ACT2_DROME
ID ACT2_DROME Reviewed; 376 AA.
AC P02572; Q24228; Q540X3; Q9V9J4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Actin-42A;
DE Flags: Precursor;
GN Name=Act42A; ORFNames=CG12051;
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 (DEC-1987) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RA Burn T.C., Tobin S.L.;
RL Submitted (OCT-1990) 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160 AND 229-376.
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 1-12.
RX PubMed=2436146; DOI=10.1093/nar/15.6.2549;
RA Couderc J.-L., Hilal L., Sobier M.L., Dastugue B.;
RT "20-hydroxyecdysone regulates cytoplasmic actin gene expression in
RT Drosophila cultured cells.";
RL Nucleic Acids Res. 15:2549-2561(1987).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=1694472; DOI=10.1002/dvg.1020110104;
RA Tobin S.L., Cook P.J., Burn T.C.;
RT "Transcripts of individual Drosophila actin genes are differentially
RT distributed during embryogenesis.";
RL Dev. Genet. 11:15-26(1990).
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).
RN [10]
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 -!- INTERACTION:
CC P02572; P02574: Act79B; NbExp=4; IntAct=EBI-110368, EBI-178503;
CC P02572; P83967: Act88F; NbExp=4; IntAct=EBI-110368, EBI-184828;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: All cells and tissues of the developing embryo.
CC Later in development, expression is higher in midgut, brain, nerve
CC cord, and gonads. {ECO:0000269|PubMed:1694472}.
CC -!- INDUCTION: By 20-hydroxyecdysone.
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; K00670; AAA28314.1; -; Genomic_DNA.
DR EMBL; X54848; CAA38618.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57294.1; -; Genomic_DNA.
DR EMBL; AY118907; AAM50767.1; -; mRNA.
DR EMBL; X05176; CAA28809.1; -; Genomic_DNA.
DR PIR; A03000; A03000.
DR PIR; S14851; S14851.
DR RefSeq; NP_523625.1; NM_078901.3.
DR AlphaFoldDB; P02572; -.
DR SMR; P02572; -.
DR BioGRID; 61432; 23.
DR DIP; DIP-20355N; -.
DR IntAct; P02572; 12.
DR STRING; 7227.FBpp0085365; -.
DR PaxDb; P02572; -.
DR PRIDE; P02572; -.
DR DNASU; 35526; -.
DR EnsemblMetazoa; FBtr0086029; FBpp0085365; FBgn0000043.
DR GeneID; 35526; -.
DR KEGG; dme:Dmel_CG12051; -.
DR CTD; 35526; -.
DR FlyBase; FBgn0000043; Act42A.
DR VEuPathDB; VectorBase:FBgn0000043; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P02572; -.
DR OMA; FHTTAER; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P02572; -.
DR SignaLink; P02572; -.
DR BioGRID-ORCS; 35526; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 35526; -.
DR PRO; PR:P02572; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0000043; Expressed in embryonic/larval hemocyte (Drosophila) and 27 other tissues.
DR Genevisible; P02572; DM.
DR GO; GO:0035060; C:brahma complex; IDA:FlyBase.
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 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 Nucleotide-binding; Oxidation; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000658"
FT CHAIN 3..376
FT /note="Actin-42A"
FT /id="PRO_0000000659"
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"
FT CONFLICT 12..287
FT /note="Missing (in Ref. 2; CAA38618)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="I -> L (in Ref. 1; AAA28314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41824 MW; 7C6D13CC6E42331E CRC64;
MCDEEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS
YELPDGQVIT IGNERFRCPE SLFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI VAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPSI VHRKCF
