ID   ARP8_AEDAE              Reviewed;         562 AA.
AC   Q0IEG8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Actin-related protein 8;
GN   Name=Arp8 {ECO:0000250|UniProtKB:Q9VX09}; ORFNames=AAEL010762;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1] {ECO:0000312|EMBL:EAT37227.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
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; CH477691; EAT37227.1; -; Genomic_DNA.
DR   RefSeq; XP_001654858.1; XM_001654808.1.
DR   AlphaFoldDB; Q0IEG8; -.
DR   SMR; Q0IEG8; -.
DR   STRING; 7159.AAEL010762-PA; -.
DR   GeneID; 5573829; -.
DR   KEGG; aag:5573829; -.
DR   VEuPathDB; VectorBase:AAEL010762; -.
DR   eggNOG; KOG0797; Eukaryota.
DR   HOGENOM; CLU_006974_1_0_1; -.
DR   InParanoid; Q0IEG8; -.
DR   OMA; CFIQESL; -.
DR   OrthoDB; 1258783at2759; -.
DR   PhylomeDB; Q0IEG8; -.
DR   Proteomes; UP000008820; Chromosome 3.
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; 1.
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..562
FT                   /note="Actin-related protein 8"
FT                   /id="PRO_0000307119"
FT   BINDING         248..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   562 AA;  63400 MW;  0CF901229F961591 CRC64;
     MSNNKETPEH LQAQNIIVIH PGSLYLRMGR ASDVNPCRLL HAIGRRRKPG GRAYRDRVLS
     VPIAKPKESL SEFEECRLQV SHTLQSCVQS DGRRRYATPP QQISAFNRRS GAETVQASRV
     DWKDDLPGDK VFGEEVLWLN PAGEFNVHYP IRRGELNLHK DVGGSMSGVM CDLQDIWEYV
     LRHRLRIDLK QLKQYKAVLV ISDIYNRAHL KELTSLLLNK IGFGCCFLVQ DHVSATFGAG
     LGYACVVDVG DQKTSISCVE DGISHPNTRV RLPYGGADIT QTFHWMLQKC SFPYKECDQS
     RPQDAFLLKQ LKEDICHVNL DVCGAQEKTF AVHQPQQEKR RFTLQIGDEA IVAPLGLFHT
     ELLSVTGVNK STPMTQKPSR AQPHPEDCFD AEYLRETGRR GKENLEQTAN ESGMANAENA
     DEDMVVEGLE QDREGKVNEK DFILPGGQMI GIDQAVLQSI ERCPNDELKR KMYGCILVVG
     GGMKFTGISN WLQNRVALKI PLMYRSEHNI VTSSKDIDAE ITAWKGAAIM SCLESAAELW
     LTEAEWTRYG LRILREKAVF MW