ID   ARP8_DICDI              Reviewed;         873 AA.
AC   Q54JV5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Actin-related protein 8 {ECO:0000250|UniProtKB:Q8R2S9, ECO:0000312|EMBL:EAL63536.1};
GN   Name=arpG {ECO:0000312|EMBL:EAL63536.1};
GN   Synonyms=actr8 {ECO:0000250|UniProtKB:Q8R2S9}; ORFNames=DDB_G0287779;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(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}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q8R2S9, ECO:0000250|UniProtKB:Q9VX09}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP8 subfamily. {ECO:0000255}.
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; AAFI02000104; EAL63536.1; -; Genomic_DNA.
DR   RefSeq; XP_637047.1; XM_631955.1.
DR   AlphaFoldDB; Q54JV5; -.
DR   STRING; 44689.DDB0234011; -.
DR   PaxDb; Q54JV5; -.
DR   EnsemblProtists; EAL63536; EAL63536; DDB_G0287779.
DR   GeneID; 8626301; -.
DR   KEGG; ddi:DDB_G0287779; -.
DR   dictyBase; DDB_G0287779; arpG.
DR   eggNOG; KOG0797; Eukaryota.
DR   HOGENOM; CLU_329136_0_0_1; -.
DR   InParanoid; Q54JV5; -.
DR   OMA; KSHVELF; -.
DR   PRO; PR:Q54JV5; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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; 3.
PE   3: Inferred from homology;
KW   ATP-binding; Chromatin regulator; Coiled coil; Cytoplasm; Cytoskeleton;
KW   DNA damage; DNA recombination; DNA repair; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..873
FT                   /note="Actin-related protein 8"
FT                   /id="PRO_0000370208"
FT   REGION          108..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          762..804
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        108..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         368..371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   873 AA;  98035 MW;  7AC461E9F71BE4BF CRC64;
     MESKVIVIHH GSHSLKIGLA SESVPKTIPN YIARKKKEKI STPTITTTET PTIVSPVEST
     IINNKSNENN DDIMKIDVEN TVTPSEAVGT TTEDVKSTLP MATTITTDEQ VKPTSSTSST
     STTEEVEIKP TESMDIDKPI TDSKTNITSN IKIEQPPPPI NIQTQTKIHI PKKLLEEVEQ
     SVKETTKLLP PVDYIKVRQK PTLYNENNST TFEIIKKKKK KTSSLSSLTN VSTTPPPYVP
     QPLNYNEIDY CIGDDAIAVS RDKDKWFAYQ PITMSTFNTG IYHSVQSMFD DITQMWKYAI
     QRYLNIPSSD LSSYGCVYVV TDNIDRKSLK QITTLLLKEL QFTSVLFFQE SICSSFGVSM
     ATQSCVIDLG HQKISIACVD EGYLLPNTRL TLGYGGEQLT KLLEYLLTGM DKSDSDTLTR
     QMVAKQIHKY YFPFKSSIYE LVDFSPFYLN VFDNIKIENL DYYYNDFQKQ RVGTFKVKDI
     KHDKHMNIYH FNADEVYQVV GMSLFYPNIL SQFGGSSVNY LIKSRSLANT SESNLYVEDQ
     KHYYNHYLSS YDHEDPFDDH SHILSFAQNN TSRDNKDGSN NNNIINNNII NNIINNNNNN
     NNNSSSSSNN NNNNNNSGSN SNINSYNNNN NNNNNNNNNN NNNNNNSFNN VTIVTSTLNS
     NSTVPSTLNS NSTVPSISNS NSTVPSTSTS TTSSPTKKLK IESSSNCEDN YIDIPLDIAI
     LKSVSQLERS DINKKKYLSN ILLVGGGALA PGIQDVLRVC IFKQLEQQYQ AQQLQFQQQL
     QQQQQQQQQL QQQLQNSTNS ATTTPTPSST TIMPLENYIG FANSSIRSDV DCRHAGWRGG
     AILGCLESTR EIWITRSEWQ DGKNSSALNK LPF