ARP2_BOVIN
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 03-AUG-2022, entry version 93.
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}.
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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 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; A7MB62; -.
DR SMR; A7MB62; -.
DR BioGRID; 195053; 3.
DR DIP; DIP-29789N; -.
DR IntAct; A7MB62; 4.
DR STRING; 9913.ENSBTAP00000012872; -.
DR PaxDb; A7MB62; -.
DR PeptideAtlas; A7MB62; -.
DR PRIDE; A7MB62; -.
DR Ensembl; ENSBTAT00000012872; ENSBTAP00000012872; ENSBTAG00000009761.
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; 649708at2759; -.
DR EvolutionaryTrace; A7MB62; -.
DR PRO; PR:A7MB62; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000009761; Expressed in monocyte and 106 other 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 InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 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 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 HELIX 84..93
FT /evidence="ECO:0007829|PDB:2P9I"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:4JD2"
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:4JD2"
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 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 369..374
FT /evidence="ECO:0007829|PDB:4JD2"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:4JD2"
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
