ACT4_DROME
ID ACT4_DROME Reviewed; 376 AA.
AC P02574; Q540X7; Q9VNW5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Actin, larval muscle;
DE AltName: Full=Actin-79B;
DE Flags: Precursor;
GN Name=Act79B; ORFNames=CG7478;
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], AND DEVELOPMENTAL STAGE.
RX PubMed=6405041; DOI=10.1016/0022-2836(83)90111-0;
RA Sanchez F., Tobin S.L., Rdest U., Zulauf E., McCarthy B.J.;
RT "Two Drosophila actin genes in detail. Gene structure, protein structure
RT and transcription during development.";
RL J. Mol. Biol. 163:533-551(1983).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [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).
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 -!- INTERACTION:
CC P02574; P02572: Act42A; NbExp=4; IntAct=EBI-178503, EBI-110368;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- DEVELOPMENTAL STAGE: Expressed during larval stages and at a lower
CC level in pupae. {ECO:0000269|PubMed:6405041}.
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}.
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DR EMBL; M18827; AAA28317.1; -; Genomic_DNA.
DR EMBL; M18828; AAA28317.1; JOINED; Genomic_DNA.
DR EMBL; M18829; AAA28318.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51800.1; -; Genomic_DNA.
DR EMBL; AY118735; AAM50595.1; -; mRNA.
DR PIR; A03002; ATFF7.
DR RefSeq; NP_001262200.1; NM_001275271.1.
DR RefSeq; NP_524210.1; NM_079486.4.
DR AlphaFoldDB; P02574; -.
DR SMR; P02574; -.
DR BioGRID; 65684; 37.
DR DIP; DIP-23587N; -.
DR IntAct; P02574; 6.
DR STRING; 7227.FBpp0078131; -.
DR PaxDb; P02574; -.
DR PRIDE; P02574; -.
DR DNASU; 40444; -.
DR EnsemblMetazoa; FBtr0078478; FBpp0078131; FBgn0000045.
DR EnsemblMetazoa; FBtr0334090; FBpp0306215; FBgn0000045.
DR GeneID; 40444; -.
DR KEGG; dme:Dmel_CG7478; -.
DR CTD; 40444; -.
DR FlyBase; FBgn0000045; Act79B.
DR VEuPathDB; VectorBase:FBgn0000045; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000175284; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P02574; -.
DR OMA; ERFCASE; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P02574; -.
DR SignaLink; P02574; -.
DR BioGRID-ORCS; 40444; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Act79B; fly.
DR GenomeRNAi; 40444; -.
DR PRO; PR:P02574; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000045; Expressed in adult organism and 18 other tissues.
DR ExpressionAtlas; P02574; baseline and differential.
DR Genevisible; P02574; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Muscle protein; Nucleotide-binding; Oxidation; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000662"
FT CHAIN 3..376
FT /note="Actin, larval muscle"
FT /id="PRO_0000000663"
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:0000250|UniProtKB:P02572"
FT CONFLICT 185
FT /note="D -> H (in Ref. 1; AAA28318)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="I -> M (in Ref. 1; AAA28317/AAA28318)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41787 MW; D08BB1B42DE86B94 CRC64;
MCDEEASALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDCYVGDEAQ
SKRGILSLKY PIEHGIITNW DDMEKVWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS
YELPDGQVIT IGNERFRTPE ALFQPSFLGM ESCGIHETVY QSIMKCDVDI RKDLYANNVL
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPGI VHRKCF
