ID   ACT_MAYDE               Reviewed;         376 AA.
AC   O16808;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Actin;
DE   Flags: Precursor;
OS   Mayetiola destructor (Hessian fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Sciaroidea; Cecidomyiidae;
OC   Mayetiola.
OX   NCBI_TaxID=39758;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Russell V.W., Shukle R.H.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; AF017427; AAB70258.1; -; mRNA.
DR   AlphaFoldDB; O16808; -.
DR   SMR; O16808; -.
DR   EnsemblMetazoa; Mdes016052-RA; Mdes016052-RA:cds; Mdes016052.
DR   OrthoDB; 649708at2759; -.
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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Oxidation.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000700"
FT   CHAIN           3..376
FT                   /note="Actin"
FT                   /id="PRO_0000000701"
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"
SQ   SEQUENCE   376 AA;  41817 MW;  FB47CC33F3C8CAAC CRC64;
     MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNA PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLSYV ALDFEQEMAT AAASTSLEKS
     YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANIVM
     SGGTTMYPGI ADRMQKEITS LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     EEYDESGPGI VHRKCF