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 07-JAN-2015, entry version 124. 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; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; 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 RT conserved 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic 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 RT Mical."; RL Science 334:1710-1713(2011). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- FUNCTION: Multiple isoforms are involved in various cellular CC functions such as cytoskeleton structure, cell mobility, CC chromosome movement and muscle contraction. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide CC promotes actin filament depolymerization. Methionine sulfoxide is CC produced stereospecifically, but it is not known whether the (S)- CC S-oxide or the (R)-S-oxide is produced. CC {ECO:0000269|PubMed:22116028}. CC -!- MISCELLANEOUS: In Drosophila there are 6 closely related actin CC 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 UniGene; Dm.36749; -. DR ProteinModelPortal; P53501; -. DR SMR; P53501; 7-376. DR BioGrid; 63011; 31. DR DIP; DIP-17270N; -. DR IntAct; P53501; 2. DR MINT; MINT-909872; -. 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; COG5277; -. DR GeneTree; ENSGT00760000118957; -. DR InParanoid; P53501; -. DR KO; K05692; -. DR OMA; FNINIQF; -. DR OrthoDB; EOG72RMZ1; -. DR PhylomeDB; P53501; -. DR Reactome; REACT_180258; Factors involved in megakaryocyte development and platelet production. DR Reactome; REACT_180852; Translocation of GLUT4 to the plasma membrane. DR Reactome; REACT_181315; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; REACT_208005; Formation of annular gap junctions. DR Reactome; REACT_209888; Adherens junctions interactions. DR Reactome; REACT_236136; Recycling pathway of L1. DR Reactome; REACT_238518; EPHB-mediated forward signaling. DR Reactome; REACT_241000; Gap junction degradation. DR Reactome; REACT_241128; EPH-ephrin mediated repulsion of cells. DR Reactome; REACT_248438; Prefoldin mediated transfer of substrate to CCT/TriC. DR Reactome; REACT_249864; Folding of actin by CCT/TriC. DR Reactome; REACT_252605; VEGFA-VEGFR2 Pathway. DR Reactome; REACT_79920; Interaction between L1 and Ankyrins. DR SignaLink; P53501; -. DR ChiTaRS; Act57B; fly. DR GenomeRNAi; 37368; -. DR NextBio; 803303; -. DR Proteomes; UP000000803; Chromosome 2R. DR Bgee; P53501; -. DR GO; GO:0005884; C:actin filament; ISS:FlyBase. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:FlyBase. DR GO; GO:0051297; P:centrosome organization; IMP:FlyBase. DR GO; GO:0007010; P:cytoskeleton organization; ISS:FlyBase. DR GO; GO:0007507; P:heart development; NAS:FlyBase. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase. DR GO; GO:0051533; P:positive regulation of NFAT protein import into nucleus; 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; Complete proteome; Cytoplasm; Cytoskeleton; KW Nucleotide-binding; Oxidation; Reference proteome. FT PROPEP 1 2 Removed in mature form. {ECO:0000250}. FT /FTId=PRO_0000000660. FT CHAIN 3 376 Actin-57B. FT /FTId=PRO_0000000661. FT MOD_RES 3 3 N-acetylaspartate. {ECO:0000250}. FT MOD_RES 45 45 Methionine sulfoxide. FT {ECO:0000269|PubMed:22116028}. FT MOD_RES 48 48 Methionine sulfoxide. FT {ECO:0000269|PubMed:22116028}. 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 //