ID   ARP8_DANRE              Reviewed;         623 AA.
AC   P59679;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Actin-related protein 8;
GN   Name=actr8; ORFNames=zgc:55313;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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. Required for the recruitment of
CC       INO80 (and probably the INO80 complex) to sites of DNA damage Strongly
CC       prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting
CC       it may act as a nucleosome recognition module within the complex (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC       specifically part of a complex module associated with the DBINO domain
CC       of INO80. Exists as monomers and dimers, but the dimer is most probably
CC       the biologically relevant form required for stable interactions with
CC       histones that exploits the twofold symmetry of the nucleosome core (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC       Note=Specifically localizes to mitotic chromosomes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. ARP8 subfamily. {ECO:0000305}.
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DR   EMBL; BC044364; AAH44364.1; -; mRNA.
DR   RefSeq; NP_001001400.1; NM_001001400.1.
DR   AlphaFoldDB; P59679; -.
DR   SMR; P59679; -.
DR   STRING; 7955.ENSDARP00000088695; -.
DR   PaxDb; P59679; -.
DR   GeneID; 326866; -.
DR   KEGG; dre:326866; -.
DR   CTD; 93973; -.
DR   ZFIN; ZDB-GENE-030131-5065; actr8.
DR   eggNOG; KOG0797; Eukaryota.
DR   InParanoid; P59679; -.
DR   OrthoDB; 1258783at2759; -.
DR   PhylomeDB; P59679; -.
DR   Reactome; R-DRE-5689603; UCH proteinases.
DR   Reactome; R-DRE-5696394; DNA Damage Recognition in GG-NER.
DR   PRO; PR:P59679; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Chromosome; DNA damage;
KW   DNA recombination; DNA repair; Mitosis; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..623
FT                   /note="Actin-related protein 8"
FT                   /id="PRO_0000089125"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         283..286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   623 AA;  70133 MW;  BEBD7B3663E507B7 CRC64;
     MTQTDRDAEN GRDREKDREK EQQRGVKRPI MPAAVPEPVQ EQIQANFIVV IHPGSRTLRL
     GRATDTLPIS VPHVIARRHK HPGQSRYEDK CLLREGLNSA DSNEQRQNGL KMVDQVIWSK
     KMSNGVRRTP VSAEQARLYN RQIRPAVLDP NSKVSWTNTS HHPEYVVGEE ALYVNPTDCY
     SVHWPVCRGR LNLHSGSGGS LSAVMMDLEH IWTHALQKLL QIPLKDLKYY RCILLIPDIY
     NRQHVKEIVN MLLVKMGFSA VVVHQESVCA TFGSGLSSAC VVDVGDQKTS VCCVEDGVSH
     RSSRLCLAYG GSDVTRCFFW LMQRAGFPYR DCQLGNKLDC VLLQQLKESF CHLDQDISGL
     QDHEFRTRFP DSPVLLYQLR LGDEKLQAPM TLFYPAAFGI VGQRMTSLLH RSQGDAEDPH
     DEHFLLTTQS KQDQSSKASA DRKSFPKPSS FEGESSVCEV SDRSSLGQDL DLGHSQAECL
     VGGAETEETP SALLSRKTAM SQFEGKALGI DKAILHSIDS CASDETKRKM YSCILVVGGG
     LLFHGAQEFL QHRILNKMPP SFRCMVESVD VITRPKDTDA RVCVWKGGSV LACLDTTQEL
     WIHQREWQRF GVRMLRERAA FVW