AR1AA_XENLA
ID AR1AA_XENLA Reviewed; 370 AA.
AC Q8AVT9;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Actin-related protein 2/3 complex subunit 1A-A {ECO:0000305};
GN Name=arpc1a-a; ORFNames=XELAEV_18047443mg {ECO:0000312|EMBL:OCT61420.1};
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:AAH41267.1};
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP 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: Probably functions as component of the Arp2/3 complex which
CC is involved in regulation of actin polymerization and together with an
CC activating nucleation-promoting factor (NPF) mediates the formation of
CC branched actin networks (By similarity). In addition to its role in the
CC 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). {ECO:0000250|UniProtKB:Q92747,
CC ECO:0000305|PubMed:29925947}.
CC -!- SUBUNIT: Component of the Arp2/3 complex.
CC {ECO:0000269|PubMed:29925947}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q92747}. Nucleus {ECO:0000269|PubMed:29925947}.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; CM004483; OCT61420.1; -; Genomic_DNA.
DR EMBL; BC041267; AAH41267.1; -; mRNA.
DR EMBL; BC106316; AAI06317.1; -; mRNA.
DR RefSeq; NP_001080153.1; NM_001086684.1.
DR AlphaFoldDB; Q8AVT9; -.
DR SMR; Q8AVT9; -.
DR STRING; 8355.Q8AVT9; -.
DR DNASU; 379845; -.
DR GeneID; 379845; -.
DR KEGG; xla:379845; -.
DR CTD; 379845; -.
DR Xenbase; XB-GENE-6254683; arpc1a.S.
DR OMA; GCPTFIS; -.
DR OrthoDB; 848569at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 379845; Expressed in testis and 19 other tissues.
DR GO; GO:0005885; C:Arp2/3 protein complex; IDA:UniProtKB.
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; 2.130.10.10; -; 1.
DR InterPro; IPR030140; ARC1A.
DR InterPro; IPR017383; ARPC1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10709; PTHR10709; 1.
DR PANTHER; PTHR10709:SF11; PTHR10709:SF11; 1.
DR Pfam; PF00400; WD40; 2.
DR PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..370
FT /note="Actin-related protein 2/3 complex subunit 1A-A"
FT /id="PRO_0000445567"
FT REPEAT 6..45
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 50..89
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 140..179
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 202..241
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 244..284
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 322..365
FT /note="WD 6"
FT /evidence="ECO:0000255"
SQ SEQUENCE 370 AA; 41572 MW; 9818692F0366261E CRC64;
MSLHQFLLEP ISCHAWNKDL TQIAISPNNH EVHIYKKSGD QWVKGHELKE HNGHITGIDW
APKSDRIVTC GADRNAYVWS QKDGVWKPTL VILRINRAAT FVKWSPLENK FAVGSGARLI
SVCYFESEND WWVSKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKTRVFS AYIKEVDEKP
ASTPWGSKMP FGQMMAEFGG VSSGGWVHSV SFSASGNKLA WVSHDSTVSV ADASKNMSVS
QLKTEFLPLL SVIFVSENSL IAAGHDCCPM LFTYDEHGSL TFVSKLDIPK QSTQRNISAM
ERFRNMDKRA TTEDRNTTLE TLHQNSITQV SIYDGDKTEC RKFCTTGIDG AMTIWDFKTL
ESYIQGLKIM
