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ARC3A_XENLA
ID   ARC3A_XENLA             Reviewed;         178 AA.
AC   A1DPK7;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 3-A;
GN   Name=arpc3-a; ORFNames=XELAEV_18010654mg {ECO:0000312|EMBL:OCT98422.1};
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=Gastrula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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: 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 (Probable). 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:O15145, ECO:0000269|PubMed:17178911,
CC       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 ARPC3 family. {ECO:0000305}.
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DR   EMBL; EF011866; ABL63899.1; -; mRNA.
DR   EMBL; CM004467; OCT98422.1; -; Genomic_DNA.
DR   EMBL; BC169449; AAI69449.1; -; mRNA.
DR   EMBL; BC169453; AAI69453.1; -; mRNA.
DR   RefSeq; NP_001090588.1; NM_001097119.1.
DR   AlphaFoldDB; A1DPK7; -.
DR   SMR; A1DPK7; -.
DR   STRING; 8355.A1DPK7; -.
DR   GeneID; 100036831; -.
DR   KEGG; xla:100036831; -.
DR   OrthoDB; 1451115at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 100036831; 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; IEA:UniProtKB-KW.
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:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   Gene3D; 1.10.1760.10; -; 1.
DR   InterPro; IPR007204; ARPC3.
DR   InterPro; IPR036753; ARPC3_sf.
DR   PANTHER; PTHR12391; PTHR12391; 1.
DR   Pfam; PF04062; P21-Arc; 1.
DR   PIRSF; PIRSF016315; ARP2/3_P21-Arc; 1.
DR   SUPFAM; SSF69060; SSF69060; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..178
FT                   /note="Actin-related protein 2/3 complex subunit 3-A"
FT                   /id="PRO_0000445561"
SQ   SEQUENCE   178 AA;  20656 MW;  39709470B7383F54 CRC64;
     MPAYHSMLME PDTKLIGNMA MLPIRSQFKG PAPRETKDTD IIDEAIYYFK ANVFFKNYEI
     KNEADRTLIY ITLYISECLK KLQKCNSKGQ GEKEMYTLGI TNFPIPGEPG FPLNAMYVKP
     SNKQEDEVMR AYLQQLRQET GLRLCDKVFD PQTDKPSKWW TCFVKRQFMN KSLSAPGQ
 
 
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