ID   ACT6_DROSI              Reviewed;         376 AA.
AC   P83968; B4QYG8; P02575; P45893; Q9VF62;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Actin, indirect flight muscle;
DE   AltName: Full=Actin-88F;
DE   Flags: Precursor;
GN   Name=Act88F; ORFNames=GD19025;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1511890; DOI=10.1016/0378-1119(92)90185-r;
RA   Beifuss M.J., Durica D.S.;
RT   "Sequence analysis of the indirect flight muscle actin-encoding gene of
RT   Drosophila simulans.";
RL   Gene 118:163-170(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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 (By similarity). {ECO:0000250}.
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; M87274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CM000364; EDX12813.1; -; Genomic_DNA.
DR   PIR; JC1246; JC1246.
DR   RefSeq; XP_016034553.1; XM_016175375.1.
DR   AlphaFoldDB; P83968; -.
DR   SMR; P83968; -.
DR   STRING; 7240.P83968; -.
DR   EnsemblMetazoa; FBtr0218935; FBpp0217427; FBgn0012823.
DR   GeneID; 6727955; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   OMA; THNTIHA; -.
DR   PhylomeDB; P83968; -.
DR   ChiTaRS; Act88F; fly.
DR   Proteomes; UP000000304; Chromosome 3r.
DR   Bgee; FBgn0012823; Expressed in adult organism and 2 other tissues.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0071689; P:muscle thin filament assembly; IEA:EnsemblMetazoa.
DR   GO; GO:0014866; P:skeletal myofibril assembly; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
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_0000000670"
FT   CHAIN           3..376
FT                   /note="Actin, indirect flight muscle"
FT                   /id="PRO_0000000671"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         45
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         48
FT                   /note="Methionine sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         74
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P02572"
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