ARPC4_XENLA
ID ARPC4_XENLA Reviewed; 168 AA.
AC Q641G7; A0A1L8GHV5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Actin-related protein 2/3 complex subunit 4;
GN Name=arpc4 {ECO:0000312|Xenbase:XB-GENE-865976};
GN ORFNames=XELAEV_18025964mg {ECO:0000312|EMBL:OCT83422.1};
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) 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: Actin-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). In addition to
CC its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also
CC promotes actin polymerization in the nucleus, thereby regulating gene
CC transcription and repair of damaged DNA (Probable). The Arp2/3 complex
CC promotes homologous recombination (HR) repair in response to DNA damage
CC by promoting nuclear actin polymerization, leading to drive motility of
CC double-strand breaks (DSBs) (By similarity).
CC {ECO:0000250|UniProtKB:P59998, 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 ARPC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=OCT83422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF011870; ABL63903.1; -; mRNA.
DR EMBL; CM004473; OCT83422.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC082370; AAH82370.1; -; mRNA.
DR RefSeq; NP_001087956.1; NM_001094487.1.
DR RefSeq; XP_018114645.1; XM_018259156.1.
DR AlphaFoldDB; Q641G7; -.
DR SMR; Q641G7; -.
DR IntAct; Q641G7; 1.
DR MINT; Q641G7; -.
DR STRING; 8355.Q641G7; -.
DR MaxQB; Q641G7; -.
DR DNASU; 494639; -.
DR GeneID; 108714705; -.
DR GeneID; 494639; -.
DR KEGG; xla:108714705; -.
DR KEGG; xla:494639; -.
DR CTD; 494639; -.
DR Xenbase; XB-GENE-865976; arpc4.S.
DR OrthoDB; 1351067at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 108714705; 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:0030041; P:actin filament polymerization; IEA:InterPro.
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; 3.30.1460.20; -; 1.
DR InterPro; IPR034666; ARPC2/4.
DR InterPro; IPR008384; ARPC4.
DR PANTHER; PTHR22629; PTHR22629; 1.
DR Pfam; PF05856; ARPC4; 1.
DR PIRSF; PIRSF039100; ARPC4; 1.
DR SUPFAM; SSF69645; SSF69645; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..168
FT /note="Actin-related protein 2/3 complex subunit 4"
FT /id="PRO_0000445563"
SQ SEQUENCE 168 AA; 19692 MW; 719BC7D31BA73A7D CRC64;
MTATLRPYLN AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP VVISRNEKEK
VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN FFILRRKPVE GYDISFLITN
FHTEQMYKHK LVDFVIHFME EIDKEISEMK LSVNARARIV AEEFLKNF