ID   ACT3B_HELAM             Reviewed;         376 AA.
AC   P84184; O02508; Q27250;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Actin-A3b, cytoplasmic;
DE   Flags: Precursor;
GN   Name=actA3b;
OS   Helicoverpa armigera (Cotton bollworm) (Heliothis armigera).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Helicoverpa.
OX   NCBI_TaxID=29058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=AN; TISSUE=Egg;
RX   PubMed=9069177; DOI=10.1007/pl00006133;
RA   Rourke I.J., East P.D.;
RT   "Evidence for gene conversion between tandemly duplicated cytoplasmic actin
RT   genes of Helicoverpa armigera (Lepidoptera: Noctuidae).";
RL   J. Mol. Evol. 44:169-177(1997).
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. Multiple isoforms are involved in various cellular
CC       functions such as cytoskeleton structure, cell mobility, chromosome
CC       movement and muscle contraction.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Brain of newly enclosed adults.
CC       {ECO:0000269|PubMed:9069177}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during pupal development and in adults.
CC       {ECO:0000269|PubMed:9069177}.
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; X97615; CAA66219.1; -; Genomic_DNA.
DR   AlphaFoldDB; P84184; -.
DR   SMR; P84184; -.
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_0000000674"
FT   CHAIN           3..376
FT                   /note="Actin-A3b, cytoplasmic"
FT                   /id="PRO_0000000675"
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;  41822 MW;  BDAF13C191BB1BBC 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 ALFQPSFLGM EACGIHETTY NSIMKCDVDI RKDLYANTVL
     SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF