ID APC5A_XENLA Reviewed; 150 AA. AC Q68FI4; DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 25-MAY-2022, entry version 85. DE RecName: Full=Actin-related protein 2/3 complex subunit 5-A {ECO:0000305}; GN Name=arpc5-a; ORFNames=XELAEV_18023257mg {ECO:0000312|EMBL:OCT85093.1}; 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], FUNCTION, AND SUBCELLULAR LOCATION. 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 GENOMIC DNA]. RC STRAIN=J; RX PubMed=27762356; DOI=10.1038/nature19840; RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S., RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I., RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O., RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M., RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I., RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J., RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y., RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J., RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M., RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J., RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.; RT "Genome evolution in the allotetraploid frog Xenopus laevis."; RL Nature 538:336-343(2016). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that CC mediates actin polymerization upon stimulation by nucleation-promoting CC factor (NPF) (PubMed:17178911). The Arp2/3 complex mediates the CC formation of branched actin networks in the cytoplasm, providing the CC force for cell motility (PubMed:17178911). In addition to its role in CC the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin CC polymerization in the nucleus, thereby regulating gene transcription CC and repair of damaged DNA (By similarity). 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) (By similarity). CC {ECO:0000250|UniProtKB:O15511, ECO:0000250|UniProtKB:Q6DE18, CC ECO:0000269|PubMed:17178911}. 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:0000250|UniProtKB:Q6DE18}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:17178911}. Cell projection CC {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000250|UniProtKB:Q6DE18}. CC -!- SIMILARITY: Belongs to the ARPC5 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; EF011868; ABL63901.1; -; mRNA. DR EMBL; CM004472; OCT85093.1; -; Genomic_DNA. DR EMBL; BC079805; AAH79805.1; -; mRNA. DR RefSeq; NP_001087450.1; NM_001093981.1. DR AlphaFoldDB; Q68FI4; -. DR SMR; Q68FI4; -. DR IntAct; Q68FI4; 5. DR MINT; Q68FI4; -. DR STRING; 8355.Q68FI4; -. DR DNASU; 447274; -. DR GeneID; 447274; -. DR KEGG; xla:447274; -. DR CTD; 447274; -. DR Xenbase; XB-GENE-866317; arpc5.L. DR OMA; GMALPGW; -. DR OrthoDB; 1565115at2759; -. DR Proteomes; UP000186698; Chromosome 4L. 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; 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:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro. DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro. DR Gene3D; 1.25.40.190; -; 1. DR InterPro; IPR006789; ARPC5. DR InterPro; IPR036743; ARPC5_sf. DR PANTHER; PTHR12644; PTHR12644; 1. DR Pfam; PF04699; P16-Arc; 1. DR PIRSF; PIRSF039096; p16-ARC; 1. DR SUPFAM; SSF69103; SSF69103; 1. PE 2: Evidence at transcript level; KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; Nucleus; KW Reference proteome. FT CHAIN 1..150 FT /note="Actin-related protein 2/3 complex subunit 5-A" FT /id="PRO_0000445564" FT REGION 21..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..35 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 150 AA; 16400 MW; 686E7C42BBDF5726 CRC64; MAKNTVSARF RKVDVDEYDE NKFVDEEEAG EGQQGPDEGE VDSAIRGGNM MGALQAALKN PPINTKNQSA KDRAENLVLK VLISFKANEI EKAVQSLDKN STDLLMKYIY KGFESPSDNS SAVLLQWHEK ALAVAGVGSI VRVLTARKTV //