ACT5_DROME
ID ACT5_DROME Reviewed; 376 AA.
AC P10981; A4V2T6; Q5U0U0; Q8MZ23; Q9VFU9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Actin-87E;
DE Flags: Precursor;
GN Name=Act87E; ORFNames=CG18290;
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]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=2840338; DOI=10.1093/genetics/119.2.407;
RA Manseau L.J., Ganetzky B., Craig E.A.;
RT "Molecular and genetic characterization of the Drosophila melanogaster 87E
RT actin gene region.";
RL Genetics 119:407-420(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.;
RL Submitted (DEC-1987) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION IN THE TIP60 COMPLEX, AND FUNCTION.
RX PubMed=15528408; DOI=10.1126/science.1103455;
RA Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
RA Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
RT "Acetylation by Tip60 is required for selective histone variant exchange at
RT DNA lesions.";
RL Science 306:2084-2087(2004).
RN [8]
RP OXIDATION AT MET-45 AND MET-48.
RX PubMed=22116028; DOI=10.1126/science.1211956;
RA Hung R.J., Pak C.W., Terman J.R.;
RT "Direct redox regulation of F-actin assembly and disassembly by Mical.";
RL Science 334:1710-1713(2011).
RN [9]
RP METHYLATION AT HIS-74.
RX PubMed=30526847; DOI=10.7554/elife.37921;
RA Kwiatkowski S., Seliga A.K., Vertommen D., Terreri M., Ishikawa T.,
RA Grabowska I., Tiebe M., Teleman A.A., Jagielski A.K., Veiga-da-Cunha M.,
RA Drozak J.;
RT "SETD3 protein is the actin-specific histidine N-methyltransferase.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility and are ubiquitously expressed in all
CC eukaryotic cells. {ECO:0000269|PubMed:15528408}.
CC -!- FUNCTION: Multiple isoforms are involved in various cellular functions
CC such as cytoskeleton structure, cell mobility, chromosome movement and
CC muscle contraction. {ECO:0000269|PubMed:15528408}.
CC -!- SUBUNIT: Component of the Tip60 chromatin-remodeling complex which
CC contains the catalytic subunit Tip60 and the subunits Domino, Tra1,
CC Brd8, E(Pc), DMAP1, Pontin, Reptin, Ing3, Act87E, BAP55, Mrg15, MrgBP,
CC Gas41 and YL-1. {ECO:0000269|PubMed:15528408}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide promotes
CC actin filament depolymerization. Methionine sulfoxide is produced
CC stereospecifically, but it is not known whether the (S)-S-oxide or the
CC (R)-S-oxide is produced. {ECO:0000269|PubMed:22116028}.
CC -!- MISCELLANEOUS: In Drosophila there are 6 closely related actin genes.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29410.1; Type=Erroneous translation; Evidence={ECO:0000305};
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DR EMBL; X12452; CAA30982.1; -; Genomic_DNA.
DR EMBL; K00674; AAA28320.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54950.2; -; Genomic_DNA.
DR EMBL; AE014297; AAN13567.1; -; Genomic_DNA.
DR EMBL; AY089587; AAL90325.1; -; mRNA.
DR EMBL; AY113405; AAM29410.1; ALT_SEQ; mRNA.
DR EMBL; BT016152; AAV37037.1; -; mRNA.
DR PIR; S04538; S04538.
DR RefSeq; NP_001287314.1; NM_001300385.1.
DR RefSeq; NP_477091.1; NM_057743.5.
DR RefSeq; NP_731812.1; NM_169525.2.
DR AlphaFoldDB; P10981; -.
DR SMR; P10981; -.
DR BioGRID; 71541; 19.
DR DIP; DIP-18091N; -.
DR IntAct; P10981; 9.
DR STRING; 7227.FBpp0082253; -.
DR PaxDb; P10981; -.
DR PRIDE; P10981; -.
DR DNASU; 48632; -.
DR EnsemblMetazoa; FBtr0082785; FBpp0082253; FBgn0000046.
DR EnsemblMetazoa; FBtr0082786; FBpp0082254; FBgn0000046.
DR EnsemblMetazoa; FBtr0346242; FBpp0312019; FBgn0000046.
DR GeneID; 48632; -.
DR KEGG; dme:Dmel_CG18290; -.
DR CTD; 48632; -.
DR FlyBase; FBgn0000046; Act87E.
DR VEuPathDB; VectorBase:FBgn0000046; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000166560; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P10981; -.
DR OMA; NILPICC; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P10981; -.
DR BioGRID-ORCS; 48632; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 48632; -.
DR PRO; PR:P10981; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000046; Expressed in oviduct (Drosophila) and 40 other tissues.
DR ExpressionAtlas; P10981; baseline and differential.
DR Genevisible; P10981; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0043486; P:histone exchange; IDA:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW Nucleotide-binding; Oxidation; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000664"
FT CHAIN 3..376
FT /note="Actin-87E"
FT /id="PRO_0000000665"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:22116028"
FT MOD_RES 48
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:22116028"
FT MOD_RES 74
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|PubMed:30526847"
SQ SEQUENCE 376 AA; 41802 MW; 60252541882B0A7F CRC64;
MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNA PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS
YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANIVM
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPGI VHRKCF
