ID   ARP3A_XENLA             Reviewed;         418 AA.
AC   Q801P7;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Actin-related protein 3-A {ECO:0000305};
GN   Name=actr3-a {ECO:0000312|Xenbase:XB-GENE-5915333};
GN   ORFNames=XELAEV_18046895mg {ECO:0000312|EMBL:OCT60872.1};
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 {ECO:0000312|EMBL:AAH47983.1};
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2003) 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: 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 (By similarity).
CC       In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3
CC       complex also promotes actin polymerization in the nucleus, thereby
CC       regulating gene transcription and repair of damaged DNA (Probable). The
CC       Arp2/3 complex promotes homologous recombination (HR) repair in
CC       response to DNA damage by promoting nuclear actin polymerization,
CC       leading to drive motility of double-strand breaks (DSBs) (By
CC       similarity). {ECO:0000250|UniProtKB:P61158,
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. ARP3 subfamily. {ECO:0000305}.
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DR   EMBL; EF011871; ABL63904.1; -; mRNA.
DR   EMBL; CM004483; OCT60872.1; -; Genomic_DNA.
DR   EMBL; BC047983; AAH47983.1; -; mRNA.
DR   RefSeq; NP_001080392.1; NM_001086923.1.
DR   AlphaFoldDB; Q801P7; -.
DR   SMR; Q801P7; -.
DR   IntAct; Q801P7; 1.
DR   MINT; Q801P7; -.
DR   STRING; 8355.Q801P7; -.
DR   DNASU; 380084; -.
DR   GeneID; 380084; -.
DR   KEGG; xla:380084; -.
DR   CTD; 380084; -.
DR   Xenbase; XB-GENE-5915333; actr3.S.
DR   OMA; GKYVKQW; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 380084; Expressed in spleen and 20 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IEA:InterPro.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR015623; Arp3.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   PANTHER; PTHR11937:SF175; PTHR11937:SF175; 1.
DR   Pfam; PF00022; Actin; 1.
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..418
FT                   /note="Actin-related protein 3-A"
FT                   /id="PRO_0000445571"
SQ   SEQUENCE   418 AA;  47290 MW;  2F9C7D04EF16B739 CRC64;
     MAARLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR LMKGVDDLDF
     HIGDEAIDKP TYATKWPIRH GIVEDWDLME RFMEQIIFKY LRAEPEDHYF LLTEPPLNTP
     ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV
     AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKEK FSYVCPDLVK
     EFSKYDTDGA KWIKQYMGVN AVSKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
     DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDVK RTVDARLKLS EELSGGRLKP
     KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS