ARC2A_XENLA
ID ARC2A_XENLA Reviewed; 300 AA.
AC Q0IH88;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Actin-related protein 2/3 complex subunit 2-A;
GN Name=arpc2-a; ORFNames=XELAEV_18044424mg {ECO:0000312|EMBL:OCT63327.1};
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-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). The Arp2/3
CC complex promotes homologous recombination (HR) repair in response to
CC DNA damage by promoting nuclear actin polymerization, leading to drive
CC motility of double-strand breaks (DSBs) (By similarity).
CC {ECO:0000250|UniProtKB:O15144, ECO:0000250|UniProtKB:Q6IRB1,
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:Q6IRB1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17178911}. Cell projection
CC {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000250|UniProtKB:Q6IRB1}.
CC -!- SIMILARITY: Belongs to the ARPC2 family. {ECO:0000305}.
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DR EMBL; EF011864; ABL63897.1; -; mRNA.
DR EMBL; CM004482; OCT63327.1; -; Genomic_DNA.
DR EMBL; BC123262; AAI23263.1; -; mRNA.
DR RefSeq; NP_001090493.1; NM_001097024.1.
DR AlphaFoldDB; Q0IH88; -.
DR SMR; Q0IH88; -.
DR IntAct; Q0IH88; 1.
DR MINT; Q0IH88; -.
DR STRING; 8355.Q0IH88; -.
DR MaxQB; Q0IH88; -.
DR DNASU; 779406; -.
DR GeneID; 779406; -.
DR KEGG; xla:779406; -.
DR CTD; 779406; -.
DR Xenbase; XB-GENE-866076; arpc2.L.
DR OMA; GPYIVSP; -.
DR OrthoDB; 1345377at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 779406; Expressed in internal ear 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: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; -; 2.
DR InterPro; IPR007188; ARPC2.
DR InterPro; IPR034666; ARPC2/4.
DR PANTHER; PTHR12058; PTHR12058; 1.
DR Pfam; PF04045; P34-Arc; 1.
DR SUPFAM; SSF69645; SSF69645; 2.
PE 2: Evidence at transcript level;
KW Actin-binding; Cell projection; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..300
FT /note="Actin-related protein 2/3 complex subunit 2-A"
FT /id="PRO_0000445559"
SQ SEQUENCE 300 AA; 34352 MW; 1F855B2C924D6B1B CRC64;
MILLEVNNRI IEEILTLKFE NAAAGNKPEA VEVTFADFDG VLYHVSNPNG DKAKVLISIS
LKFYKELQEH GTDEVLKKVY GNFLVAPESG YNVSLLYDLE SLPSNKDSVI HQAGMLKRNC
FASVFEKYFK FQEEGKDGEK RAVIHYRDDE TMYVEAKKDR VTVVFSTVFK DDDDVVIGKV
FMQEFKEGRR ASHTAPQVLF SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNANARDNT
INLIHTFRDY LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFAAR
