ACT3A_HELAM
ID ACT3A_HELAM Reviewed; 376 AA.
AC Q25010;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Actin, cytoplasmic A3a;
DE Flags: Precursor;
GN Name=actA3a;
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 and Met-48 to form methionine sulfoxide
CC promotes actin filament depolymerization. Methionine sulfoxide is
CC produced stereospecifically, but it is not known whether the (S)-S-
CC oxide or the (R)-S-oxide is produced. {ECO:0000250|UniProtKB:P62737}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; X97614; CAA66218.1; -; Genomic_DNA.
DR AlphaFoldDB; Q25010; -.
DR SMR; Q25010; -.
DR PRIDE; Q25010; -.
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_0000000672"
FT CHAIN 3..376
FT /note="Actin, cytoplasmic A3a"
FT /id="PRO_0000000673"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 48
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P62737"
SQ SEQUENCE 376 AA; 41833 MW; CD488DB8762BF2B6 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 EANGIHETTY NSIMKCDVDI RKDLYANTVL
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
QEYDESGPSI VHRKCF
