APC5A_XENLA
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 03-AUG-2022, entry version 86.
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}.
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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 Bgee; 447274; Expressed in spleen and 19 other tissues.
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
