ARP8_DROPS
ID ARP8_DROPS Reviewed; 608 AA.
AC Q29G73;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Actin-related protein 8;
GN Name=Arp8 {ECO:0000250|UniProtKB:Q9VX09}; ORFNames=GA20628;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Plays an important role in the functional organization of
CC mitotic chromosomes. Exhibits low basal ATPase activity, and unable to
CC polymerize (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. Strongly prefer nucleosomes and
CC H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a
CC nucleosome recognition module within the complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the chromatin remodeling Ino80 complex. Exists as
CC monomers and dimers, but the dimer is most probably the biologically
CC relevant form required for stable interactions with histones that
CC exploits the twofold symmetry of the nucleosome core (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9VX09}.
CC -!- SIMILARITY: Belongs to the actin family. ARP8 subfamily. {ECO:0000305}.
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DR EMBL; CH379064; EAL32237.2; -; Genomic_DNA.
DR AlphaFoldDB; Q29G73; -.
DR SMR; Q29G73; -.
DR STRING; 7237.FBpp0275624; -.
DR eggNOG; KOG0797; Eukaryota.
DR HOGENOM; CLU_006974_1_0_1; -.
DR InParanoid; Q29G73; -.
DR OMA; CFIQESL; -.
DR Proteomes; UP000001819; Genome assembly.
DR GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR027668; Arp8/plant_Arp9.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF13; PTHR11937:SF13; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; Nucleotide-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..608
FT /note="Actin-related protein 8"
FT /id="PRO_0000307120"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 272..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 608 AA; 68556 MW; E021F436202DB540 CRC64;
MQRSRASSTS SGRLQASQQV QPLDAPKIIV IHPGSQHLRI GRACDLNPLT MLHAVAYKRK
HQEGDWPYHD PMLPSLDNIN PAQLQVEFEE QRLIASRILQ NCVIDDKQRL RVATPPQQLA
HFNRKSVAEK IPPPGNLSEE RNRQWLDRDA PVLFDEQILR LSTFDARDYD IHFPIQRGEL
NVHKQKGGSL QCTLQHIERI WSYALEARLK INLRDLRTHS AVLVVNDVYV RRHLREFMTL
LLQRLGFQRC FLVQDSVAST YGAGIGFGCV VDIGAQKTSI ACIEDGISQL NSRVRLQYGG
GDINQVLLML LRKCGFPYRE CSVQDSYVDA RLMDKLKERF CHLNAKVCGA QEKQFHLRKQ
NGQWLRYTLQ VGDEAIMAPL AFFHTELLNI TGKARKAFTQ QPPQEQYDCE DCFDAEYLRE
TGRKNGARAA DPIVAQLLAQ PRPLPPITAD DEELNVVDQD EPSSNGVAVH NTSSPSVGHA
QKHFADTANG VYQYGQGQVM PLDQAVLEAI GRCATNETKR KMYGSILLVG SSVKIPGLAA
WLQSCISQQV QPGTEVNVFT KGMDAGMVAW KGAAIMSVLE SARELWITQV DWSRHGLRLL
RERSPFLW