ID   ARP2_PONAB              Reviewed;         394 AA.
AC   Q5R4K0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Actin-related protein 2;
DE   AltName: Full=Actin-like protein 2;
GN   Name=ACTR2; Synonyms=ARP2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Interacts with AVIL. {ECO:0000250|UniProtKB:P61160}.
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; CR861247; CAH93316.1; -; mRNA.
DR   RefSeq; NP_001126951.1; NM_001133479.1.
DR   AlphaFoldDB; Q5R4K0; -.
DR   SMR; Q5R4K0; -.
DR   STRING; 9601.ENSPPYP00000013782; -.
DR   GeneID; 100173969; -.
DR   KEGG; pon:100173969; -.
DR   CTD; 10097; -.
DR   eggNOG; KOG0677; Eukaryota.
DR   InParanoid; Q5R4K0; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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: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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; ATP-binding; Cell projection; Cytoplasm;
KW   Cytoskeleton; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..394
FT                   /note="Actin-related protein 2"
FT                   /id="PRO_0000089069"
FT   BINDING         160..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A7MB62"
FT   BINDING         214..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A7MB62"
FT   BINDING         305..310
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:A7MB62"
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"
SQ   SEQUENCE   394 AA;  44819 MW;  8837A9680C138B76 CRC64;
     MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI EIKDLMVGDE
     ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRNCKILLT EPPMNPTKNR
     EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EDFSLPHLTR
     RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL
     VESYTLPDGR IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH
     IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV
     LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR