDB:8TAH" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:4JD2" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:2P9I" FT TURN 117..119 FT /evidence="ECO:0007829|PDB:2P9K" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:8TAH" FT HELIX 141..147 FT /evidence="ECO:0007829|PDB:2P9I" FT TURN 148..150 FT /evidence="ECO:0007829|PDB:2P9I" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:7T5Q" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 171..174 FT /evidence="ECO:0007829|PDB:3UKU" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:2P9I" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 186..199 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 206..209 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 210..220 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 227..236 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:2P9P" FT STRAND 242..245 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 251..254 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 257..260 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 278..288 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 291..293 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 294..298 FT /evidence="ECO:0007829|PDB:1K8K" FT STRAND 302..305 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 306..308 FT /evidence="ECO:0007829|PDB:1K8K" FT HELIX 313..328 FT /evidence="ECO:0007829|PDB:1K8K" FT TURN 329..332 FT /evidence="ECO:0007829|PDB:3UKR" FT HELIX 336..339 FT /evidence="ECO:0007829|PDB:2P9I" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:2P9I" FT HELIX 353..361 FT /evidence="ECO:0007829|PDB:2P9I" FT TURN 365..367 FT /evidence="ECO:0007829|PDB:4JD2" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:8TAH" FT HELIX 375..379 FT /evidence="ECO:0007829|PDB:8TAH" FT HELIX 384..387 FT /evidence="ECO:0007829|PDB:8TAH" SQ SEQUENCE 394 AA; 44761 MW; 1BFA6B442ED1A797 CRC64; MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRNCKILLT EPPMNPTKNR EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL VESYTLPDGR IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR //