ID A0A340WCL9_LIPVE Unreviewed; 624 AA.
AC A0A340WCL9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Actin-related protein 8 {ECO:0000256|ARBA:ARBA00021608, ECO:0000256|RuleBase:RU364121};
GN Name=ACTR8 {ECO:0000313|RefSeq:XP_007447293.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007447293.1};
RN [1] {ECO:0000313|RefSeq:XP_007447293.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays an important role in the functional organization of
CC mitotic chromosomes. Exhibits low basal ATPase activity, and unable to
CC polymerize. {ECO:0000256|ARBA:ARBA00025560,
CC ECO:0000256|RuleBase:RU364121}.
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. {ECO:0000256|RuleBase:RU364121}.
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.
CC {ECO:0000256|RuleBase:RU364121}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364121}.
CC Chromosome {ECO:0000256|RuleBase:RU364121}. Note=Specifically localizes
CC to mitotic chromosomes. {ECO:0000256|RuleBase:RU364121}.
CC -!- SIMILARITY: Belongs to the actin family. ARP8 subfamily.
CC {ECO:0000256|ARBA:ARBA00007720, ECO:0000256|RuleBase:RU364121}.
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 RefSeq; XP_007447293.1; XM_007447231.1.
DR AlphaFoldDB; A0A340WCL9; -.
DR STRING; 118797.A0A340WCL9; -.
DR GeneID; 103075496; -.
DR KEGG; lve:103075496; -.
DR CTD; 93973; -.
DR InParanoid; A0A340WCL9; -.
DR OrthoDB; 11729at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 2.30.36.90; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; ACTIN; 1.
DR PANTHER; PTHR11937:SF13; ACTIN-RELATED PROTEIN 8; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364121};
KW DNA damage {ECO:0000256|RuleBase:RU364121};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU364121}; DNA repair {ECO:0000256|RuleBase:RU364121};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364121};
KW Nucleus {ECO:0000256|RuleBase:RU364121};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW Transcription {ECO:0000256|RuleBase:RU364121};
KW Transcription regulation {ECO:0000256|RuleBase:RU364121}.
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..463
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"
SQ SEQUENCE 624 AA; 70527 MW; 856C0B1D381B3F25 CRC64;
MTQAEKGDTE NGKEKGGEKE KEQRGVKRPI VPALVPESLQ EQIQSNFIVV IHPGSTTLRI
GRATDTLPAS IPHVIARRHK QQGQPLYKDN WLLREGLNKP ESNEQRQNGL KMVDQAIWSK
KMSNGTRRIP VSPEQARSYN KQMRPAILDH CSGNKWTNTS HHPEFLVGEE 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 VDLGSSQGDC
LMAGNDSEEA LTALMSRKTA ISLFEGKALG LDKAILHSID CCSSDEAKKK MYSSILVVGG
GLMFHKAQEF LQHRILNKMP PSFRRIIENV DVITRPKDMD PRLIAWKGGA VLACLDTTQE
LWIYQREWQR FGVRMLRERA AFVW
//
