ARP8_MOUSE
ID ARP8_MOUSE Reviewed; 624 AA.
AC Q8R2S9; Q9CYC4;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Actin-related protein 8;
GN Name=Actr8; Synonyms=Arp8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=20971067; DOI=10.1016/j.bbrc.2010.10.066;
RA Kashiwaba S., Kitahashi K., Watanabe T., Onoda F., Ohtsu M., Murakami Y.;
RT "The mammalian INO80 complex is recruited to DNA damage sites in an ARP8
RT dependent manner.";
RL Biochem. Biophys. Res. Commun. 402:619-625(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; AK017815; BAB30952.1; -; mRNA.
DR EMBL; BC027281; AAH27281.1; -; mRNA.
DR CCDS; CCDS26891.1; -.
DR RefSeq; NP_081769.2; NM_027493.3.
DR AlphaFoldDB; Q8R2S9; -.
DR SMR; Q8R2S9; -.
DR BioGRID; 207864; 2.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR IntAct; Q8R2S9; 1.
DR MINT; Q8R2S9; -.
DR STRING; 10090.ENSMUSP00000016115; -.
DR iPTMnet; Q8R2S9; -.
DR PhosphoSitePlus; Q8R2S9; -.
DR EPD; Q8R2S9; -.
DR jPOST; Q8R2S9; -.
DR MaxQB; Q8R2S9; -.
DR PaxDb; Q8R2S9; -.
DR PeptideAtlas; Q8R2S9; -.
DR PRIDE; Q8R2S9; -.
DR ProteomicsDB; 265105; -.
DR Antibodypedia; 31436; 53 antibodies from 15 providers.
DR DNASU; 56249; -.
DR Ensembl; ENSMUST00000016115; ENSMUSP00000016115; ENSMUSG00000015971.
DR Ensembl; ENSMUST00000224797; ENSMUSP00000153076; ENSMUSG00000015971.
DR GeneID; 56249; -.
DR KEGG; mmu:56249; -.
DR UCSC; uc007sum.2; mouse.
DR CTD; 93973; -.
DR MGI; MGI:1860775; Actr8.
DR VEuPathDB; HostDB:ENSMUSG00000015971; -.
DR eggNOG; KOG0797; Eukaryota.
DR GeneTree; ENSGT00390000001763; -.
DR HOGENOM; CLU_006974_1_0_1; -.
DR InParanoid; Q8R2S9; -.
DR OMA; CFIQESL; -.
DR OrthoDB; 1258783at2759; -.
DR PhylomeDB; Q8R2S9; -.
DR TreeFam; TF324575; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR BioGRID-ORCS; 56249; 17 hits in 108 CRISPR screens.
DR PRO; PR:Q8R2S9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8R2S9; protein.
DR Bgee; ENSMUSG00000015971; Expressed in embryonic brain and 252 other tissues.
DR ExpressionAtlas; Q8R2S9; baseline and differential.
DR Genevisible; Q8R2S9; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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; ISO:MGI.
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:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
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_0000089124"
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"
FT CONFLICT 127
FT /note="R -> G (in Ref. 1; BAB30952)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 70546 MW; 96B79E1119C50FEA CRC64;
MTQAEKGDAE NGKEKGGEKE KEQRGVKRPI VPALVPESLQ EQIQSNFIVV IHPGSTTLRL
GRATDTLPVS VPHVIARRHK QQGQPLYKDN WLLREGLNKP ESNEQRQNGL KMVDQAIWSK
KMSNGTRRIP VSPEQTRSYN KQMRPAILDH CSGNKWTNTS QQPEYLVGEE ALYVNPLDCY
NIHWPIRRGQ LNIHPGPGGS LTAVLADIEV IWSHAIQKYL EIPLKDLKYY RCILLIPDIY
NKQHVKELVH MILMKMGFAG IVVHQESVCA TFGSGLSSTC VVDVGDQKTS VCCVEDGVSH
RNTRLCLAYG GSDVSRCFYW LMQRAGFPYR ECQLTNKMDC LLLQHLKETF CHLDQDISGL
QDHEFQIRHP DSPALLYQFR LGDEKLQAPM ALFYPATFGI VGQKMTTLQH RSQGDPEDPH
DEHYLLATQS KQEQSAKATA DRKSASKPIG FEGDLRGQSS DLPERLHSQE VDLASSQGDC
LMAGNESEEA LTALMSRKTA ISLFEGKALG LDKAILHSVD CCSSDDTKKK MYSSILVVGG
GLMFHKAQEF LQHRILNKMP PSFRRIIENV DVITRPKDMD PRLIAWKGGA VLACLDTTQE
LWIYQREWQR FGVRMLRERA AFVW
