ID   ACT1_BACDO              Reviewed;         376 AA.
AC   P83969; 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 63.
DE   RecName: Full=Actin, indirect flight muscle;
DE   Flags: Precursor;
OS   Bactrocera dorsalis (Oriental fruit fly) (Dacus dorsalis).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Bactrocera; Bactrocera.
OX   NCBI_TaxID=27457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Puna;
RX   PubMed=7951267; DOI=10.1016/0965-1748(94)90018-3;
RA   He M., Haymer D.S.;
RT   "The actin gene family in the oriental fruit fly Bactrocera dorsalis.
RT   Muscle specific actins.";
RL   Insect Biochem. Mol. Biol. 24:891-906(1994).
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 to form methionine sulfoxide promotes actin
CC       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   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; L12253; AAA62341.1; -; Genomic_DNA.
DR   RefSeq; XP_011208262.1; XM_011209960.1.
DR   AlphaFoldDB; P83969; -.
DR   SMR; P83969; -.
DR   GeneID; 105229580; -.
DR   Proteomes; UP000504616; Unplaced.
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   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_0000000666"
FT   CHAIN           3..376
FT                   /note="Actin, indirect flight muscle"
FT                   /id="PRO_0000000667"
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