AR1BA_XENLA
ID AR1BA_XENLA Reviewed; 369 AA.
AC Q7ZXD5; A1DPL3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Actin-related protein 2/3 complex subunit 1B-A {ECO:0000305};
GN Name=arpc1b-a; ORFNames=XELAEV_18045069mg {ECO:0000312|EMBL:OCT63972.1};
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 (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that
CC mediates actin polymerization upon stimulation by nucleation-promoting
CC factor (NPF) (PubMed:17178911). The Arp2/3 complex mediates the
CC formation of branched actin networks in the cytoplasm, providing the
CC force for cell motility (PubMed:17178911). In addition to its role in
CC the 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). The Arp2/3 complex promotes
CC homologous recombination (HR) repair in response to DNA damage by
CC promoting nuclear actin polymerization, leading to drive motility of
CC double-strand breaks (DSBs) (By similarity).
CC {ECO:0000250|UniProtKB:O15143, 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:O15143}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17178911}. Nucleus {ECO:0000250|UniProtKB:O15143}.
CC -!- SIMILARITY: Belongs to the WD repeat ARPC1 family. {ECO:0000305}.
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DR EMBL; EF011872; ABL63905.1; -; mRNA.
DR EMBL; CM004482; OCT63972.1; -; Genomic_DNA.
DR EMBL; BC045043; AAH45043.1; -; mRNA.
DR RefSeq; NP_001080416.1; NM_001086947.1.
DR AlphaFoldDB; Q7ZXD5; -.
DR SMR; Q7ZXD5; -.
DR STRING; 8355.Q7ZXD5; -.
DR DNASU; 380108; -.
DR GeneID; 380108; -.
DR KEGG; xla:380108; -.
DR CTD; 380108; -.
DR Xenbase; XB-GENE-490414; arpc1b.L.
DR OMA; AXQISVL; -.
DR OrthoDB; 848569at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 380108; Expressed in spleen and 19 other tissues.
DR GO; GO:0005885; C:Arp2/3 protein complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR030141; ARC1B.
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:SF10; PTHR10709:SF10; 1.
DR Pfam; PF00400; WD40; 2.
DR PIRSF; PIRSF038093; ARP2/3_su1; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..369
FT /note="Actin-related protein 2/3 complex subunit 1B-A"
FT /id="PRO_0000445569"
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 94..135
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 140..179
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 200..239
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 242..282
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 321..364
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT CONFLICT 229
FT /note="S -> A (in Ref. 1; ABL63905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41444 MW; CB2EA4A41B33B2F8 CRC64;
MAYHSFLLEP ITCHAWNKDA TQIAFCPNSH DVHIYKKDGD KWSKIHELKE HNGHVTGIDW
APESNRIVTC GTDRNAYVWT LKNNVWKPTL VILRINRAAR CVKWSPKENK FAVGSGSRLI
SICYFEQEND WWVCKHIKKP IRSTVLSLDW HPNNVLLAAG SSDFKSRIFS AYIKEVEERP
APTPWGSKMP FGELMFESSS SCGWVHSVCF SHSGDRMAWV SHDSTICISD ATKKMRVTSL
ITDTLPLLCV TFITENSLVA AGHDCFPVLY IYDEAQGTLS FGGKLDIPKQ SSQRGMTARE
RFQNLDKKAS SDTNNITLDS LHKNSISQLS VLSGGKAKCS KFCTTGLDGG MCIWDVKSLE
SAMKDLKIK
