ID   ACT3_BOMMO              Reviewed;         376 AA.
AC   P04829; P90694;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Actin, cytoplasmic A3;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic A3, intermediate form;
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=European 200 X 300;
RX   PubMed=3096383; DOI=10.1016/s0300-9084(86)80179-1;
RA   Mounier N., Prudhomme J.-C.;
RT   "Isolation of actin genes in Bombyx mori: the coding sequence of a
RT   cytoplasmic actin gene expressed in the silk gland is interrupted by a
RT   single intron in an unusual position.";
RL   Biochimie 68:1053-1061(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=European 200 X 300;
RX   PubMed=9018041; DOI=10.1006/jmbi.1996.0734;
RA   Mange A., Julien E., Prudhomme J.-C., Couble P.;
RT   "A strong inhibitory element down-regulates SRE-stimulated transcription of
RT   the A3 cytoplasmic actin gene of Bombyx mori.";
RL   J. Mol. Biol. 265:266-274(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.
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 and Met-48 by MICALs (MICAL1, MICAL2 or
CC       MICAL3) to form methionine sulfoxide promotes actin filament
CC       depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The
CC       (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin
CC       repolymerization. {ECO:0000250|UniProtKB:P68033}.
CC   -!- PTM: Monomethylation at Lys-85 (K85me1) regulates actin-myosin
CC       interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC       is required for maintaining actomyosin dynamics supporting normal
CC       cleavage furrow ingression during cytokinesis and cell migration.
CC       {ECO:0000250|UniProtKB:P68032}.
CC   -!- MISCELLANEOUS: There are at least 5 different actin genes in this
CC       organism.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; X04507; CAA28192.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U49854; AAC47446.1; -; Genomic_DNA.
DR   PIR; A25135; A25135.
DR   RefSeq; NP_001119726.1; NM_001126254.1.
DR   AlphaFoldDB; P04829; -.
DR   SMR; P04829; -.
DR   GeneID; 100145915; -.
DR   KEGG; bmor:100145915; -.
DR   CTD; 5657641; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   OrthoDB; 649708at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
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   Nucleotide-binding; Oxidation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..376
FT                   /note="Actin, cytoplasmic A3, intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT                   /id="PRO_0000443010"
FT   CHAIN           3..376
FT                   /note="Actin, cytoplasmic A3"
FT                   /evidence="ECO:0000250|UniProtKB:P68135"
FT                   /id="PRO_0000000637"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine; in intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate; in Actin, cytoplasmic A3"
FT                   /evidence="ECO:0000250|UniProtKB:P68135"
FT   MOD_RES         45
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P68033"
FT   MOD_RES         48
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P68033"
FT   MOD_RES         74
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P62739"
FT   MOD_RES         85
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68032"
FT   CONFLICT        44
FT                   /note="V -> L (in Ref. 1; CAA28192)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  41918 MW;  DE5B8DAB652BF2B6 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 ADRMQKEITR LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF