ACT6_DROME
ID ACT6_DROME Reviewed; 376 AA.
AC P83967; P02575; P45893; Q9VF62;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Actin, indirect flight muscle;
DE AltName: Full=Actin-88F;
DE Flags: Precursor;
GN Name=Act88F; ORFNames=CG5178;
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].
RA Fyrberg E.A., Bond B.J., Hershey N.D., Mixter K.S., Davidson N.;
RL Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Okamoto H., Hiromi Y., Ishikawa E., Yamada T., Isoda K., Maekawa H.,
RA Hotta Y.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 302-376, FUNCTION, AND MUTAGENESIS OF
RP 357-TRP--PHE-376.
RX PubMed=6488317; DOI=10.1016/0092-8674(84)90266-6;
RA Karlik C.C., Coutu M.D., Fyrberg E.A.;
RT "A nonsense mutation within the act88F actin gene disrupts myofibril
RT formation in Drosophila indirect flight muscles.";
RL Cell 38:711-719(1984).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17353360; DOI=10.1083/jcb.200610053;
RA Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K.,
RA Matera A.G.;
RT "A Drosophila melanogaster model of spinal muscular atrophy reveals a
RT function for SMN in striated muscle.";
RL J. Cell Biol. 176:831-841(2007).
RN [9]
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. Required for proper formation of indirect flight
CC muscle (IFM) myofibrils.
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 P83967; P02572: Act42A; NbExp=4; IntAct=EBI-184828, EBI-110368;
CC P83967; Q9VPX6: capt; NbExp=4; IntAct=EBI-184828, EBI-15115807;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: In adult thorax, expressed in the IFMs.
CC {ECO:0000269|PubMed:17353360}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Expression is
CC weak during embryonic stages and peaks during larval and pupal stages.
CC {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 -!- DISRUPTION PHENOTYPE: Homozygous mutants are viable and fertile, but
CC fail to form proper IFMs and are flightless. The IFMs of these mutants
CC display mislocalized Smn and Actn. {ECO:0000269|PubMed:17353360}.
CC -!- MISCELLANEOUS: Abnormalities in Act88F-ifm(3)7 flight muscles result
CC from incorporation of the mutant actin isoform into assembling
CC myofibrils.
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; M18826; AAA28323.1; -; Genomic_DNA.
DR EMBL; K02065; AAA28322.1; -; Genomic_DNA.
DR EMBL; AB003910; BAA20058.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55198.1; -; Genomic_DNA.
DR EMBL; M18830; AAA28321.1; -; Genomic_DNA.
DR PIR; A03003; ATFF8.
DR RefSeq; NP_524367.1; NM_079643.2.
DR AlphaFoldDB; P83967; -.
DR SMR; P83967; -.
DR BioGRID; 66947; 27.
DR IntAct; P83967; 13.
DR STRING; 7227.FBpp0082597; -.
DR SwissPalm; P83967; -.
DR PaxDb; P83967; -.
DR PRIDE; P83967; -.
DR DNASU; 41885; -.
DR EnsemblMetazoa; FBtr0083143; FBpp0082597; FBgn0000047.
DR GeneID; 41885; -.
DR KEGG; dme:Dmel_CG5178; -.
DR CTD; 41885; -.
DR FlyBase; FBgn0000047; Act88F.
DR VEuPathDB; VectorBase:FBgn0000047; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000166560; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P83967; -.
DR OMA; THNTIHA; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P83967; -.
DR SignaLink; P83967; -.
DR BioGRID-ORCS; 41885; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Act88F; fly.
DR GenomeRNAi; 41885; -.
DR PRO; PR:P83967; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000047; Expressed in second segment of antenna (Drosophila) and 15 other tissues.
DR ExpressionAtlas; P83967; baseline and differential.
DR Genevisible; P83967; DM.
DR GO; GO:0030016; C:myofibril; IDA:FlyBase.
DR GO; GO:0005865; C:striated muscle thin filament; HDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0071689; P:muscle thin filament assembly; IMP:FlyBase.
DR GO; GO:0014866; P:skeletal myofibril assembly; IMP:FlyBase.
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_0000000668"
FT CHAIN 3..376
FT /note="Actin, indirect flight muscle"
FT /id="PRO_0000000669"
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 MUTAGEN 357..376
FT /note="Missing: In allele Act88F-ifm(3)7."
FT /evidence="ECO:0000269|PubMed:6488317"
FT CONFLICT 200
FT /note="S -> T (in Ref. 2; AAA28321)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="I -> T (in Ref. 2; AAA28321)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="Q -> D (in Ref. 2; AAA28321)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="A -> T (in Ref. 2; AAA28321)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="S -> L (in Ref. 2; AAA28321)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="G -> S (in Ref. 2; AAA28321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41700 MW; C64C33A1674B7886 CRC64;
MCDDDAGALV IDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGF ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS
YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANSVL
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPGI VHRKCF
