ID   ARP8_PONAB              Reviewed;         624 AA.
AC   Q5RDA1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Actin-related protein 8;
GN   Name=ACTR8; Synonyms=ARP8;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR858015; CAH90256.1; -; mRNA.
DR   AlphaFoldDB; Q5RDA1; -.
DR   SMR; Q5RDA1; -.
DR   STRING; 9601.ENSPPYP00000015423; -.
DR   eggNOG; KOG0797; Eukaryota.
DR   InParanoid; Q5RDA1; -.
DR   Proteomes; UP000001595; Unplaced.
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; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cell cycle; Cell division; Chromosome;
KW   DNA damage; DNA recombination; DNA repair; Mitosis; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..624
FT                   /note="Actin-related protein 8"
FT                   /id="PRO_0000320538"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         283..286
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H981"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H981"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H981"
SQ   SEQUENCE   624 AA;  70408 MW;  E219DC6CF8BD1787 CRC64;
     MTQAEKGDTE NGKEKGGEKE KEQRGVKRPI VPALVPESLQ EQIQSNFIIV IHPGSTTLRI
     GRATDTLPAS IPHVIARRHK QQGQPLYKDS WLLREGLNKP ESNEQRQNGL KMVDQAIWSK
     KMSNGTRRIP VSPEQARSYN KQMRPAILDH CSGNKWTNTS HHPECLVGEE ALYVNPLDCY
     NIHWPIRRGQ LNIHPGPGGS LTAVLADIEV IWSHAIQKYL EIPLKDLKYY RCILLIPDIY
     NKQHVKELVN MILMKMGFSG IVVHQESVCA TYGSGLSSTC IVDVGDQKTS VCCVEDGVSH
     RNTRLCLAYG GSDVSRCFYW LMQRAGFPYR ECQLTNKMDC LLLQHLKETF CHLDQDISGL
     QDHEFQIRHP DSPALLYQFR LGDEKLQAPM ALFYPATFGI VGQKMTTLQH RSQGDPEDPH
     DEHYLLATQS KQEQSAKATA DRKSASKPIG FEGDLRGQSS DLPERLHSQE VDLGSAQGDG
     LMAGNDSEEA LTALMSRKTA ISLFEGKALG PDKAILHSID CCSSDDTKKK MYSSILVVGG
     GLMFHKAQEF LQHRILNKMP PSFRRIIENV DVITRPKDMD PRLIAWKGGA VLACLDTTQE
     LWIYQREWQR FGVRMLRERA AFVW