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 26-FEB-2020, entry version 169. DE RecName: Full=Actin-57B; DE Flags: Precursor; GN Name=Act57B; ORFNames=CG10067; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; 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 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 [6] 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 -!- 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 --------------------------------------------------------------------------- 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 SMR; P53501; -. DR BioGrid; 63011; 44. DR DIP; DIP-17270N; -. DR IntAct; P53501; 8. DR MINT; P53501; -. DR STRING; 7227.FBpp0071448; -. DR PaxDb; P53501; -. DR PRIDE; P53501; -. DR EnsemblMetazoa; FBtr0071519; FBpp0071448; FBgn0000044. DR GeneID; 37368; -. DR KEGG; dme:Dmel_CG10067; -. DR CTD; 37368; -. DR FlyBase; FBgn0000044; Act57B. DR eggNOG; KOG0676; Eukaryota. DR eggNOG; COG5277; LUCA. DR GeneTree; ENSGT00940000166560; -. DR HOGENOM; CLU_027965_0_2_1; -. DR InParanoid; P53501; -. DR KO; K05692; -. DR OMA; RIRNECT; -. DR OrthoDB; 649708at2759; -. DR PhylomeDB; P53501; -. DR SignaLink; P53501; -. DR ChiTaRS; Act57B; fly. DR GenomeRNAi; 37368; -. DR PRO; PR:P53501; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; FBgn0000044; Expressed in larva and 12 other tissues. DR ExpressionAtlas; P53501; baseline. DR Genevisible; P53501; DM. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase. DR GO; GO:0098529; P:neuromuscular junction development, skeletal muscle fiber; IMP:FlyBase. DR GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR PANTHER; PTHR11937; PTHR11937; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. 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_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 //