ID ACT3_DROME Reviewed; 376 AA. AC P53501; Q9W2Q0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-OCT-2024, entry version 189. DE RecName: Full=Actin-57B; DE EC=3.6.4.- {ECO:0000250|UniProtKB:P68137}; DE Flags: Precursor; GN Name=Act57B; ORFNames=CG10067; 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]. RX PubMed=6263481; DOI=10.1016/0092-8674(81)90506-7; RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RT "The actin genes of Drosophila: protein coding regions are highly conserved RT but intron positions are not."; RL Cell 24:107-116(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.; RL Submitted (JUN-1985) 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 SUBCELLULAR LOCATION. RX PubMed=9344535; DOI=10.1006/dbio.1997.8697; RA Rodesch C., Pettus J., Nagoshi R.N.; RT "The Drosophila ovarian tumor gene is required for the organization of RT actin filaments during multiple stages in oogenesis."; RL Dev. Biol. 190:153-164(1997). RN [6] 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 [7] 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. CC -!- FUNCTION: Multiple isoforms are involved in various cellular functions CC such as cytoskeleton structure, cell mobility, chromosome movement and CC muscle contraction. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P68137}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:9344535}. Note=Associated with spectrosomes during CC female cystocyte proliferation and differentiation, but dissociates, or CC becomes undetectable, upon fusome maturation (PubMed:9344535). CC Component of the inner rim of ring canals connecting the cytoplasm of CC nurse cells and oocyte during oogenesis (PubMed:9344535). CC {ECO:0000269|PubMed:9344535}. CC -!- PTM: N-terminal cleavage of acetylated cysteine of immature actin by CC ACTMAP. {ECO:0000250|UniProtKB:P68134}. 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 --------------------------------------------------------------------------- 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 EMBL; K00673; AAA28319.1; -; Genomic_DNA. DR EMBL; K00672; AAA28319.1; JOINED; Genomic_DNA. DR EMBL; AE013599; AAF46640.1; -; Genomic_DNA. DR RefSeq; NP_523800.1; NM_079076.4. DR AlphaFoldDB; P53501; -. DR SMR; P53501; -. DR BioGRID; 63011; 53. DR DIP; DIP-17270N; -. DR IntAct; P53501; 9. DR MINT; P53501; -. DR STRING; 7227.FBpp0071448; -. DR PaxDb; 7227-FBpp0071448; -. DR DNASU; 37368; -. DR EnsemblMetazoa; FBtr0071519; FBpp0071448; FBgn0000044. DR GeneID; 37368; -. DR KEGG; dme:Dmel_CG10067; -. DR AGR; FB:FBgn0000044; -. DR CTD; 37368; -. DR FlyBase; FBgn0000044; Act57B. DR VEuPathDB; VectorBase:FBgn0000044; -. DR eggNOG; KOG0676; Eukaryota. DR GeneTree; ENSGT00940000166560; -. DR HOGENOM; CLU_027965_0_2_1; -. DR InParanoid; P53501; -. DR OMA; WIAKGEY; -. DR OrthoDB; 10at2759; -. DR PhylomeDB; P53501; -. DR Reactome; R-DME-445355; Smooth Muscle Contraction. DR SignaLink; P53501; -. DR BioGRID-ORCS; 37368; 0 hits in 3 CRISPR screens. DR ChiTaRS; Act57B; fly. DR GenomeRNAi; 37368; -. DR PRO; PR:P53501; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0000044; Expressed in seminal fluid secreting gland and 33 other cell types or tissues. DR ExpressionAtlas; P53501; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central. DR GO; GO:0030723; P:ovarian fusome organization; IEP:UniProtKB. DR GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR PANTHER; PTHR11937:SF580; ACTIN, INDIRECT FLIGHT MUSCLE-RELATED; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 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; Hydrolase; Methylation; KW Nucleotide-binding; Oxidation; Reference proteome. FT PROPEP 1..2 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000000660" FT CHAIN 3..376 FT /note="Actin-57B" FT /id="PRO_0000000661" 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; 41835 MW; 88F72F339A2B0DF1 CRC64; MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANIVM SGGTTMYPGI ADRMQKEITS LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK EEYDESGPGI VHRKCF //