AR1AB_XENLA
ID AR1AB_XENLA Reviewed; 370 AA.
AC A0A1L8EXB5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Actin-related protein 2/3 complex subunit 1A-B {ECO:0000305};
GN Name=arpc1a-b; ORFNames=XELAEV_18045070mg {ECO:0000312|EMBL:OCT63973.1};
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 [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).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q8AVT9, ECO:0000250|UniProtKB:Q92747}.
CC -!- SUBUNIT: Component of the Arp2/3 complex.
CC {ECO:0000250|UniProtKB:Q8AVT9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q92747}. Nucleus {ECO:0000250|UniProtKB:Q8AVT9}.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM004482; OCT63973.1; -; Genomic_DNA.
DR RefSeq; XP_018091747.1; XM_018236258.1.
DR RefSeq; XP_018091748.1; XM_018236259.1.
DR AlphaFoldDB; A0A1L8EXB5; -.
DR SMR; A0A1L8EXB5; -.
DR STRING; 8355.A0A1L8EXB5; -.
DR GeneID; 108701505; -.
DR KEGG; xla:108701505; -.
DR CTD; 108701505; -.
DR OMA; YVWEPSP; -.
DR OrthoDB; 848569at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 108701505; Expressed in zone of skin and 19 other tissues.
DR GO; GO:0005885; C:Arp2/3 protein complex; ISS:UniProtKB.
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: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 3: Inferred from homology;
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-B"
FT /id="PRO_0000445568"
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; 41622 MW; 1A3C508A8F956114 CRC64;
MSLHQFLLEP ITCHAWNKDL TQIAISPNNH EVHIYKNSGN QWVKCHELKE HNGHITGIDW
APKSDRIVTC GADRNAYVWS QKDGVWKPTL VILRINRAAT FVKWSPLENK FAVGSGARLI
SVCYFESEND WWVSKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKTRVFS AYIKEVDEKP
ASTPWGSKMP FGQMMAEFGG VSSGGWVHSV SFSASGNKLA WVSHDSTVSV ADASKNMSVS
QLKTEFLPLL SVIFVSENSL IAAGHDCCPM LFTYDEQGSL TFVSKLDIPK QSTQRNISAM
ERFRNMDKRA TTEDRNTTLE TLHQNSITQV SIYDGDKTDC RKFCTTGIDG AMTIWDFKTL
ESYIQGLRIM