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 03-MAR-2009, entry version 74. DE RecName: Full=Actin-57B; GN Name=Act57B; ORFNames=CG10067; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=81210174; 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 MEDLINE=20196006; 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. RX MEDLINE=22426069; PubMed=12537572; 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). 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 -!- MISCELLANEOUS: In Drosophila there are 6 closely related actin CC genes. CC -!- SIMILARITY: Belongs to the actin family. 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; -. DR UniGene; Dm.2897; -. DR HSSP; P10983; 1D4X. DR SMR; P53501; 5-372. DR DIP; DIP:17270N; -. DR IntAct; P53501; 9. DR Ensembl; CG10067; Drosophila melanogaster. DR GeneID; 37368; -. DR KEGG; dme:Dmel_CG10067; -. DR FlyBase; FBgn0000044; Act57B. DR HOGENOM; P53501; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-005717-MON; -. DR NextBio; 803303; -. DR GermOnline; CG10067; Drosophila melanogaster. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0015020; F:glucuronosyltransferase activity; NAS:FlyBase. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; NAS:FlyBase. DR GO; GO:0000910; P:cytokinesis; IMP:FlyBase. DR GO; GO:0007507; P:heart development; NAS:FlyBase. DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic p...; NAS:FlyBase. DR GO; GO:0051533; P:positive regulation of NFAT protein import ...; IMP:FlyBase. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 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 3: Inferred from homology; KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; KW Nucleotide-binding. FT PROPEP 1 2 Removed in mature form (By similarity). FT /FTId=PRO_0000000660. FT CHAIN 3 376 Actin-57B. FT /FTId=PRO_0000000661. FT MOD_RES 3 3 N-acetylaspartate (By similarity). 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 //