ARP8_BOVIN
ID ARP8_BOVIN Reviewed; 624 AA.
AC Q1LZF2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Actin-related protein 8;
GN Name=ACTR8; Synonyms=ARP8;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) 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; BC116036; AAI16037.1; -; mRNA.
DR RefSeq; NP_001069829.1; NM_001076361.1.
DR AlphaFoldDB; Q1LZF2; -.
DR SMR; Q1LZF2; -.
DR STRING; 9913.ENSBTAP00000014847; -.
DR PaxDb; Q1LZF2; -.
DR PRIDE; Q1LZF2; -.
DR Ensembl; ENSBTAT00000014847; ENSBTAP00000014847; ENSBTAG00000011180.
DR GeneID; 615133; -.
DR KEGG; bta:615133; -.
DR CTD; 93973; -.
DR VEuPathDB; HostDB:ENSBTAG00000011180; -.
DR VGNC; VGNC:25589; ACTR8.
DR eggNOG; KOG0797; Eukaryota.
DR GeneTree; ENSGT00390000001763; -.
DR HOGENOM; CLU_006974_1_0_1; -.
DR InParanoid; Q1LZF2; -.
DR OMA; CFIQESL; -.
DR OrthoDB; 1258783at2759; -.
DR TreeFam; TF324575; -.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000011180; Expressed in spermatocyte and 107 other tissues.
DR ExpressionAtlas; Q1LZF2; baseline.
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 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_0000260759"
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; 70485 MW; 5113E2DC0C801CD1 CRC64;
MTQAEKGEAE NGKEKGGEKE KEQRGVKRPI VPALVPESLQ EQIQSNFIVV IHPGSTTLRI
GRATDTLPAS VPHVIARRHK QQGQPLYKDS WLLREGLNKP ESNEQRQNGL KMVDQAIWSK
KMSNGTRRIP VSPEQARSYN KQMRPAILDH CSGNKWTNTS HHPEFLVGEE ALYVNPLDCY
NIHWPIRRGQ LNIHPGPGGS LTAVLADIEV IWSHAIQKYL EIPLKDLKYY RCILLIPDIY
NKQHVKELVN MILMKMGFSG IVVHQESVCA TFGSGLSSTC IVDVGDQKTS VCCVEDGVSH
RNTRLCLAYG GSDVSRCFYW LMQRAGFPYR ECQLTNKMDC LLLQHLKETF CHLDQDISGL
QDHEFQIRHP DSPALLYQFR LGDEKLQAPM ALFYPATFGI VGQKMTTLQH RSQGDPEDPH
DEQYLLATQS KQEQSAKATA DRKSASKPIG FEGDLRGQSS DLPERLHSQE VDLGPSQGDC
LMAGNDSEEA LTALMSRKTA ISLFEGKALG LDKAILHSID CCSSDETKKK MYSSILVVGG
GLMFHKAQEF LQHRILNKMP PSFRRIIENV DVITRPKDMD PRLIAWKGGA VLACLDTTQE
LWIYQREWQR FGVRMLRERA AFVW
