ID   ACT2_BOMMO              Reviewed;         376 AA.
AC   P07837;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Actin, muscle-type A2;
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=703;
RX   PubMed=3562238; DOI=10.1093/nar/15.6.2781;
RA   Mounier N., Gaillard J., Prudhomme J.-C.;
RT   "Nucleotide sequence of the coding region of two actin genes in Bombyx
RT   mori.";
RL   Nucleic Acids Res. 15:2781-2781(1987).
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   -!- 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; X06363; CAA29661.1; -; Genomic_DNA.
DR   PIR; S07382; S07382.
DR   RefSeq; NP_001119725.1; NM_001126253.1.
DR   AlphaFoldDB; P07837; -.
DR   SMR; P07837; -.
DR   PRIDE; P07837; -.
DR   GeneID; 100145914; -.
DR   KEGG; bmor:100145914; -.
DR   CTD; 100145914; -.
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; Nucleotide-binding;
KW   Oxidation; Reference proteome.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000634"
FT   CHAIN           3..376
FT                   /note="Actin, muscle-type A2"
FT                   /id="PRO_0000000635"
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;  41803 MW;  E3E72BBEE0B4846B CRC64;
     MCDDDAGALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPILLTEAP LNPKANREKM
     TQIMFETFNC PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMQT AAASTSLEKS
     YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANTVL
     SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPGI VHRKCF