ID   ARP8_SALSA              Reviewed;         632 AA.
AC   B5X2S3;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Actin-related protein 8;
GN   Name=actr8;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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; BT045342; ACI33604.1; -; mRNA.
DR   RefSeq; NP_001133630.1; NM_001140158.1.
DR   AlphaFoldDB; B5X2S3; -.
DR   SMR; B5X2S3; -.
DR   STRING; 8030.ENSSSAP00000029655; -.
DR   GeneID; 100195129; -.
DR   KEGG; sasa:100195129; -.
DR   CTD; 93973; -.
DR   OrthoDB; 1258783at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa13.
DR   GO; GO:0031011; C:Ino80 complex; IEA:InterPro.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
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   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..632
FT                   /note="Actin-related protein 8"
FT                   /id="PRO_0000403983"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         288..291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   632 AA;  71349 MW;  76351C6098E629AE CRC64;
     MTQAEREQEN GKEKEKEREK EKEKEKEQRG IKRPIAPPVI PEPLQEQIQS NFIVVLHPGS
     KTLRIGRATD TLPATVPHVI ARRHKQTCQT RYEDGWLVRE GLNKPESNEQ RQNGLKMVDQ
     AIWSKKMSNG VRRTPVSAEQ ARSYNRLIRP AGLDTSSRMK WTNTAHHPEH LVGEEALYVN
     PTDCYNVHWP ISRGQLNVHG GVGGSLTAVL ADLEAIWSHV IQKQLEIPLK DLKYYRCILL
     VPDIYNRHHI KELVNMLLLN MGFSAIVVHQ ESVCATFGSG LSSACVVDVG DQKTSLCCVE
     DGVSHRNSRL CLAYGGADVT RCFFWLLQRA GFPYRECQLS NRVDCILLQQ LKETFCHLDQ
     DISGLQDHEF RTRFPESPAL LYQVRLGDEK LQAPMALFYP TTFGIVGQKM TSLQHRSQGD
     PEDPHDEHYL LGTQSKQDQS SKASAERKSL PKPPGFEGEL SSQGGDPSER GGGAHGQDVE
     LGHSQNDCLM GGAEMEEPPS ALLSRKTAMT QFEGKALGLD KAILHSIDCC ASDETKRKMY
     SSILVVGGGL LFHRAQEFLQ HRILNKMPPS FRRVVESVEV ITRPKDMDPR LISWKGGAVL
     ACLDTTQEMW IHQREWQRFG VRMLRERAAF VW