ARP5_DROME
ID ARP5_DROME Reviewed; 648 AA.
AC Q9VEC3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Actin-related protein 5;
GN Name=Arp5 {ECO:0000303|PubMed:16618800}; ORFNames=CG7940;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF55504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF55504.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL39676.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39676.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP IDENTIFICATION IN THE INO80 COMPLEX, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo {ECO:0000269|PubMed:16618800};
RX PubMed=16618800; DOI=10.1101/gad.377406;
RA Klymenko T., Papp B., Fischle W., Koecher T., Schelder M., Fritsch C.,
RA Wild B., Wilm M., Mueller J.;
RT "A Polycomb group protein complex with sequence-specific DNA-binding and
RT selective methyl-lysine-binding activities.";
RL Genes Dev. 20:1110-1122(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471 AND SER-473, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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:0000250}.
CC -!- SUBUNIT: Component of the chromatin remodeling Ino80 complex.
CC {ECO:0000269|PubMed:16618800}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16618800}.
CC -!- SIMILARITY: Belongs to the actin family. ARP5 subfamily. {ECO:0000305}.
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DR EMBL; AE014297; AAF55504.1; -; Genomic_DNA.
DR EMBL; AY069531; AAL39676.1; -; mRNA.
DR RefSeq; NP_001262697.1; NM_001275768.1.
DR RefSeq; NP_650684.1; NM_142427.4.
DR AlphaFoldDB; Q9VEC3; -.
DR BioGRID; 67194; 7.
DR IntAct; Q9VEC3; 4.
DR STRING; 7227.FBpp0082979; -.
DR iPTMnet; Q9VEC3; -.
DR PaxDb; Q9VEC3; -.
DR PRIDE; Q9VEC3; -.
DR DNASU; 42173; -.
DR EnsemblMetazoa; FBtr0083557; FBpp0082979; FBgn0038576.
DR EnsemblMetazoa; FBtr0336468; FBpp0307571; FBgn0038576.
DR GeneID; 42173; -.
DR KEGG; dme:Dmel_CG7940; -.
DR CTD; 42173; -.
DR FlyBase; FBgn0038576; Arp5.
DR VEuPathDB; VectorBase:FBgn0038576; -.
DR eggNOG; KOG0681; Eukaryota.
DR GeneTree; ENSGT00720000108866; -.
DR HOGENOM; CLU_008246_1_0_1; -.
DR InParanoid; Q9VEC3; -.
DR OMA; TNWNHQE; -.
DR OrthoDB; 344271at2759; -.
DR PhylomeDB; Q9VEC3; -.
DR Reactome; R-DME-5689603; UCH proteinases.
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q9VEC3; -.
DR BioGRID-ORCS; 42173; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42173; -.
DR PRO; PR:Q9VEC3; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038576; Expressed in testis and 34 other tissues.
DR ExpressionAtlas; Q9VEC3; baseline and differential.
DR Genevisible; Q9VEC3; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031011; C:Ino80 complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR027664; Arp5.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF16; PTHR11937:SF16; 1.
DR Pfam; PF00022; Actin; 2.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW Coiled coil; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..648
FT /note="Actin-related protein 5"
FT /id="PRO_0000307117"
FT REGION 34..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 277..311
FT /evidence="ECO:0000255"
FT COILED 340..364
FT /evidence="ECO:0000255"
FT COMPBIAS 357..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 473
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 648 AA; 75122 MW; A7C0301D295F9479 CRC64;
MAGKRVLVID NGSYECRVGW SDSKEPDLRF RNVLTKPRKD RKKEAAASEG SASQTTVEQS
AEIQVGNDIT NIEAVRAHLK SPFERNVITN WNHQEQIFDY IFTKMGFDGQ DKIDHPIILT
EALANPNFCR QQMNELLFEC YGIPSVSYGI DALYSWKHHQ QKQKNISDAL IISFGYSTTH
VIPVLDGKLQ LEHVRRLNVG GYHIITYLFR LMQMKYPVHL NAITISRMEK LVHEHCHIAV
DYKEELVQWA QMDYYDEHIM KIQLPYNAVT ATNAMLTAEQ KQEKRRELAH RLLDIKKNRE
QEKLREDEQQ LFVYNKLRQL YEQKKLDKFE RALQQQQIGT LEDLDSLIAT INSRIKRAQE
RAQSGPRPSK QQERLNKMPK PPEGMSQADW LAELQGKREK ILGRKQARQQ QRSEQAKRHT
HAAQERMRII SSLAKNEKRR KANGEEEDDG FGMNDNDWDV YKRINRYNDD SDSDADNEKL
MQFDKILNHY DANTDGNSNV PPQSAAENYQ LHFGVENIRV PEVLFQPSMI GCSEAGLAEL
IAFVLKLFPA AEQQRLVEHV YLTGGCAQFK GLKERLIKEL MEMRPFQSKF AIYESDEPTL
SAWLGACVHA GEPTFGQTLT TRQDHQEHGR EFFREHTASN IFYPTPKD
