ARP2A_XENLA
ID ARP2A_XENLA Reviewed; 394 AA.
AC Q7ZTP2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Actin-related protein 2-A;
DE AltName: Full=Actin-like protein 2-A;
GN Name=actr2-a; Synonyms=arp2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17178911; DOI=10.1083/jcb.200604176;
RA Miyoshi T., Tsuji T., Higashida C., Hertzog M., Fujita A., Narumiya S.,
RA Scita G., Watanabe N.;
RT "Actin turnover-dependent fast dissociation of capping protein in the
RT dendritic nucleation actin network: evidence of frequent filament
RT severing.";
RL J. Cell Biol. 175:947-955(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE ARP2/3 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29925947; DOI=10.1038/s41586-018-0237-5;
RA Schrank B.R., Aparicio T., Li Y., Chang W., Chait B.T., Gundersen G.G.,
RA Gottesman M.E., Gautier J.;
RT "Nuclear ARP2/3 drives DNA break clustering for homology-directed repair.";
RL Nature 559:61-66(2018).
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) (PubMed:17178911). The Arp2/3 complex
CC mediates the formation of branched actin networks in the cytoplasm,
CC providing the force for cell motility (PubMed:17178911). Seems to
CC contact the pointed end of the daughter actin filament
CC (PubMed:17178911). In addition to its role in the cytoplasmic
CC cytoskeleton, the Arp2/3 complex also promotes actin polymerization in
CC the nucleus, thereby regulating gene transcription and repair of
CC damaged DNA (Probable). The Arp2/3 complex promotes homologous
CC recombination (HR) repair in response to DNA damage by promoting
CC nuclear actin polymerization, leading to drive motility of double-
CC strand breaks (DSBs) (By similarity). {ECO:0000250|UniProtKB:P61160,
CC ECO:0000269|PubMed:17178911, ECO:0000305|PubMed:29925947}.
CC -!- SUBUNIT: Component of the Arp2/3 complex composed of actr2/arp2,
CC actr3/arp3, arpc1 (arpc1a or arpc1b), arpc2, arpc3, arpc4 and arpc5.
CC {ECO:0000269|PubMed:29925947}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17178911}. Cell projection
CC {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000269|PubMed:29925947}.
CC -!- SIMILARITY: Belongs to the actin family. ARP2 subfamily. {ECO:0000305}.
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DR EMBL; EF011865; ABL63898.1; -; mRNA.
DR EMBL; BC043992; AAH43992.1; -; mRNA.
DR RefSeq; NP_001089193.1; NM_001095724.1.
DR AlphaFoldDB; Q7ZTP2; -.
DR SMR; Q7ZTP2; -.
DR BioGRID; 592020; 1.
DR MaxQB; Q7ZTP2; -.
DR DNASU; 734239; -.
DR GeneID; 734239; -.
DR KEGG; xla:734239; -.
DR CTD; 734239; -.
DR OMA; WDDMKYL; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 734239; Expressed in spleen and 19 other tissues.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA: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; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA: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: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 Actin-binding; ATP-binding; Cell projection; Cytoplasm; Cytoskeleton;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..394
FT /note="Actin-related protein 2-A"
FT /id="PRO_0000327249"
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"
SQ SEQUENCE 394 AA; 44662 MW; FCE09E4BD8218EFD CRC64;
MDSQGKKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPV IRSTAKVGNI EIKDLMVGDE
ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI DTRDCKILLT EPPMNPTKNR
EKIVEVMFET YQFSGVYVAI QAVLTLYAQG LLTGVVVDSG DGVTHICPVY EGFSLPHLTR
RLDIAGRDIT RYLIKLLLLR GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL
VESYTLPDGR VIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRAEFYKH
IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR KHMVFLGGAV
LADIMKDKDN FWMTRQEYQE KGTRVLEKLG VTVR